Cited by 1,022Enzyme function and inhibitionPhysical Organic Chemistry and Reaction KineticsEnzyme Structure and Function

The DOI matches its Crossref record; 206 of the 212 references it cites were found in a registry or an index.

Structure and mechanism of carbonic anhydrase

Lindskog, Sven·1997·Pharmacology & Therapeutics

DOI 10.1016/s0163-7258(96)00198-2

Open this paper in CoChat — free account

Abstract

Carbonic anhydrase (CA; carbonate hydro-lyase, EC 4.2.1.1) is a zinc-containing enzyme that catalyzes the reversible hydration of carbon dioxide: CO2+ H2O<-->HCO3(-)+H+. The enzyme is the target for drugs, such as acetazolamide, methazolamide, and dichlorphenamide, for the treatment of glaucoma. There are three evolutionarily unrelated CA families, designated alpha, beta, and gamma. All known CAs from the animal kingdom are of the alpha type. There are seven mammalian CA isozymes with different tissue distributions and intracellular locations, CA I-VII. Crystal structures of human CA I and II, bovine CA III, and murine CA V have been determined. All of them have the same tertiary fold, with a central 10-stranded beta-sheet as the dominating secondary structure element. The zinc ion is located in a cone-shaped cavity and coordinated to three histidyl residues and a solvent molecule. Inhibitors bind at or near the metal center guided by a hydrogen-bonded system comprising Glu-106 and Thr-199. The catalytic mechanism of CA II has been studied in particular detail. It involves an attack of zinc-bound OH- on a CO2 molecule loosely bound in a hydrophobic pocket. The resulting zinc-coordinated HCO3- ion is displaced from the metal ion by H2O. The rate-limiting step is an intramolecular proton transfer from the zinc-bound water molecule to His-64, which serves as a proton shuttle between the metal center and buffer molecules in the reaction medium.

Integrity signals

Registry

Crossref · 10.1016/s0163-7258(96)00198-2

Cites

206 of 206 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011
The Carbon Dioxide Hydration Activity of Carbonic Anhydrase
Khalifah, R. G. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62326-9 · Cited by 1,916
Carbonic anhydrase: chemistry, physiology, and inhibition
Maren, T. H. (1967) · Physiological Reviews · doi:10.1152/physrev.1967.47.4.595 · Cited by 1,895
HUMAN CARBONIC ANHYDRASES AND CARBONIC ANHYDRASE DEFICIENCIES
Sly, W. S., & Hu, P. Y. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.002111 · Cited by 833
The Role of Carbonic Anhydrase in Photosynthesis
Badger, M. R., & Price, G. D. (1994) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.pp.45.060194.002101 · Cited by 818
The catalytic mechanism of carbonic anhydrase: implications of a rate-limiting protolysis of water
Silverman, D. N., & Lindskog, S. F. (1988) · Accounts of Chemical Research · doi:10.1021/ar00145a005 · Cited by 749
Self-citation
Carbonic anhydrase II deficiency identified as the primary defect in the autosomal recessive syndrome of osteopetrosis with renal tubular acidosis and cerebral calcification.
Sly, W. S., Hewett‐Emmett, D., Whyte, M. P., Yu, Y. S., & Tashian, R. E. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.9.2752 · Cited by 623
Functional Diversity, Conservation, and Convergence in the Evolution of the α-, β-, and γ-Carbonic Anhydrase Gene Families
Hewett‐Emmett, D., & Tashian, R. E. (1996) · Molecular Phylogenetics and Evolution · doi:10.1006/mpev.1996.0006 · Cited by 616
Refined structure of human carbonic anhydrase II at 2.0 Å resolution
Sauer-Eriksson, A. E., Jones, T. A., & Liljas, A. (1988) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340040406 · Cited by 550
Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes
Håkansson, K., Carlsson, M., Svensson, L. A., & Liljas, A. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90531-n · Cited by 512
Cloning and characterization of MN, a human tumor-associated protein with a domain homologous to carbonic anhydrase and a putative helix-loop-helix DNA binding segment.
Pastorek, J., Pastoreková, S., Callebaut, I., Mornon, J., Zelnı́k, V., Opavský, R., Zaťovičová, M., Liao, S., Portetelle, D., & Stanbridge, E. J. (1994) · PubMed · Cited by 509
Crystal Structure of Human Carbonic Anhydrase C
Liljas, A., Kannan, K. K., Bergstén, P.-C., Vaara, I., Fridborg, K., Strandberg, B., Carlbom, U., Järup, L., Lövgren, S., & Petef, M. (1972) · Nature New Biology · doi:10.1038/newbio235131a0 · Cited by 452
The Catalytic Mechanism of Carbonic Anhydrase. Hydrogen-Isotope Effects on the Kinetic Parameters of the Human C Isoenzyme
Steiner, H., Jonsson, B., & Lindskog, S. F. (1975) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1975.tb02449.x · Cited by 426
Self-citation
The carbonic anhydrase domain of receptor tyrosine phosphatase β is a functional ligand for the axonal cell recognition molecule contactin
Peles, E., Nativ, M., Campbell, P. L., Sakurai, T., Martinez, R., Lev, S., Clary, D. O., Schilling, J., Barnea, G., Plowman, G. D., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90312-7 · Cited by 397
HumanMN/CA9Gene, a Novel Member of the Carbonic Anhydrase Family: Structure and Exon to Protein Domain Relationships
Opavský, R., Pastoreková, S., Zelnı́k, V., Gibadulinová, A., Stanbridge, E. J., Závada, J., Kettmann, R., & Pastorek, J. (1996) · Genomics · doi:10.1006/geno.1996.0223 · Cited by 383
Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant
Tu, C., Silverman, D. N., Forsman, C., Jonsson, B. H., & Lindskog, S. (1989) · Biochemistry · doi:10.1021/bi00445a054 · Cited by 376
Self-citation
Multiple Roles of Carbonic Anhydrase in Cellular Transport and Metabolism
Henry, R. P. (1996) · Annual Review of Physiology · doi:10.1146/annurev.ph.58.030196.002515 · Cited by 323
The Catalytic Mechanism of Carbonic Anhydrase
Lindskog, S. F., & Coleman, J. E. (1973) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.70.9.2505 · Cited by 316
Self-citation
A left‐hand beta‐helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila.
Kisker, C., Schindelin, H., Alber, B. E., Ferry, J. G., & Rees, D. C. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00588.x · Cited by 261
Metal Binding and Catalytic Activity in Bovine Carbonic Anhydrase
Lindskog, S. F., & Malmström, B. G. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60295-9 · Cited by 260
Self-citation
A carbonic anhydrase from the archaeon Methanosarcina thermophila.
Alber, B. E., & Ferry, J. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.6909 · Cited by 253
The Carbonic anhydrases : cellular physiology and molecular genetics
Dodgson, S. J., Tashian, R. E., Gros, G., & Carter, N. D. (1991) · Plenum Press eBooks · Cited by 252
Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution.
Kannan, K. K., Notstrand, B., Fridborg, K., Lövgren, S., Ohlsson, Å., & Petef, M. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.1.51 · Cited by 247
21 Carbonic Anhydrase
Lindskog, S., Henderson, L. E., Kannan, K. K., Liljas, A., Nyman, P. O., & Strandberg, B. (1971) · The Enzymes · doi:10.1016/s1874-6047(08)60104-3 · Cited by 232
Self-citation
The cloning of a receptor-type protein tyrosine phosphatase expressed in the central nervous system
Levy, J. B., Canoll, P., Silvennoinen, O., Barnea, G., Morse, B., Honegger, A., Huang, J., Cannizzaro, L. A., Park, S., & Druck, T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82237-2 · Cited by 229
Metal-binding properties of human erythrocyte carbonic anhydrases
Lindskog, S. F., & Nyman, P. O. (1964) · Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects · doi:10.1016/0926-6569(64)90310-4 · Cited by 228
Self-citation
A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases.
Krueger, N. X., & Saito, H. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7417 · Cited by 221
A gene homologous to chloroplast carbonic anhydrase (icfA) is essential to photosynthetic carbon dioxide fixation by Synechococcus PCC7942.
Fukuzawa, H., Suzuki, E., Komukai, Y., & Miyachi, S. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.10.4437 · Cited by 213
cDNA cloning, sequence, and expression of carbonic anhydrase in Chlamydomonas reinhardtii: regulation by environmental CO2 concentration.
Fukuzawa, H., Fujiwara, S., Yamamoto, Y., Dionisio‐Sese, M. L., & Miyachi, S. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.11.4383 · Cited by 208
Unexpected pH-dependent conformation of His-64, the proton shuttle of carbonic anhydrase II
Nair, S. K., & Christianson, D. W. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00025a005 · Cited by 198
Thienothiopyran-2-sulfonamides: novel topically active carbonic anhydrase inhibitors for the treatment of glaucoma
Baldwin, J. J., Ponticello, G. S., Anderson, P., Christy, M. E., Murcko, M. A., Randall, W. C., Schwam, H., Sugrue, M. F., & Gautheron, P. (1989) · Journal of Medicinal Chemistry · doi:10.1021/jm00132a003 · Cited by 197
Two-Site Binding of Phenol in the Active Site of Human Carbonic Anhydrase II: Structural Implications for Substrate Association
Nair, S. K., Ludwig, P. A., & Christianson, D. W. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00087a086 · Cited by 189
Hydrogen bond network in the metal binding site of carbonic anhydrase enhances zinc affinity and catalytic efficiency
Kiefer, L. L., Paterno, S. A., & Fierke, C. A. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00131a004 · Cited by 181
Discovery of an algal mitochondrial carbonic anhydrase: molecular cloning and characterization of a low-CO2-induced polypeptide in Chlamydomonas reinhardtii.
Eriksson, M., Karlsson, J. E., Ramazanov, Z., Gardeström, P., & Samuelsson, G. S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.12031 · Cited by 178
Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: A pentacoordinated binding of the SCN− ion to the zinc at high pH
Sauer-Eriksson, A. E., Kylsten, P. M., Jones, T. A., & Liljas, A. (1988) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340040407 · Cited by 177
Advances in Inorganic Biochemistry
Eichhorn, G. L., & Marzilli, L. G. (1994) · Medical Entomology and Zoology · Cited by 175
Drug-Protein Interactions
Chakravarty, S., & Kannan, K. K. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1655 · Cited by 173
Purification and characterization of human salivary carbonic anhydrase.
Murakami, H., & Sly, W. S. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75797-4 · Cited by 172
Carbon dioxide binding to human carbonic anhydrase II
Merz, K. M. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00002a004 · Cited by 154
Design of enzyme inhibitors as drugs
(1990) · International Journal of Biochemistry · doi:10.1016/0020-711x(90)90152-s · Cited by 152
The phosphatase activity of carbonic anhydrase III is reversibly regulated by glutathiolation.
Cabiscol, E., & Levine, R. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4170 · Cited by 148
A 13C Nuclear‐Magnetic‐Resonance Study of CO2‐HCO3− Exchange Catalyzed by Human Carbonic Anhydrase C at Chemical Equilibrium
Simonsson, I., Jonsson, B., & Lindskog, S. F. (1979) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1979.tb12837.x · Cited by 146
Self-citation
Mitochondrial carbonic anhydrase.
Dodgson, S. J., Forster, R. E., Storey, B. T., & Mela, L. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.9.5562 · Cited by 144
Carbonic Anhydrase: Structure, Catalytic Versatility, and Inhibition
Pocker, Y., & Sarkanen, S. (1979) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122921.ch3 · Cited by 140
Inhibition and catalysis of carbonic anhydrase
Liljas, A., HÅKANSSON, K., JONSSON, B. H., & Xue, Y. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb19909.x · Cited by 140
Characterization of cobalt(II) bovine carbonic anhydrase and of its derivatives
Bertini, I., Canti, G., Luchinat, C., & Scozzafava, A. (1978) · Journal of the American Chemical Society · doi:10.1021/ja00483a038 · Cited by 138
Functional consequences of engineering the hydrophobic pocket of carbonic anhydrase II
Fierke, C. A., Calderone, T. L., & Krebs, J. (1991) · Biochemistry · doi:10.1021/bi00110a007 · Cited by 134
A rapid and convenient preparation of apocarbonic anhydrase
Hunt, J. B., Rhee, M.-J., & Storm, C. B. (1977) · Analytical Biochemistry · doi:10.1016/0003-2697(77)90444-4 · Cited by 133
Cobalt(II) as a probe of the structure and function of carbonic anhydrase
Bertini, I., & Luchinat, C. (1983) · Accounts of Chemical Research · doi:10.1021/ar00092a002 · Cited by 132
Carbonic anhydrase in Escherichia coli. A product of the cyn operon.
Guilloton, M., Korte, J. J., Lamblin, A. F., Fuchs, J. A., & Anderson, P. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50586-5 · Cited by 130
Primary structure of human carbonic anhydrase C.
Henderson, L. E., Henriksson, D., & Nyman, P. O. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33081-8 · Cited by 128
Genetics of the Mammalian Carbonic Anhydrases
Tashian, R. E. (1992) · Advances in genetics · doi:10.1016/s0065-2660(08)60323-5 · Cited by 128
Amino acid sequence of human erythrocyte carbonic anhydrase B
Andersson, B., Nyman, P. O., & Strid, L. (1972) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(72)90400-7 · Cited by 126
Binding of substrate CO2 to the active site of human carbonic anhydrase II: a molecular dynamics study.
Liang, J. Y., & Lipscomb, W. N. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.10.3675 · Cited by 125
Amino acid sequence of human erythrocyte carbonic anhydrase C
Henderson, L. E., Henriksson, D., & Nyman, P. O. (1973) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(73)90655-4 · Cited by 124
Functional Characterization of Human Carbonic Anhydrase II Variants with Altered Zinc Binding Sites
Kiefer, L. L., & Fierke, C. A. (1994) · Biochemistry · doi:10.1021/bi00255a003 · Cited by 118
Participation of buffer in the catalytic mechanism of carbonic anhydrase
Jonsson, B.-H., Steiner, H., & Lindskog, S. (1976) · FEBS Letters · doi:10.1016/0014-5793(76)80317-1 · Cited by 117
Self-citation
The Development of Topical Carbonic Anhydrase Inhibitors
Maren, T. H. (1995) · Journal of Glaucoma · doi:10.1097/00061198-199502000-00012 · Cited by 117
Secondary Interactions Significantly Removed from the Sulfonamide Binding Pocket of Carbonic Anhydrase II Influence Inhibitor Binding Constants
Boriack, P. A., Christianson, D. W., Kingery-Wood, J. E., & Whitesides, G. M. (1995) · Journal of Medicinal Chemistry · doi:10.1021/jm00013a004 · Cited by 115
Molecular basis of human carbonic anhydrase II deficiency.
Roth, D. E., Venta, P. J., Tashian, R. E., & Sly, W. S. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.5.1804 · Cited by 113
Refined structure of bovine carbonic anhydrase III at 2.0 Å resolution
Sauer-Eriksson, A. E., & Liljas, A. (1993) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340160104 · Cited by 110
Structure and function of carbonic anhydrases
(1977) · FEBS Letters · doi:10.1016/0014-5793(77)80028-8 · Cited by 110
A new class of carbonic anhydrase inhibitor.
Maren, T. H., & Conroy, C. W. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74305-1 · Cited by 108
Rate of exchange of water from the active site of human carbonic anhydrase C
Silverman, D. N., Tu, C., LINDSKOG, S., & Wynns, G. C. (1979) · Journal of the American Chemical Society · doi:10.1021/ja00516a040 · Cited by 107
Self-citation
Role of hepatic carbonic anhydrase in de novo lipogenesis
Lynch, C. J., Fox, H. L., Hazen, S. A., Stanley, B. A., Dodgson, S. J., & LaNoue, K. F. (1995) · Biochemical Journal · doi:10.1042/bj3100197 · Cited by 106
X-ray crystallographic studies of engineered hydrogen bond networks in a protein-zinc binding site
Lesburg, C. A., & Christianson, D. W. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00131a005 · Cited by 106
Membrane-associated carbonic anhydrase from rat lung. Purification, characterization, tissue distribution, and comparison with carbonic anhydrase IVs of other mammals.
Waheed, A. A., Zhu, X. L., & Sly, W. S. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50732-3 · Cited by 104
Identification of Two Hydrophobic Patches in the Active-Site Cavity of Human Carbonic Anhydrase II by Solution-Phase and Solid-State Studies and Their Use in the Development of Tight-Binding Inhibitors
Jain, A., Whitesides, G. M., Alexander, R., & Christianson, D. W. (1994) · Journal of Medicinal Chemistry · doi:10.1021/jm00039a023 · Cited by 103
Intracellular Carbonic Anhydrase of Chlamydomonas reinhardtii
Karlsson, J. E., Hiltonen, T., Husic, H. D., Ramazanov, Z., & Samuelsson, G. S. (1995) · PLANT PHYSIOLOGY · doi:10.1104/pp.109.2.533 · Cited by 102
Structure determination of murine mitochondrial carbonic anhydrase V at 2.45-A resolution: implications for catalytic proton transfer and inhibitor design.
Boriack‐Sjodin, P. A., Heck, R. W., Laipis, P. J., Silverman, D. N., & Christianson, D. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.24.10949 · Cited by 101
The Complete Sequence, Expression in Escherichia Coli, Purification and Some Properties of Carbonic Anhydrase from Neisseria Gonorrhoeae
Chirică, L. C., Elleby, B., Jonsson, B., & Lindskog, S. F. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00755.x · Cited by 100
Self-citation
Refined structure of the acetazolamide complex of human carbonic anhydrase II at 1.9 Å
Vidgren, J., Liljas, A., & Walker, N. P. C. (1990) · International Journal of Biological Macromolecules · doi:10.1016/0141-8130(90)90040-h · Cited by 99
Fine tuning of the catalytic properties of carbonic anhydrase
Behravan, G., Jonsson, B., & LINDSKOG, S. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15582.x · Cited by 98
Self-citation
Importance of the conserved active‐site residues Try7, Glu106 and Thr199 for the catalytic function of human carbonic anhydrase II
LIANG, Z., Xue, Y., Behravan, G., Jonsson, B., & LINDSKOG, S. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17614.x · Cited by 98
Self-citation
A study of the histidine residues of human carbonic anhydrase C using 270 MHz proton magnetic resonance
Campbell, I. D., LINDSKOG, S., & White, A. I. (1975) · Journal of Molecular Biology · doi:10.1016/s0022-2836(75)80089-1 · Cited by 95
Self-citation
Reversal of the Hydrogen Bond to Zinc Ligand Histidine-119 Dramatically Diminishes Catalysis and Enhances Metal Equilibration Kinetics in Carbonic Anhydrase II
Huang, C.-C., Lesburg, C. A., Kiefer, L. L., Fierke, C. A., & Christianson, D. W. (1996) · Biochemistry · doi:10.1021/bi9526692 · Cited by 95
Crystallographic analysis of Thr‐200 → His human carbonic anhydrase II and its complex with the substrate, HCO
Xue, Y., Vidgren, J., Svensson, L. A., Liljas, A., Jonsson, B., & Lindskog, S. F. (1993) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340150110 · Cited by 94
Self-citation
Comparative distribution of carbonic anhydrase isozymes III and II in rodent tissues
Spicer, S. S., Ge, Z. H., Tashian, R. E., Hazen‐Martin, D. J., & Schulte, B. A. (1990) · American Journal of Anatomy · doi:10.1002/aja.1001870107 · Cited by 93
Carbonic anhydrase activity in skeletal muscle fiber types, axons, spindles, and capillaries of rat soleus and extensor digitorum longus muscles.
Riley, D. A., Ellis, S., & Bain, J. L. W. (1982) · Journal of Histochemistry & Cytochemistry · doi:10.1177/30.12.6218195 · Cited by 93
Spinach Carbonic Anhydrase: Investigation of the Zinc-Binding Ligands by Site-Directed Mutagenesis, Elemental Analysis, and Exafs
Bracey, M. H., Christiansen, J., Tovar, P., Cramer, S. P., & Bartlett, S. G. (1994) · Biochemistry · doi:10.1021/bi00248a023 · Cited by 92
Enhancement of the catalytic properties of human carbonic anhydrase III by site-directed mutagenesis
Jewell, D. A., Tu, C., Paranawithana, S. R., Tanhauser, S. M., LoGrasso, P. V., Laipis, P. J., & Silverman, D. N. (1991) · Biochemistry · doi:10.1021/bi00220a006 · Cited by 92
Sequence of a novel carbonic anhydrase‐related polypeptide and its exclusive presence in purkinje cells
Kato, K. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80390-5 · Cited by 91
The Interaction of Sulfate with Carbonic Anhydrase
Simonsson, I., & Lindskog, S. F. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb06494.x · Cited by 91
Self-citation
Structure of cobalt carbonic anhydrase complexed with bicarbonate
Håkansson, K., & Wehnert, A. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90327-g · Cited by 90
Differentiation‐dependent expression of CA V and the role of carbonic anhydrase isozymes in pyruvate carboxylation in adipocytes
Hazen, S. A., Waheed, A., Sly, W. S., LaNoue, K. F., & Lynch, C. J. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.4.8647347 · Cited by 89
Insights into the function of the zinc hydroxide-Thr199-Glu106 hydrogen bonding network in carbonic anhydrases
Merz, K. M. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90333-h · Cited by 89
Engineering the hydrophobic pocket of carbonic anhydrase II
Alexander, R., Nair, S. K., & Christianson, D. W. (1991) · Biochemistry · doi:10.1021/bi00110a008 · Cited by 88
Challenging times for bioinformatics
Casari, G., Andrade-Navarro, M. A., Peer Bork, B., Boyle, J., de Daruvar, A., Ouzounis, C. A., Schneider, R., Tamames, J., Valencia, A., & Sander, C. (1995) · Nature · doi:10.1038/376647a0 · Cited by 88
Spinach Chloroplastic Carbonic Anhydrase
Burnell, J. N., Gibbs, M. J., & Mason, J. G. (1990) · PLANT PHYSIOLOGY · doi:10.1104/pp.92.1.37 · Cited by 88
Human carbonic anhydrase IV: cDNA cloning, sequence comparison, and expression in COS cell membranes.
Okuyama, T., Sato, S., Zhu, X. L., Waheed, A., & Sly, W. S. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.4.1315 · Cited by 87
Spinach carbonic anhydrase primary structure deduced from the sequence of a cDNA clone.
Fawcett, T. W., Browse, J., Volokita, M., & Bartlett, S. G. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39375-5 · Cited by 86
Structural and functional importance of a conserved hydrogen bond network in human carbonic anhydrase II.
Krebs, J., Ippolito, J. A., Christianson, D. W., & Fierke, C. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74269-0 · Cited by 86
Kinetic and Structural Characterization of Spinach Carbonic Anhydrase
Rowlett, R. S., Chance, M. R., Wirt, M. D., Sidelinger, D. E., Royal, J. R., Woodroffe, M., Wang, Y.-F. A., Saha, R., & Lam, M. C. W. (1994) · Biochemistry · doi:10.1021/bi00251a003 · Cited by 85
A physiological role for cyanate-induced carbonic anhydrase in Escherichia coli
Guilloton, M., Lamblin, A. F., Kozliak, E. I., Gerami‐Nejad, M., Tu, C., Silverman, D. N., Anderson, P. M., & Fuchs, J. A. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.5.1443-1451.1993 · Cited by 83
Contribution of Individual Tryptophan Residues to the Fluorescence Spectrum of Native and Denatured Forms of Human Carbonic Anhydrase II
Maartensson, L.-G., Jonasson, P., Freskgaard, P.-O., Svensson, M., Carlsson, U., & Jonsson, B.-H. (1995) · Biochemistry · doi:10.1021/bi00003a036 · Cited by 83
The structure of human carbonic anhydrase II in complex with bromide and azide
Jonsson, B., Håkansson, K., & Liljas, A. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81565-h · Cited by 83
Kinetics of the protonation of buffer and hydration of carbon dioxide catalyzed by human carbonic anhydrase II
Rowlett, R. S., & Silverman, D. N. (1982) · Journal of the American Chemical Society · doi:10.1021/ja00388a043 · Cited by 83
Production of Active Human Carbonic Anhydrase II in E. Coli.
Forsman, C., Behravan, G., Osterman, A., Jonsson, B., Enzell, C. R., Berg, J.-E., Bartók, M., Pelczer, I., & Dombi, G. (1988) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.42b-0314 · Cited by 80
Nitrogen-15 nuclear magnetic resonance study of benzenesulfonamide and cyanate binding to carbonic anhydrase
Kanamori, K., & Roberts, J. D. (1983) · Biochemistry · doi:10.1021/bi00280a011 · Cited by 79
Design of enzyme inhibitors as drugs
Whiteley, J. M. (1989) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(89)90305-8 · Cited by 78
Rate-equilibria relationships in intramolecular proton transfer in human carbonic anhydrase III
Silverman, D. N., Tu, C., Chen, X., Tanhauser, S. M., Kresge, A. J., & Laipis, P. J. (1993) · Biochemistry · doi:10.1021/bi00091a029 · Cited by 77
Kinetic studies of pea carbonic anhydrase
Johansson, I., & Forsman, C. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18394.x · Cited by 76
X-Ray Crystallographic Studies of Engineered Hydrogen Bond Networks in a Protein-Zinc Binding Site
Lesburg, C. A., & Christianson, D. W. (1995) · Journal of the American Chemical Society · doi:10.2210/pdb1cng/pdb · Cited by 76
Increasing Binding Constants of Ligands to Carbonic Anhydrase by Using "Greasy Tails"
Gao, J., Qiao, S., & Whitesides, G. M. (1995) · Journal of Medicinal Chemistry · doi:10.1021/jm00013a005 · Cited by 76
A study of the histidine residues of human carbonic anhydrase B using 270 MHz proton magnetic resonance
Campbell, I. D., LINDSKOG, S., & White, A. I. (1974) · Journal of Molecular Biology · doi:10.1016/0022-2836(74)90229-0 · Cited by 76
Self-citation
The p-nitrophenyl phosphatase activity of muscle carbonic anhydrase
Koester, M. K., Pullan, L. M., & Noltmann, E. A. (1981) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(81)90499-9 · Cited by 74
Structural and functional characterization of a cell surface binding protein of vaccinia virus.
Maa, J. S., Rodrígúez, J. F., & Estéban, M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40055-0 · Cited by 72
Kinetic and spectroscopic studies of hydrophilic amino acid substitutions in the hydrophobic pocket of human carbonic anhydrase II
Krebs, J., Rana, F. R., Dluhy, R. A., & Fierke, C. A. (1993) · Biochemistry · doi:10.1021/bi00068a004 · Cited by 72
Conformational mobility of His-64 in the Thr-200 .fwdarw. Ser mutant of human carbonic anhydrase II
Krebs, J., Fierke, C. A., Alexander, R., & Christianson, D. W. (1991) · Biochemistry · doi:10.1021/bi00102a005 · Cited by 72
Characterization of the human gene for a newly discovered carbonic anhydrase, CA VII, and its localization to chromosome 16
Montgomery, J. C., Venta, P. J., Eddy, R. L., Fukushima, Y., Shows, T. B., & Tashian, R. E. (1991) · Genomics · doi:10.1016/0888-7543(91)90006-z · Cited by 72
Human Carbonic Anhydrases
Lin, K. D., & DEUTSCH, H. F. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44161-6 · Cited by 71
X-ray analysis of metal-substituted human carbonic anhydrase II derivatives
Håkansson, K., Wehnert, A., & Liljas, A. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444993008790 · Cited by 71
Phenol, a competitive inhibitor of CO2 hydration catalyzed by carbonic anhydrase
Simonsson, I., Jonsson, B., & Lindskog, S. F. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(82)80063-6 · Cited by 70
Self-citation
Carbon dioxide hydration activity of carbonic anhydrase in mixtures of water and deuterium oxide
Venkatasubban, K. S., & Silverman, D. N. (1980) · Biochemistry · doi:10.1021/bi00563a008 · Cited by 70
A Kinetic Analysis of the Folding of Human Carbonic Anhydrase II and Its Catalysis by Cyclophilin
Kern, G., Kern, D., Schmid, F. X., & Fischer, G. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.740 · Cited by 69
Evidence for direct metal-nitrogen binding in aromatic sulfonamide complexes of cadmium(II)-substituted carbonic anhydrases by cadmium-113 nuclear magnetic resonance
Evelhoch, J. L., Bocian, D. F., & Sudmeier, J. L. (1981) · Biochemistry · doi:10.1021/bi00520a022 · Cited by 69
Positions of His‐64 and a bound water in human carbonic anhydrase II upon binding three structurally related inhibitors
SMITH, G. M., Alexander, R., Christianson, D. W., McKeever, B. M., Ponticello, G. S., Springer, J. P., Randall, W. C., Baldwin, J. J., & Habecker, C. N. (1994) · Protein Science · doi:10.1002/pro.5560030115 · Cited by 67
Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions
Mangani, S., & Håkansson, K. E. J. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17490.x · Cited by 67
Inhibition of CA V decreases glucose synthesis from pyruvate
Dodgson, S. J., & Forster, R. E. (1986) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(86)90066-4 · Cited by 65
Human secreted carbonic anhydrase: cDNA cloning, nucleotide sequence, and hybridization histochemistry
Aldred, P., Fu, P., Barrett, G. L., Penschow, J. D., WRIGHT, R. D., Coghlan, J. P., & Fernley, R. T. (1991) · Biochemistry · doi:10.1021/bi00216a035 · Cited by 65
Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity.
Ippolito, J. A., Baird, T., Mcgee, S., Christianson, D. W., & Fierke, C. A. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.11.5017 · Cited by 64
Structural analysis of the zinc hydroxide–Thr‐199–Glu‐106 hydrogen‐bond network in human carbonic anhydrase II
Xue, Y., Liljas, A., Jonsson, B., & Lindskog, S. F. (1993) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340170112 · Cited by 64
Self-citation
Catalytic properties of mouse carbonic anhydrase V.
Heck, R. W., Tanhauser, S. M., Manda, R., Tu, C., Laipis, P. J., & Silverman, D. N. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31454-0 · Cited by 63
Carbonic anhydrase: inhibition results in decreased urea production by hepatocytes
Dodgson, S. J., & Forster, R. E. (1986) · Journal of Applied Physiology · doi:10.1152/jappl.1986.60.2.646 · Cited by 62
Determinants of catalytic activity and stability of carbonic anhydrase II as revealed by random mutagenesis.
Krebs, J., & Fierke, C. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54025-4 · Cited by 61
Determination of pKas of ionizable groups in proteins: the pKa of Glu 7 and 35 in hen eggs white lysozyme and Glu 106 in human carbonic anhydrase II
Merz, K. M. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00009a053 · Cited by 61
Immunochemical determination of tubulin
Kannan, K. K., Petef, M., Fridborg, K., Cid-Dresdner, H., & Lövgren, S. (1977) · FEBS Letters · doi:10.1016/0014-5793(77)80027-6 · Cited by 60
Engineering the zinc binding site of human carbonic anhydrase II: Structure of the His-94.fwdarw.Cys apoenzyme in a new crystalline form
Alexander, R., Kiefer, L. L., Fierke, C. A., & Christianson, D. W. (1993) · Biochemistry · doi:10.1021/bi00057a015 · Cited by 60
Cis‐trans isomerization is rate‐determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase
Fransson, C., Freskgård, P., Herbertsson, H., Johansson, Å., Jonasson, P., Mårtensson, L., Svensson, M., Jonsson, B., & Carlsson, U. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80410-i · Cited by 59
Enzyme-Substrate Interactions
Kumar, V., & Kannan, K. K. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1491 · Cited by 59
Subunit constitution of carbonic anhydrase from Chlamydomonas reinhardtii
Tomoko, K. A. M. O., Shimogawara, K., Fukuzawa, H., Muto, S., & Miyachi, S. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19261.x · Cited by 57
Structural and functional differences between carbonic anhydrase isoenzymes I and II as studied by site‐directed mutagenesis
Behravan, G., JONASSON, P., Jonsson, B., & Lindskog, S. F. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16054.x · Cited by 55
Self-citation
Structural basis of inhibitor affinity to variants of human carbonic anhydrase II
Nair, S. K., Krebs, J., Christianson, D. W., & Fierke, C. A. (1995) · Biochemistry · doi:10.1021/bi00012a016 · Cited by 55
Carbonic anhydrase IV: Role of removal of C-terminal domain in glycosylphosphatidylinositol anchoring and realization of enzyme activity
Okuyama, T., Waheed, A., Kusumoto, W., Zhu, X. L., & Sly, W. S. (1995) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(95)90015-2 · Cited by 55
Engineering a cysteine ligand into the zinc binding site of human carbonic anhydrase II
Kiefer, L. L., Krebs, J., Paterno, S. A., & Fierke, C. A. (1993) · Biochemistry · doi:10.1021/bi00089a004 · Cited by 54
Hydrolysis of 4-nitrophenyl acetate catalyzed by carbonic anhydrase III from bovine skeletal muscle.
Tu, C. K., Thomas, H. G., Wynns, G. C., & Silverman, D. N. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67496-4 · Cited by 53
Erythrocyte Carbonic Anhydrase I: Inherited Deficiency in Humans
Kendall, A. G., & Tashian, R. E. (1977) · Science · doi:10.1126/science.406674 · Cited by 53
Metal poison inhibition of carbonic anhydrase
Lindahl, M., Svensson, L. A., & Liljas, A. (1993) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340150207 · Cited by 52
Folding and Stability of the N-Terminus of Human Carbonic Anhydrase II
Aronsson, G., Mrtensson, L.-G., Carlsson, U., & Jonsson, B. (1995) · Biochemistry · doi:10.1021/bi00007a008 · Cited by 51
Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization
Semisotnov, G. V., Uversky, V. N., Sokolovskiy, I. V., Gutin, A. M., RAZGULYAEV, O. I., & Родионова, Н. А. (1990) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80215-3 · Cited by 51
The catalytic mechanism of carbonic anhydrase
Silverman, D. N. (1991) · Canadian Journal of Botany · doi:10.1139/b91-137 · Cited by 51
Histidine 64 is not required for high CO2 hydration activity of human carbonic anhydrase II
Forsman, C., Behravan, G., Jonsson, B., Liang, Z.-W., Lindskog, S., Ren, X., Sandström, J., & Wallgren, K. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)81156-6 · Cited by 50
Self-citation
Inhibition and catalysis of carbonic anhydrase
Liljas, A., Håkansson, K., Jonsson, B. H., & Xue, Y. (1994) · Springer eBooks · doi:10.1007/978-3-642-79502-2_1 · Cited by 50
Mapping Protein-Peptide Affinity: Binding of Peptidylsulfonamide Inhibitors to Human Carbonic Anhydrase II
Bunn, A. M. C., Alexander, R., & Christianson, D. W. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00091a006 · Cited by 50
Nucleotide sequence of pea cDNA encoding chloroplast carbonic anhydrase
Roeske, C. A., & Ogren, W. L. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.11.3413 · Cited by 49
Catalytic enhancement of human carbonic anhydrase III by replacement of phenylalanine-198 with leucine
LoGrasso, P. V., Tu, C., Jewell, D. A., Wynns, G. C., Laipis, P. J., & Silverman, D. N. (1991) · Biochemistry · doi:10.1021/bi00098a025 · Cited by 49
Refined structure of the aminobenzolamide complex of human carbonic anhydrase II at 1.9Åand sulphonamide modelling of bovine carbonic anhydrase III
Vidgren, J., Svensson, A. E., & Liljas, A. (1993) · International Journal of Biological Macromolecules · doi:10.1016/0141-8130(93)90004-6 · Cited by 49
Two point mutations convert a catalytically inactive carbonic anhydrase‐related protein (CARP) to an active enzyme
Sjöblom, B., Elleby, B., Wallgren, K., Jonsson, B., & Lindskog, S. F. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01263-x · Cited by 48
Self-citation
Carbonic anhydrase and the role of orientation in catalysis
Lindskog, S. F., & Liljas, A. (1993) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(93)90156-f · Cited by 47
Self-citation
The deduced amino acid sequence of human carbonic anhydrase-related protein (CARP) is 98% identical to the mouse homologue
Skaggs, L. A., Bergenhem, N. C. H., Venta, P. J., & Tashian, R. E. (1993) · Gene · doi:10.1016/0378-1119(93)90385-g · Cited by 47
Polymorphic gene for human carbonic anhydrase II: a molecular disease marker located on chromosome 8.
Venta, P. J., Shows, T. B., Curtis, P. J., & Tashian, R. E. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.14.4437 · Cited by 46
The pH dependence of the hydration of CO2 catalyzed by carbonic anhydrase III from skeletal muscle of the cat. Steady state and equilibrium studies.
Tu, C., Sanyal, G., Wynns, G. C., & Silverman, D. N. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32136-7 · Cited by 44
Proton Transfer by Histidine 67 in Site-Directed Mutants of Human Carbonic Anhydrase III
Ren, X., Tu, C., Laipis, P. J., & Silverman, D. N. (1995) · Biochemistry · doi:10.1021/bi00026a033 · Cited by 44
Structure and energetics of a non-proline cis-peptidyl linkage in a proline-202 .fwdarw. alanine carbonic anhydrase II variant
Tweedy, N. B., Nair, S. K., Paterno, S. A., Fierke, C. A., & Christianson, D. W. (1993) · Biochemistry · doi:10.1021/bi00092a003 · Cited by 44
Nucleotide sequence and derived amino acid sequence of a cDNA encoding human muscle carbonic anhydrase
Lloyd, J. C., McMillan, S., Hopkinson, D. A., & Edwards, Y. H. (1986) · Gene · doi:10.1016/0378-1119(86)90103-4 · Cited by 44
Redesigning the zinc binding site of human carbonic anhydrase II: structure of a His2Asp-Zn2+ metal coordination polyhedron
Kiefer, L. L., Ippolito, J. A., Fierke, C. A., & Christianson, D. W. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00079a046 · Cited by 43
Purification and characterization of a carbonic anhydrase II inhibitor from porcine plasma
Roush, E. D., & Fierke, C. A. (1992) · Biochemistry · doi:10.1021/bi00164a034 · Cited by 42
A nuclear‐magnetic‐resonance study of the binding of novel N ‐hydroxybenzenesulphonamide carbonic anhydrase inhibitors to native and cadmium‐111‐substituted carbonic anhydrase
Blackburn, G. M., Mann, B. E., Taylor, B. F., & Worrall, A. F. (1985) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1985.tb09336.x · Cited by 42
Structural Consequences of Redesigning a Protein-Zinc Binding Site
Ippolito, J. A., & Christianson, D. W. (1994) · Biochemistry · doi:10.1021/bi00255a004 · Cited by 39
Human muscle carbonic anhydrase: gene structure and DNA methylation patterns in fetal and adult tissues.Preprint
Lloyd, J. C., Brownson, C., Tweedie, S., Charlton, J. A., & Edwards, Y. H. (1987) · Genes & Development · doi:10.1101/gad.1.6.594 · Cited by 37
The structure of a complex between carbonic anhydrase II and a new inhibitor, trifluoromethane sulphonamide
Håkansson, K., & Liljas, A. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00798-5 · Cited by 36
Genomic Organization and Localization of Gene for Human Carbonic Anhydrase IV to Chromosome 17q
Okuyama, T., Batanian, J. R., & Sly, W. S. (1993) · Genomics · doi:10.1006/geno.1993.1247 · Cited by 34
Role of an evolutionarily invariant serine for the stability of human carbonic anhydrase II
Mårtensson, L., Jonsson, B., Andersson, M., Kihlgren, A., Bergenhem, N. C. H., & Carlsson, U. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90148-7 · Cited by 33
Mitochondrial carbonic anhydrase (isozyme V) in mouse and rat: cDNA cloning, expression, subcellular localization, processing, and tissue distribution.
Nagao, Y., Srinivasan, M., Platero, J. S., Svendrowski, M., Waheed, A., & Sly, W. S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10330 · Cited by 33
The inhibition of human carbonic anhydrase II by some organic compounds
Tibell, L. A. E., Forsman, C., Simonsson, I., & Lindskog, S. F. (1985) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(85)90189-x · Cited by 33
Self-citation
Comparison of intra- and intermolecular proton transfer in human carbonic anhydrase II.
Taoka, S., Tu, C., Kistler, K. A., & Silverman, D. N. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32407-9 · Cited by 32
A multinuclear ligand NMR investigation of cyanide, cyanate, and thiocyanate binding to zinc and cobalt carbonic anhydrase
Bertini, I., Luchinat, C., Pierattelli, R., & Vila, A. J. (1992) · Inorganic Chemistry · doi:10.1021/ic00045a022 · Cited by 32
Unexpected Binding Mode of the Sulfonamide Fluorophore 5-Dimethylamino-1-naphthalene Sulfonamide to Human Carbonic Anhydrase II
Nair, S. K., Elbaum, D., & Christianson, D. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.2.1003 · Cited by 32
Crystal Structure of the Complex between Human Carbonic Anhydrase II and the Aromatic Inhibitor 1,2,4-Triazole
Mangani, S., & Liljas, A. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1365 · Cited by 31
In vitro activity of sulfonamides against red cell carbonic anhydrases. Effect of ionic and substrate variation on the hydration reaction
Maren, T. H., & Wiley, C. E. (1968) · Journal of Medicinal Chemistry · doi:10.1021/jm00308a008 · Cited by 30
Catalytic and Inhibitor‐Binding Properties of Some Active‐Site Mutants of Human Carbonic Anhydrase I
Engstrand, C., Jonsson, B., & Lindskog, S. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0696j.x · Cited by 29
Self-citation
Solvent Hydrogen Isotope Effects and Anion Inhibition of CO2 Hydration Catalysed by Carbonic Anhydrase from Pisum sativum
Johansson, I., & Forsman, C. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.00901.x · Cited by 29
Structure and methylation patterns of the gene encoding human carbonic anhydrase I
Lowe, N., Brady, H. J. M., Barlow, J. H., Sowdes, J. C., Edwards, M., & Butterworth, P. H. W. (1990) · Gene · doi:10.1016/0378-1119(90)90236-k · Cited by 29
Expression of carbonic anhydrase in neisseriae and other heterotrophic bacteria
NAFI, B., Miles, R. J., Butler, L. O., CARTER, N. D., KELLY, C., & JEFFERY, S. (1990) · Journal of Medical Microbiology · doi:10.1099/00222615-32-1-1 · Cited by 29
Interaction of the unique competitive inhibitor imidazole with human carbonic anhydrase B
Wolpert, H. R., Strader, C. D., & Khalifah, R. G. (1977) · Biochemistry · doi:10.1021/bi00645a011 · Cited by 28
[18] Proton transfer in carbonic anhydrase measured by equilibrium isotope exchange
Silverman, D. N. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)49046-9 · Cited by 27
Buffer dependence of CO2 hydration catalyzed by human carbonic anhydrase I
Ren, X., & Lindskog, S. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90427-f · Cited by 27
Self-citation
Crystallographic studies of azide binding to human carbonic anhydrase II
Nair, S. K., & Christianson, D. W. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17788.x · Cited by 27
Structure of an engineered His3 Cys zinc binding site in human carbonic anhydrase II
Ippolito, J. A., & Christianson, D. W. (1993) · Biochemistry · doi:10.1021/bi00089a005 · Cited by 26
The interaction of acetate and formate with cobalt carbonic anhydrase
Bertini, I., Luchinat, C., Pierattelli, R., & Vila, A. J. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17225.x · Cited by 25
Proton transfer in the catalytic mechanism of carbonic anhydrase. Effects of placing histidine residues at various positions in the active site of human isoenzyme II
Liang, Z., Jonsson, B., & Lindskog, S. F. (1993) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(93)90048-v · Cited by 25
Self-citation
Proton transfer roles of lysine 64 and glutamic acid 64 replacing histidine 64 in the active site of human carbonic anhydrase II
Engstrand, C., Forsman, C., Liang, Z., & Lindskog, S. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90412-7 · Cited by 25
Self-citation
Some properties of site‐specific mutants of human carbonic anhydrase II having active‐site residues characterizing carbonic anhydrase III
Ren, X., Jonsson, B., & Lindskog, S. F. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16299.x · Cited by 24
Self-citation
Catalytic and Inhibitor-Binding Properties of Some Active-Site Mutants of Human Carbonic Anhydrase I
Engstrand, C., Jonsson, B., & Lindskog, S. F. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20516.x · Cited by 23
Self-citation
Inactivation of bovine carbonic anhydrase by dipicolinate: kinetic studies and mechanistic implications
Pocker, Y., & Fong, C. T. O. (1983) · Biochemistry · doi:10.1021/bi00273a016 · Cited by 22
The gene for human carbonic anhydrase VI (CA6) is on the tip of the short arm of chromosome 1
Sutherland, G. R., Baker, E. G., Fernandez, K. E. W., Callen, D. F., Aldred, P., Coghlan, J. P., WRIGHT, R. D., & Fernley, R. T. (2008) · Cytogenetics and Cell Genetics · doi:10.1159/000132746 · Cited by 22
The Sulfhydryl Groups of Cys 269 and Cys 272 Are Critical for the Oligomeric State of Chloroplast Carbonic Anhydrase from Pisum sativum
Björkbacka, H., Johansson, I., Skärfstad, E., & Forsman, C. (1997) · Biochemistry · doi:10.1021/bi962825k · Cited by 21
The human carbonic anhydrase I gene has two promoters with different tissue specificities
Brady, H. J. M., Lowe, N., Sowden, J. C., Edwards, M., & Butterworth, P. H. W. (1991) · Biochemical Journal · doi:10.1042/bj2770903 · Cited by 20
Wild-type and E106Q mutant carbonic anhydrase complexed with acetate
Håkansson, K., Briand, C., Зайцев, В. Н., Xue, Y., & Liljas, A. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444993009667 · Cited by 20
Organization of the Mouse and Human Carbonic Anhydrase II Genesa
Venta, P. J., Montgomery, J. C., Wiebauer, K., Hewett‐Emmett, D., & Tashian, R. E. (1984) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1984.tb12355.x · Cited by 20
Differences in anionic inhibition of human carbonic anhydrase I revealed from the structures of iodide and gold cyanide inhibitor complexes
Kumar, V., Kannan, K. K., & Sathyamurthi, P. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994001873 · Cited by 20
Expression of Mouse Carbonic Anhydrase VII inE. coliand Demonstration of Its CO2Hydrase Activity
Lakkis, M. M., Bergenhem, N. C. H., & Tashian, R. E. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1344 · Cited by 19
Structural properties of human carbonic anhydrase II at pH 9.5
Nair, S. K., & Christianson, D. W. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91229-6 · Cited by 18
Interaction and influence of phenylalanine-198 and threonine-199 on catalysis by human carbonic anhydrase III
Chen, X., Tu, C., LoGrasso, P. V., Laipis, P. J., & Silverman, D. N. (1993) · Biochemistry · doi:10.1021/bi00082a004 · Cited by 18
Physical mapping of the human carbonic anhydrase gene cluster on chromosome 8
Lowe, N., Edwards, Y. H., Edwards, M., & Butterworth, P. H. W. (1991) · Genomics · doi:10.1016/0888-7543(91)90176-f · Cited by 16
Über Inhibitoren der Carboanhydrase
Keller, H. M. (1955) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1955.299.1.85 · Cited by 15
Kinetic analysis of a mutant (His107–>Tyr) responsible for human carbonic anhydrase II deficiency syndrome.
Tu, C., Couton, J. M., Heeke, G. V., Richards, N. G. J., & Silverman, D. N. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53464-5 · Cited by 14
Kinetics, anion binding and mechanism of Co(II)‐substituted bovine muscle carbonic anhydrase
Ren, X., Sandström, A. G., & Lindskog, S. F. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb13968.x · Cited by 14
Self-citation
A Topical Carbonic Anhydrase Inhibitor Finally Arrives
Palmberg, P. F. (1995) · Archives of Ophthalmology · doi:10.1001/archopht.1995.01100080035025 · Cited by 14
The Structure of Cobalt(II)‐substituted Carbonic Anhydrase and Its Implications for the Catalytic Mechanism of the Enzyme
Bertini, I., & Luchinat, C. (1984) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1984.tb12318.x · Cited by 13

Research works printed but not linked: 5

Campbell, 1974, A study of the histidine residues of human carbonic anhydrase B using 270 MHz proton magnetic resonance, J. Mol. Biol., 90, 469, 10.1016/0022-2836(74)90229-0 · DOI
Kumar, 1989, Crystal structure of carbonic anhydrase II from erythrocyte of indian buffalo (Bubalus bubalis), Curr. Sci., 58, 344
Lindskog, 1982, Carbonic anhydrase, Vol. 4, 115
Lindskog, 1971, Carbonic anhydrase, Vol. 5, 587
Wagner, 1991, A human carbonic anhydrase I deficiency appears to be caused by a destabilizing amino acid substitution (246-Arg→His), Isozyme Bull., 24, 35

Sorted by citations

Aggregation-induced emission: phenomenon, mechanism and applications
Hong, Y., Lam, J. W. Y., & Tang, B. Z. (2009) · Chemical Communications · doi:10.1039/b904665h · Cited by 4,153
Controlling Mineral Morphologies and Structures in Biological and Synthetic Systems
Meldrum, F. C., & Cölfen, H. (2008) · Chemical Reviews · doi:10.1021/cr8002856 · Cited by 1,397
Industrial use of immobilized enzymes
DiCosimo, R., McAuliffe, J. C., Poulose, A. J., & Bohlmann, G. (2013) · Chemical Society Reviews · doi:10.1039/c3cs35506c · Cited by 1,269
Multiple Binding Modes of Inhibitors to Carbonic Anhydrases: How to Design Specific Drugs Targeting 15 Different Isoforms?
Alterio, V., Fiore, A. D., D’Ambrosio, K., Supuran, C. T., & Simone, G. D. (2012) · Chemical Reviews · doi:10.1021/cr200176r · Cited by 1,281
Function and Mechanism of Zinc Metalloenzymes
McCall, K. A., Huang, C.-C., & Fierke, C. A. (2000) · Journal of Nutrition · doi:10.1093/jn/130.5.1437s · Cited by 1,167

See all 1,022

Authors: Lindskog, S.
Affiliations: Umeå University (SE)
Corresponding author: Lindskog, Sven
Venue: Pharmacology & Therapeutics
Publisher: Elsevier BV
Published: 1997-01
Volume: 74
Issue: 1
Pages: 1-20
ISSN: 0163-7258 (ISSN-L)
DOI: 10.1016/s0163-7258(96)00198-2
OpenAlex: W2035046825
Cited by: 1,022
References: 212
Citations by year: 2026: 38 · 2025: 52 · 2024: 63 · 2023: 50 · 2022: 49 · 2021: 49 · 2020: 34 · 2019: 45 · 2018: 46 · 2017: 38 · 2016: 42 · 2015: 40 · 2014: 41 · 2013: 47 · 2012: 48
FWCI: 1.07
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Pharmacology & Therapeutics (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme function and inhibition
Physical Sciences › Chemistry › Organic Chemistry › Physical Organic Chemistry and Reaction Kinetics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: carbonic anhydrase, zinc metalloenzyme, CO2 hydration, bicarbonate, catalytic mechanism, isozymes, crystal structure, acetazolamide, carbonic anhydrase inhibitors, glaucoma, proton transfer, histidine residues
MeSH terms: Animals, Carbonic Anhydrases, Catalysis, Humans, Protein Conformation, Structure-Activity Relationship

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Structure and mechanism of carbonic anhydrase

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks