Cited by 311

The DOI matches its Crossref record; 142 of the 142 references it cites were found in a registry or an index.

Mode of Action of Bi- and Trinuclear Zinc Hydrolases and Their Synthetic Analogues

Weston, Jennie·2005·Chemical Reviews

DOI 10.1021/cr020057z

Open this paper in CoChat — free account

Abstract

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTMode of Action of Bi- and Trinuclear Zinc Hydrolases and Their Synthetic AnaloguesJennie WestonView Author Information Institut für Organische und Makromolekulare Chemie, Friedrich-Schiller-Universität, D-07743 Jena, Germany Cite this: Chem. Rev. 2005, 105, 6, 2151–2174Publication Date (Web):March 24, 2005Publication History Received19 June 2002Published online24 March 2005Published inissue 1 June 2005https://pubs.acs.org/doi/10.1021/cr020057zhttps://doi.org/10.1021/cr020057zresearch-articleACS PublicationsCopyright © 2005 American Chemical SocietyRequest reuse permissionsArticle Views2220Altmetric-Citations283LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose SUBJECTS:Ions,Ligands,Metals,Peptides and proteins,Zinc Get e-Alerts

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1021/cr020057z

Cites

142 of 142 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

On the size of the active site in proteases. I. Papain
Schechter, I., & Berger, A. (1967) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(67)80055-x · Cited by 5,204
A Chemist's Guide to Density Functional Theory
Koch, W., & Holthausen, M. C. (2001) · Wiley eBooks · doi:10.1002/3527600043 · Cited by 4,880
The crisis in antibiotic resistance
Neu, H. C. (1992) · Science · doi:10.1126/science.257.5073.1064 · Cited by 2,834
Structural and Functional Aspects of Metal Sites in Biology
Holm, R. H., Kennepohl, P., & Solomon, E. I. (1996) · Chemical Reviews · doi:10.1021/cr9500390 · Cited by 2,541
The structure of β-lactamases
Ambler, R. P. (1980) · Philosophical Transactions of the Royal Society of London. B, Biological Sciences · doi:10.1098/rstb.1980.0049 · Cited by 1,823
Coordinating properties of the amide bond. Stability and structure of metal ion complexes of peptides and related ligands
Sigel, H., & Martin, R. B. (1982) · Chemical Reviews · doi:10.1021/cr00050a003 · Cited by 1,611
Recent Advances in Zinc Enzymology
Lipscomb, W. N., & Sträter, N. (1996) · Chemical Reviews · doi:10.1021/cr950042j · Cited by 1,366
Reaction mechanism of alkaline phosphatase based on crystal structures
Kim, E. E., & Wyckoff, H. W. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90724-k · Cited by 944
Synthetic Analogues Relevant to the Structure and Function of Zinc Enzymes
Parkin, G. (2004) · Chemical Reviews · doi:10.1021/cr0206263 · Cited by 931
Binuclear Metallohydrolases
Wilcox, D. E. (1996) · Chemical Reviews · doi:10.1021/cr950043b · Cited by 893
Structure and Mechanism of Alkaline Phosphatase
Coleman, J. E. (1992) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.bb.21.060192.002301 · Cited by 883
Two‐Metal Ion Catalysis in Enzymatic Acyl‐ and Phosphoryl‐Transfer Reactions
Sträter, N., Lipscomb, W. N., Klabunde, T., & Krebs, B. (1996) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199620241 · Cited by 611
Characterization of VIM-2, a Carbapenem-Hydrolyzing Metallo-β-Lactamase and Its Plasmid- and Integron-Borne Gene from a Pseudomonas aeruginosa Clinical Isolate in France
Poirel, L., Naas, T., Nicolas, D., Collet, L., Bellais, S., Cavallo, J.-D., & Nordmann, P. (2000) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.44.4.891-897.2000 · Cited by 562
Aminopeptidases: structure and function
Taylor, A. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.2.8440407 · Cited by 554
Purification and Properties of the Phosphotriesterase from Pseudomonas diminuta
Dumas, D. P., Caldwell, S. R., Wild, J. R., & Raushel, F. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47164-0 · Cited by 498
The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold.
Carfi, A., Pares, S., Duée, E., Galleni, M., Duez, C., Frère, J. M., & Dideberg, O. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00174.x · Cited by 459
High-resolution (1.5 Å) crystal structure of phospholipase C from Bacillus cereus
Hough, E., Hansen, L. K., Birknes, B., Jynge, K., Hansen, S., Hordvik, A., Little, C., Dodson, E., & Derewenda, Z. (1989) · Nature · doi:10.1038/338357a0 · Cited by 455
Standard Numbering Scheme for Class B β-Lactamases
Galleni, M., Lamotte-Brasseur, J., Rossolini, G. M., Spencer, J., Dideberg, O., Frère, J.-M., & The Metallo-β-Lactamase Working Group (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.3.660-663.2001 · Cited by 414
Zinc: biological functions and coordination motifs
Vallee, B. L., & Auld, D. S. (1993) · Accounts of Chemical Research · doi:10.1021/ar00034a005 · Cited by 412
Dinuclear metallo-phosphodiesterase models: application of calix[4]arenes as molecular scaffolds
Molenveld, P., Engbersen, J. F. J., & Reinhoudt, D. N. (2000) · Chemical Society Reviews · doi:10.1039/a804295k · Cited by 392
Identification of an opd(Organophosphate Degradation) Gene in an Agrobacterium Isolate
Horne, I., Sutherland, T. D., Harcourt, R. L., Russell, R. J., & Oakeshott, J. G. (2002) · Applied and Environmental Microbiology · doi:10.1128/aem.68.7.3371-3376.2002 · Cited by 367
Carbapenem-hydrolyzing beta-lactamases
Rasmussen, B. A., & Bush, K. (1997) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.41.2.223 · Cited by 361
Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis
Concha, N. O., Rasmussen, B. A., Bush, K., & Herzberg, O. (1996) · Structure · doi:10.1016/s0969-2126(96)00089-5 · Cited by 359
Metalloaminopeptidases: Common Functional Themes in Disparate Structural Surroundings
Lowther, W. T., & Matthews, B. W. (2002) · Chemical Reviews · doi:10.1021/cr0101757 · Cited by 350
The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 å resolution 1 1Edited by K. Nagai
Ullah, J. H., Walsh, T. R., Taylor, I. A., Emery, D. C., Verma, C. S., Gamblin, S. J., & Spencer, J. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2148 · Cited by 337
Roles of zinc(II) ion in phosphatases. A model study with zinc(II)-macrocyclic polyamine complexes
Koike, T., & Kimura, E. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00023a048 · Cited by 334
Characterization of the zinc binding site of bacterial phosphotriesterase.
Omburo, G. A., Kuo, J. M., Mullins, L. S., & Raushel, F. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42207-7 · Cited by 325
Mechanism for the Hydrolysis of Organophosphates by the Bacterial Phosphotriesterase
Aubert, S. D., Li, Y., & Raushel, F. M. (2004) · Biochemistry · doi:10.1021/bi0497805 · Cited by 316
Crystal Structure of the IMP-1 Metallo β-Lactamase from Pseudomonas aeruginosa and Its Complex with a Mercaptocarboxylate Inhibitor: Binding Determinants of a Potent, Broad-Spectrum Inhibitor,
Concha, N. O., Janson, C. A., Rowling, P., Pearson, S., Cheever, C. A., Clarke, B. P., Lewis, C., Galleni, M., Frère, J.-M., Payne, D. J., et al. (2000) · Biochemistry · doi:10.1021/bi992569m · Cited by 307
A revised mechanism for the alkaline phosphatase reaction involving three metal ions
Stec, B., Holtz, K. M., & Kantrowitz, E. R. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3799 · Cited by 305
Expansion of the zinc metallo‐hydrolase family of the β‐lactamase fold
Daiyasu, H., Osaka, K., Ishino, Y., & Toh, H. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02686-2 · Cited by 304
Update of the Standard Numbering Scheme for Class B β-Lactamases
Garau, G., García-Sáez, I., Bebrone, C., Anne, C., Mercuri, P., Galleni, M., Frère, J.-M., & Dideberg, O. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.7.2347-2349.2004 · Cited by 286
Metallo-β-lactamase: structure and mechanism
Wang, Z., Fast, W., Valentine, A. M., & Benkovic, S. J. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)00017-4 · Cited by 275
Crystal structure of Penicillium citrinum P1 nuclease at 2.8 A resolution.
Volbeda, A., Lahm, A., Sakiyama, F., & Suck, D. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07683.x · Cited by 258
Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family
Chevrier, B., Schalk, C., D'Orchymont, H., Rondeau, J. M., Moras, D., & Tarnus, C. (1994) · Structure · doi:10.1016/s0969-2126(00)00030-7 · Cited by 244
High Resolution X-ray Structures of Different Metal-Substituted Forms of Phosphotriesterase from Pseudomonas diminuta,
Benning, M. M., Shim, H., Raushel, F. M., & Holden, H. M. (2001) · Biochemistry · doi:10.1021/bi002661e · Cited by 231
Bacterial detoxification of organophosphate nerve agents
Raushel, F. M. (2002) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(02)00314-4 · Cited by 226
Identification of a plasmid-borne parathion hydrolase gene from Flavobacterium sp. by southern hybridization with opd from Pseudomonas diminuta
Mulbry, W. W., Karns, J. S., Kearney, P. C., Nelson, J. O., McDaniel, C. S., & Wild, J. R. (1986) · Applied and Environmental Microbiology · doi:10.1128/aem.51.5.926-930.1986 · Cited by 224
Three-Dimensional Structure of Phosphotriesterase: An Enzyme Capable of Detoxifying Organophosphate Nerve Agents
Benning, M. M., Kuo, J. M., Raushel, F. M., & Holden, H. M. (1994) · Biochemistry · doi:10.1021/bi00254a008 · Cited by 216
Crystal Structure of the Zinc-Dependent β-Lactamase from Bacillus cereus at 1.9 Å Resolution: Binuclear Active Site with Features of a Mononuclear Enzyme,
Fabiane, S. M., Sohi, M. K., Wan, T., Payne, D. J., Bateson, J. H., Mitchell, T., & Sutton, B. J. (1998) · Biochemistry · doi:10.1021/bi980506i · Cited by 215
Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin
Burley, S. K., David, P. R., Sweet, R. M., Taylor, A., & Lipscomb, W. N. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90580-d · Cited by 211
Three-dimensional structure of the binuclear metal center of phosphotriesterase
Benning, M. M., Kuo, J. M., Raushel, F. M., & Holden, H. M. (1995) · Biochemistry · doi:10.1021/bi00025a002 · Cited by 204
The β-lactamase cycle: a tale of selective pressure and bacterial ingenuity
Matagne, A., Dubus, A., Galleni, M., & Frère, J.-M. (1999) · Natural Product Reports · doi:10.1039/a705983c · Cited by 202
An overview of the kinetic parameters of class B β -lactamases
Felici, A., Amicosante, G., Oratore, A., Ström, R., Ledent, P., Joris, B., Fanuel, L., & Frère, J. (1993) · Biochemical Journal · doi:10.1042/bj2910151 · Cited by 198
Mechanism and stereochemical course at phosphorus of the reaction catalyzed by a bacterial phosphotriesterase
Lewis, V. E., Donarski, W. J., Wild, J. R., & Raushel, F. M. (1988) · Biochemistry · doi:10.1021/bi00405a030 · Cited by 181
On the Mechanism of the Metallo-β-lactamase from Bacteroides fragilis
Wang, Z., Fast, W., & Benkovic, S. J. (1999) · Biochemistry · doi:10.1021/bi990356r · Cited by 178
Functional Interrelationships in the Alkaline Phosphatase Superfamily: Phosphodiesterase Activity of Escherichia coli Alkaline Phosphatase
O'Brie, P. J., & Herschlag, D. (2001) · Biochemistry · doi:10.1021/bi0028892 · Cited by 176
Zn(II) Dependence of the Aeromonas hydrophila AE036 Metallo-β-lactamase Activity and Stability
Hernandez Valladares, M., Felici, A., Weber, G., Adolph, H. W., Zeppezauer, M., Rossolini, G. M., Amicosante, G., Frère, J.-M., & Galleni, M. (1997) · Biochemistry · doi:10.1021/bi971056h · Cited by 176
Use of Isotope Effects to Elucidate Enzyme Mechanism
Wallace Cleland, W. (1982) · Critical Reviews in Biochemistry · doi:10.3109/10409238209108715 · Cited by 175
Two-Metal Ion Mechanism of Bovine Lens Leucine Aminopeptidase: Active Site Solvent Structure and Binding Mode of L-Leucinal, a gem-Diolate Transition State Analog, by X-ray Crystallography
Straeter, N., & Lipscomb, W. N. (1995) · Biochemistry · doi:10.1021/bi00045a021 · Cited by 172
Limits of diffusion in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta
Caldwell, S. R., Newcomb, J. R., Schlecht, K. A., & Raushel, F. M. (1991) · Biochemistry · doi:10.1021/bi00244a010 · Cited by 170
Alkaline Phosphatase Revisited: Hydrolysis of Alkyl Phosphates
O'Brien, P. J., & Herschlag, D. (2002) · Biochemistry · doi:10.1021/bi012166y · Cited by 162
Evolution of an organophosphate-degrading enzyme: a comparison of natural and directed evolution
Yang, H., Carr, P. D., McLoughlin, S. Y., Liu, J. W., Horne, I., Qiu, X., Jeffries, C. M. J., Russell, R. J., Oakeshott, J. G., & Ollis, D. L. (2003) · Protein Engineering, Design and Selection · doi:10.1093/proeng/gzg013 · Cited by 162
Cell Signalling Through Guanine‐Nucleotide‐Binding Regulatory Proteins (G Proteins) and Phospholipases
Exton, J. H. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00010.x · Cited by 155
PHOSPHATE INCORPORATION INTO ALKALINE PHOSPHATASE OF E. COLI
Schwartz, J. H., & Lipmann, F. A. (1961) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.47.12.1996 · Cited by 145
Mammalian Alkaline Phosphatases Are Allosteric Enzymes
Hoylaerts, M., Manes, T. D., & Millán, J. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.36.22781 · Cited by 142
Metal−Substrate Interactions Facilitate the Catalytic Activity of the Bacterial Phosphotriesterase
Hong, S.-B., & Raushel, F. M. (1996) · Biochemistry · doi:10.1021/bi960663m · Cited by 141
The Structure of the Aeromonas proteolytica Aminopeptidase Complexed with a Hydroxamate Inhibitor
Chevrier, B., d'Orchymont, H., Schalk, C., Tarnus, C., & Moras, D. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0393k.x · Cited by 139
Transition State Analog L-Leucinephosphonic Acid Bound to Bovine Lens Leucine Aminopeptidase: X-ray Structure at 1.65 .ANG. Resolution in a New Crystal Form
Sträter, N., & Lipscomb, W. N. (1995) · Biochemistry · doi:10.1021/bi00028a033 · Cited by 139
Structural Determinants of the Substrate and Stereochemical Specificity of Phosphotriesterase
Chen‐Goodspeed, M., Sogorb, M. A., Wu, F., Hong, S.-B., & Raushel, F. M. (2001) · Biochemistry · doi:10.1021/bi001548l · Cited by 138
Mono- and Binuclear Zn2+-β-Lactamase
Soto, R. P., Bauer, R., Frère, J., Galleni, M., Meyer‐Klaucke, W., Nolting, H. F., Rossolini, G. M., de Seny, D., Hernandez-Valladares, M., Zeppezauer, M. M., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13242 · Cited by 132
X‐ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site‐specific recombination
Sträter, N., Sherratt, D. J., & Colloms, S. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.16.4513 · Cited by 131
Three-dimensional Structure of FEZ-1, a Monomeric Subclass B3 Metallo-β-lactamase from Fluoribacter gormanii, in Native Form and in Complex with d-Captopril
Garcia-Saez, I., Mercuri, P. S., Papamicaël, C. A., Kahn, R., Frère, J.-M., Galleni, M., Rossolini, G. M., & Dideberg, O. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01271-8 · Cited by 131
Comparison of the Binuclear Metalloenzymes Diphosphoglycerate-Independent Phosphoglycerate Mutase and Alkaline Phosphatase: Their Mechanism of Catalysis via a Phosphoserine Intermediate
Jedrzejas, M. J., & Setlow, P. (2001) · Chemical Reviews · doi:10.1021/cr000253a · Cited by 128
Metal Ion Binding and Coordination Geometry for Wild Type and Mutants of Metallo-β-lactamase from Bacillus cereus569/H/9 (BcII)
de Seny, D., Heinz, U., Wommer, S., Kiefer, M., Meyer‐Klaucke, W., Galleni, M., Frère, J., Bauer, R., & Adolph, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106447200 · Cited by 124
Enhancement, Relaxation, and Reversal of the Stereoselectivity for Phosphotriesterase by Rational Evolution of Active Site Residues
Chen‐Goodspeed, M., Sogorb, M. A., Wu, F., & Raushel, F. M. (2001) · Biochemistry · doi:10.1021/bi001549d · Cited by 124
Phosphate transport in prokaryotes: molecules, mediators and mechanisms
van Veen, H. W. (1997) · Antonie van Leeuwenhoek · doi:10.1023/a:1000530927928 · Cited by 122
Streptomyces griseus aminopeptidase: X-ray crystallographic structure at 1.75 Å resolution
Greenblatt, H. M., Almog, O., Maras, B., Spungin‐Bialik, A., Barra, D., Blumberg, S., & Shoham, G. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0729 · Cited by 120
Substrate-activated Zinc Binding of Metallo-β-lactamases
Wommer, S., Rival, S. G., Heinz, U., Galleni, M., Frère, J., Franceschini, N., Amicosante, G., Rasmussen, B. W., Bauer, R., & Adolph, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202467200 · Cited by 120
Highly Selective Recognition of Thymidine Mono- and Diphosphate Nucleotides in Aqueous Solution by Ditopic Receptors Zinc(II)−Bis(cyclen) Complexes (Cyclen = 1,4,7,10-Tetraazacyclododecane)
Aoki, S., & Kimura, E. (2000) · Journal of the American Chemical Society · doi:10.1021/ja994537s · Cited by 119
Thiomandelic Acid, a Broad Spectrum Inhibitor of Zinc β-Lactamases
Mollard, C., Moali, C., Papamicaël, C. A., Damblon, C., Vessilier, S., Amicosante, G., Schofield, C. J., Galleni, M., Frère, J., & Roberts, G. C. K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107054200 · Cited by 118
Bimetallic dioxygen complexes derived from ‘end-off’ compartmental ligands
Suzuki, M., Furutachi, H., & Ōkawa, H. (2000) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(00)00323-4 · Cited by 112
Recognition of single-stranded DNA by nuclease P1: High resolution crystal structures of complexes with substrate analogs
Romier, C., Domínguez, R., Lahm, A., Dahl, O., & Suck, D. (1998) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(19980901)32:4<414::aid-prot2>3.0.co;2-g · Cited by 109
Effect of magnesium on the properties of zinc alkaline phosphatase
BOSRON, W. F., Anderson, R. A., Falk, M. C., Kennedy, F. S., & Vallce, B. L. (1977) · Biochemistry · doi:10.1021/bi00623a009 · Cited by 103
A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase
Sträter, N., Sun, L., Kantrowitz, E. R., & Lipscomb, W. N. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11151 · Cited by 102
Why zinc in zinc enzymes? From biological roles to DNA base-selective recognition
Kimura, E., & Kikuta, E. (2000) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050359 · Cited by 101
Alkaline Phosphatase Is an Almost Perfect Enzyme
Simopoulos, T. T., & Jencks, W. P. (1994) · Biochemistry · doi:10.1021/bi00200a018 · Cited by 100
NMR Characterization of the Metallo-β-lactamase from Bacteroides fragilis and Its Interaction with a Tight-Binding Inhibitor: Role of an Active-Site Loop
Scrofani, S. D. B., Chung, J., Huntley, J. J. A., Benkovic, S. J., Wright, P. E., & Dyson, H. J. (1999) · Biochemistry · doi:10.1021/bi990986t · Cited by 99
Transition-state structures for enzymic and alkaline phosphotriester hydrolysis
Caldwell, S. R., Raushel, F. M., Weiss, P. M., & Cleland, W. W. (1991) · Biochemistry · doi:10.1021/bi00244a011 · Cited by 98
Water-Assisted Reaction Mechanism of Monozinc β-Lactamases
Peraro, M. D., Llarrull, L. I., Röthlisberger, U., Vila, A. J., & Carloni, P. (2004) · Journal of the American Chemical Society · doi:10.1021/ja048071b · Cited by 94
pKa of zinc-bound water and nucleophilicity of hydroxo-containing species. Ab initio calculations on models for zinc enzymes
Bertini, I., Luchinat, C., Rosi, M., Sgamellotti, A., & Tarantelli, F. (1990) · Inorganic Chemistry · doi:10.1021/ic00333a004 · Cited by 92
Novel Mechanism of Hydrolysis of Therapeutic β-Lactams byStenotrophomonas maltophilia L1 Metallo-β-lactamase
SPENCER, J. M., Clarke, A. R., & Walsh, T. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105550200 · Cited by 90
Structural Analysis of Inositol Monophosphatase Complexes with Substrates
Bone, R. F., Frank, L., Springer, J. P., Pollack, S. J., Osborne, S., Atack, J. R., Knowles, M. R., McAllister, G., & RAGAN, C. I. (1994) · Biochemistry · doi:10.1021/bi00198a011 · Cited by 87
A Bimetallic Helical Heptapeptide as a Transphosphorylation Catalyst in Water
Rossi, P., Felluga, F., Tecilla, P., Formaggio, F., Crisma, M., Toniolo, C., & Scrimin, P. (1999) · Journal of the American Chemical Society · doi:10.1021/ja9908164 · Cited by 86
Mechanistic Studies on the Aminopeptidase from Aeromonas proteolytica: A Two-Metal Ion Mechanism for Peptide Hydrolysis
Chen, G., Edwards, T., D'souz, V. M., & Holz, R. C. (1997) · Biochemistry · doi:10.1021/bi9618676 · Cited by 84
EPR Studies on the Mono- and Dicobalt(II)-Substituted Forms of the Aminopeptidase from Aeromonas proteolytica. Insight into the Catalytic Mechanism of Dinuclear Hydrolases
Bennett, B., & Holz, R. C. (1997) · Journal of the American Chemical Society · doi:10.1021/ja963021v · Cited by 84
Parallel ab initio and molecular mechanics investigation of polycoordinated Zn(II) complexes with model hard and soft ligands: Variations of binding energy and of its components with number and charges of ligands
Tiraboschi, G., Gresh, N., GIESSNER‐PRETTRE, C., Pedersen, L. G., & Deerfield, D. W. (2000) · Journal of Computational Chemistry · Cited by 82
Determination of Two Structural Forms of Catalytic Bridging Ligand in Zinc−Phosphotriesterase by Molecular Dynamics Simulation and Quantum Chemical Calculation
Zhan, C., de Souza, O. N., Rittenhouse, R. C., & Ornstein, R. L. (1999) · Journal of the American Chemical Society · doi:10.1021/ja9906397 · Cited by 81
A peptide template as an allosteric supramolecular catalyst for the cleavage of phosphate esters
Scarso, A., Scheffer, U., Göbel, M., Broxterman, Q. B., Kaptein, B., Formaggio, F., Toniolo, C., & Scrimin, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072642699 · Cited by 81
Inhibition of the Aminopeptidase from Aeromonas proteolytica by l -Leucinephosphonic Acid. Spectroscopic and Crystallographic Characterization of the Transition State of Peptide Hydrolysis
Stamper, C. C., Bennett, B., Edwards, T., Holz, R. C., Ringe, D., & Petsko, G. A. (2001) · Biochemistry · doi:10.1021/bi0100891 · Cited by 81
Metallo-?-lactamases: two binding sites for one catalytic metal ion?
Heinz, U., & Adolph, H. W. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4214-9 · Cited by 80
The aminopeptidase from Aeromonas proteolytica: structure and mechanism of co-catalytic metal centers involved in peptide hydrolysis
Holz, R. C. (2002) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(01)00470-2 · Cited by 80
Conjugates of a Dinuclear Zinc(II) Complex and DNA Oligomers as Novel Sequence-Selective Artificial Ribonucleases
Matsuda, S., Ishikubo, A., Kuzuya, A., Yashiro, M., & Komiyama, M. (1998) · Angewandte Chemie International Edition · Cited by 78
Stereochemical Constraints on the Substrate Specificity of Phosphotriesterase
Hong, S.-B., & Raushel, F. M. (1998) · Biochemistry · doi:10.1021/bi982204m · Cited by 77
Insights into the Structure and Dynamics of the Dinuclear Zinc β-Lactamase Site from Bacteroides fragilis
Suárez, D., Brothers, E. N., & Merz, K. M. (2002) · Biochemistry · doi:10.1021/bi0121860 · Cited by 77
Spectral and kinetic studies of metal-substituted Aeromonas aminopeptidase: nonidentical, interacting metal-binding sites
Prescott, J. M., Wagner, F. W., Holmquist, B., & Vallée, B. L. (1985) · Biochemistry · doi:10.1021/bi00341a012 · Cited by 74
Mobility of the Active Site Bound Paraoxon and Sarin in Zinc-Phosphotriesterase by Molecular Dynamics Simulation and Quantum Chemical Calculation
Koča, J., Zhan, C., Rittenhouse, R. C., & Ornstein, R. L. (2001) · Journal of the American Chemical Society · doi:10.1021/ja000439r · Cited by 73
Study of the mechanism of Flavobacterium sp. for hydrolyzing organophosphate pesticides
Ortiz-Hernández, M. L., Ramírez, R. Q., Nava‐Ocampo, A. A., & Bello, A. M. (2003) · Fundamental and Clinical Pharmacology · doi:10.1046/j.1472-8206.2003.00202.x · Cited by 71
Bestatin-mediated inhibition of leucine aminopeptidase may hinder HIV infection
Pulido-Cejudo, G., Conway, B., Proulx, P., Brown, R., & Izaguirre, C. A. (1997) · Antiviral Research · doi:10.1016/s0166-3542(97)00052-1 · Cited by 71
Modification of Near Active Site Residues in Organophosphorus Hydrolase Reduces Metal Stoichiometry and Alters Substrate Specificity
Disioudi, B. D., Grimsley, J. K., Lai, K., & Wild, J. R. (1999) · Biochemistry · doi:10.1021/bi9825302 · Cited by 69
Metal Binding Asp-120 in Metallo-β-lactamase L1 from Stenotrophomonas maltophilia Plays a Crucial Role in Catalysis
Garrity, J. D., Carenbauer, A. L., Herron, L. R., & Crowder, M. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309852200 · Cited by 69
Spectroscopically Distinct Cobalt(II) Sites in Heterodimetallic Forms of the Aminopeptidase from Aeromonas proteolytica: Characterization of Substrate Binding
Bennett, B., & Holz, R. C. (1997) · Biochemistry · doi:10.1021/bi970735p · Cited by 68
Biochemical Characterization of the FEZ-1 Metallo-β-Lactamase of Legionella gormanii ATCC 33297 T Produced in Escherichia coli
Mercuri, P. S., Bouillenne, F., Boschi, L., Lamotte‐Brasseur, J., Amicosante, G., Devreese, B. V., BEEUMEN, J. V., Frère, J., Rossolini, G. M., & Galleni, M. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.4.1254-1262.2001 · Cited by 68
Mono‐ and binuclear Zn‐β‐lactamase from Bacteroides fragilis: catalytic and structural roles of the zinc ions
Soto, R. P., Hernandez-Valladares, M., Galleni, M., Bauer, R., Zeppezauer, M. M., Frère, J., & Adolph, H. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01289-7 · Cited by 67
Biochemical Characterization and Crystallographic Structure of an Escherichia coli Protein from the Phosphotriesterase Gene Family
Buchbinder, J. L., Stephenson, R. C., Dresser, M. J., Pitera, J. W., Scanlan, T. S., & Fletterick, R. J. (1998) · Biochemistry · doi:10.1021/bi971707+ · Cited by 65
Hydrolysis of a Model for the 5‘-Cap of mRNA by Dinuclear Copper(II) and Zinc(II) Complexes. Rapid Hydrolysis by Four Copper(II) Ions
McCue, K. P., & Morrow, J. R. (1999) · Inorganic Chemistry · doi:10.1021/ic990380t · Cited by 64
Co-catalytic metallopeptidases as pharmaceutical targets
Holz, R. C. (2003) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(03)00033-4 · Cited by 64
Structural Determinants of Substrate Binding to Bacillus cereus Metallo-β-lactamase
Rasia, R. M., & Vila, A. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311373200 · Cited by 62
The 1.20 Å Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris
Desmarais, W., Bienvenue, D., Bzymek, K. P., Holz, R. C., Petsko, G. A., & Ringe, D. (2002) · Structure · doi:10.1016/s0969-2126(02)00810-9 · Cited by 62
Molecular Bases for Interactions between β-Lactam Antibiotics and β-Lactamases
Massova, I., & Mobashery, S. (1997) · Accounts of Chemical Research · doi:10.1021/ar960007e · Cited by 61
Coordination number of zinc ions in the phosphotriesterase active site by molecular dynamics and quantum mechanics
Koča, J., Zhan, C., Rittenhouse, R. C., & Ornstein, R. L. (2003) · Journal of Computational Chemistry · doi:10.1002/jcc.10217 · Cited by 58
Molecular Dynamics Simulations of the Mononuclear Zinc-β-lactamase fromBacilluscereusComplexed with Benzylpenicillin and a Quantum Chemical Study of the Reaction Mechanism
Díaz, N., Suárez, D., & Merz, K. M. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0113246 · Cited by 57
Molecular dynamics simulations of the dinuclear zinc‐β‐lactamase from Bacteroides fragilis complexed with imipenem
Suárez, D., Díaz, N., & Merz, K. M. (2002) · Journal of Computational Chemistry · doi:10.1002/jcc.10157 · Cited by 54
The Catalytic Role of Glutamate 151 in the Leucine Aminopeptidase from Aeromonas proteolytica
Bzymek, K. P., & Holz, R. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404035200 · Cited by 52
Trapping and visualization of a covalent enzyme–phosphate intermediate
Murphy, J. E., Stec, B., Ma, L., & Kantrowitz, E. R. (1997) · Nature Structural Biology · doi:10.1038/nsb0897-618 · Cited by 51
Carboxylate- and Phosphate Ester-Bridged Dimagnesium(II), Dizinc(II), and Dicalcium(II) Complexes. Models for Intermediates in Biological Phosphate Ester Hydrolysis
Yun, J. W., Tanase, T., & Lippard, S. J. (1996) · Inorganic Chemistry · doi:10.1021/ic960894h · Cited by 50
Efficient Inhibition of Photo[2 + 2]cycloaddition of Thymidilyl(3‘−5‘)thymidine and Promotion of Photosplitting of the cis-syn-Cyclobutane Thymine Dimer by Dimeric Zinc(II)−Cyclen Complexes Containing m- and p-Xylyl Spacers
Aoki, S., Sugimura, C., & Kimura, E. (1998) · Journal of the American Chemical Society · doi:10.1021/ja981788c · Cited by 46
Phthalazine-Based Dinucleating Ligands Afford Dinuclear Centers Often Encountered in Metalloenzyme Active Sites
Barrios, A. M., & Lippard, S. J. (2001) · Inorganic Chemistry · doi:10.1021/ic000889k · Cited by 44
Phosphate Binding in the Active Site of Alkaline Phosphatase and the Interactions of 2-Nitrosoacetophenone with Alkaline Phosphatase-Induced Small Structural Changes
Zhang, L., Buchet, R., & Azzar, G. (2004) · Biophysical Journal · doi:10.1529/biophysj.103.034116 · Cited by 44
Substrate binding to mononuclear metallo‐β‐lactamase from Bacillus cereus
Peraro, M. D., Vila, A. J., & Carloni, P. (2003) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10554 · Cited by 43
Modeling of the metallo‐β‐lactamase from B. fragilis: Structural and dynamic effects of inhibitor binding
Salsbury, F. R., Crowley, M. F., & Brooks, C. L. (2001) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.1110 · Cited by 43
Zinc catalysis in metalloproteases
Auld, D. S. (1997) · Springer eBooks · doi:10.1007/3-540-62874-6_8 · Cited by 42
Trinuclear Zn(II) and Cu(II) Homo and Heterotrimetallic Complexes Involving d -Glucopyranosyl and Biscarboxylate Bridging Ligands. A Substrate Binding Model of Xylose Isomerases
Tanase, T., 犬飼裕美, Onaka, T., Kato, M., Yano, S., & Lippard, S. J. (2001) · Inorganic Chemistry · doi:10.1021/ic001419t · Cited by 41
Spectroscopic and X-ray Crystallographic Characterization of Bestatin Bound to the Aminopeptidase from Aeromonas (Vibrio) proteolytica,
Stamper, C. C., Bienvenue, D., Bennett, B., Ringe, D., Petsko, G. A., & Holz, R. C. (2004) · Biochemistry · doi:10.1021/bi049126p · Cited by 35
Structurally Distinct Active Sites in the Copper(II)-Substituted Aminopeptidases from Aeromonas proteolytica and Escherichia coli
Bennett, B., Antholine, W. E., D’souza, V. M., Chen, G., Ustinyuk, L., & Holz, R. C. (2002) · Journal of the American Chemical Society · doi:10.1021/ja026341p · Cited by 34
Slow-Binding Inhibition of the Aminopeptidase from Aeromonas proteolytica by Peptide Thiols: Synthesis and Spectroscopic Characterization
Huntington, K. M., Bienvenue, D., Wei, Y., Bennett, B., Holz, R. C., & Pei, D. (1999) · Biochemistry · doi:10.1021/bi991283e · Cited by 28
Molecular recognition of dipeptides. Catalysis of deuteration and hydrolysis of glycylglycine by dinuclear OBISDIEN Zn(II) complexes
Bordignon-Luiz, M. T., Szpoganicz, B., Rizzoto, M., Basallote, M. G., & Martell, A. E. (1999) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(98)00416-2 · Cited by 28
Computational methods for RNA structure determination
Major, F., & Griffey, R. H. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00203-7 · Cited by 28
Inhibition of the aminopeptidase from Aeromonas proteolytica by l-leucinethiol: kinetic and spectroscopic characterization of a slow, tight-binding inhibitor–enzyme complex
Bienvenue, D., Bennett, B., & Holz, R. C. (2000) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(99)00203-2 · Cited by 27
CO2 Is Required for the Assembly of the Binuclear Metal Center of Phosphotriesterase
Hong, S.-B., Kuo, J. M., Mullins, L. S., & Raushel, F. M. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00133a046 · Cited by 26
Catalytic Cycle of the Phosphatidylcholine-Preferring Phospholipase C from Bacillus cereus. Solvent Viscosity, Deuterium Isotope Effects, and Proton Inventory Studies
Martin, S. F., & Hergenrother, P. J. (1999) · Biochemistry · doi:10.1021/bi9821216 · Cited by 26
A Water Sluice Is Generated in the Active Site of Bovine Lens Leucine Aminopeptidase
Erhardt, S., Jaime, E., & Weston, J. (2005) · Journal of the American Chemical Society · doi:10.1021/ja042797q · Cited by 24
Self-citation
A novel dizinc bridged hydroxamate model for hydroxamate inhibited zinc hydrolasesAbbreviations: OAc = CH3CO2–, BHA = benzohydroxamic acid, BA=deprotonated hydroxamic acid, tmen = tetramethylethylenediamine.
Brown, D. A., Errington, W., Fitzpatrick, N. J., GLASS, W. K., Kemp, T. J., Nimir, H., & Ryan, Á. T. (2002) · Chemical Communications · doi:10.1039/b202612k · Cited by 21
General Base Catalysis by the Phosphatidylcholine-Preferring Phospholipase C from Bacillus cereus: The Role of Glu4 and Asp55
Martin, S. F., & Hergenrother, P. J. (1998) · Biochemistry · doi:10.1021/bi972948k · Cited by 21
Ab Initio Structure of the Active Site of Phosphotriesterase
Krauß, M. (2000) · Journal of Chemical Information and Computer Sciences · doi:10.1021/ci000046b · Cited by 21
Structure of the First-Shell Active Site in Metallolactamase: Effect of Water Ligands
Krauß, M., Gilson, H. S. R., & Gresh, N. (2001) · The Journal of Physical Chemistry B · doi:10.1021/jp012099h · Cited by 20
Different phosphate binding modes of Streptomyces griseus aminopeptidase between crystal and solution states and the status of zinc‐bound water
Harris, M. N., & Ming, L. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00879-0 · Cited by 20
Mg2+ Binding to Alkaline Phosphatase Correlates with Slow Changes in Protein Lability
Dirnbach, E., Steel, D. G., & Gafni, A. (2001) · Biochemistry · doi:10.1021/bi011399m · Cited by 19
Paramagnetic Cobalt(II) as a Probe for Kinetic and NMR Relaxation Studies of Phosphate Binding and the Catalytic Mechanism of Streptomyces Dinuclear Aminopeptidase
Harris, M. N., Bertolucci, C. M., & Ming, L. (2002) · Inorganic Chemistry · doi:10.1021/ic025584f · Cited by 13
ApA Cleavage Promoted by Oxa-aza Macrocycles and Their Zn(II) Complexes. The Role of pH and Metal Coordination in the Hydrolytic Mechanism
Bencini, A., Berni, E., Bianchi, A., Giorgi, C., & Valtancoli, B. (2001) · Supramolecular chemistry · doi:10.1080/10610270108029464 · Cited by 11
Glutamic acid residues as metal ligands in the active site of Escherichia coli alkaline phosphatase
Wojciechowski, C. L., & Kantrowitz, E. R. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s1570-9639(03)00156-0 · Cited by 6
Enhancement of αPNA Binding Affinity and Specificity through Hydrophobic Interactions
Garner, P., Huang, Y., & Dey, S. (2001) · ChemBioChem · doi:10.1002/1439-7633(20010302)2:3<190::aid-cbic190>3.0.co;2-7 · Cited by 4

Protein Design: Toward Functional Metalloenzymes
Yu, F., Cangelosi, V. M., Zastrow, M. L., Tegoni, M., Plegaria, J. S., Tebo, A. G., Mocny, C. S., Ruckthong, L., Qayyum, H., & Pecoraro, V. L. (2014) · Chemical Reviews · doi:10.1021/cr400458x · Cited by 441

See all 311

Authors: Weston, J.
Venue: Chemical Reviews
Publisher: American Chemical Society (ACS)
Published: 2005-03-24
Volume: 105
Issue: 6
Pages: 2151-2174
ISSN: 0009-2665 (ISSN-L)
1520-6890
DOI: 10.1021/cr020057z
OpenAlex: W1981748997
Cited by: 311
References: 142
FWCI: 0.95
Type: journal article
Language: en
Open access: closed

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

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.

Mode of Action of Bi- and Trinuclear Zinc Hydrolases and Their Synthetic Analogues

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources