Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes

Aminoacyl-S-Enzyme Intermediates in β-Hydroxylations and α,β-Desaturations of Amino Acids in Peptide Antibiotics

Chen, H., Thomas, M. G., O'Connor, S. E., et al. (2001) · Biochemistry · doi:10.1021/bi0115434 · Cited by 65

Prolyl 3‐Hydroxylase: Partial Characterization of the Enzyme from Rat Kidney Cortex

Risteli, J., Tryggvason, K., & Kivirikko, K. I. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11341.x · Cited by 63

Ferrous Active Site of Isopenicillin N Synthase: Genetic and Sequence Analysis of the Endogenous Ligands

Borovok, I., Landman, O., Kreisberg-Zakarin, R., Aharonowitz, Y., & Cohen, G. (1996) · Biochemistry · doi:10.1021/bi951534t · Cited by 63

Prolyl hydroxylase half reaction: peptidyl prolyl-independent decarboxylation of alpha-ketoglutarate.

Counts, D. F., Cardinale, G. J., & Udenfriend, S. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.5.2145 · Cited by 62

Synthesis and Characterization of Novel Alkylperoxo Mononuclear Iron(III) Complexes with a Tripodal Pyridylamine Ligand: A Model for Peroxo Intermediates in Reactions Catalyzed by Non-Heme Iron Enzymes

Wada, A., Ogo, S., Watanabe, Y., et al. (1999) · Inorganic Chemistry · doi:10.1021/ic9900298 · Cited by 62

Cloning, baculovirus expression, and characterization of the alpha subunit of prolyl 4-hydroxylase from the nematode Caenorhabditis elegans. This alpha subunit forms an active alpha beta dimer with the human protein disulfide isomerase/beta subunit.

Veijola, J., Koivunen, P., Annunen, P., Pihlajaniemi, T. A., & Kivirikko, K. I. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47082-2 · Cited by 61

Purification and properties of deacetoxycephalosporin C synthase from recombinant Escherichia coli and its comparison with the native enzyme purified from Streptomyces clavuligerus

Dotzlaf, J. E., & Yeh, W. K. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81788-4 · Cited by 60

Purification and properties of γ-butyrobetaine hydroxylase from Pseudomonas species AK 1

Lindstedt, G., Lindstedt, S., & Nordin, I. (1977) · Biochemistry · doi:10.1021/bi00629a022 · Cited by 60

Molecular characterization and expression of alfalfa (Medicago sativa L.) flavanone-3-hydroxylase and dihydroflavonol-4-reductase encoding genes

Charrier, B., Coronado, C., Kondorosi, Á., et al. (1995) · Plant Molecular Biology · doi:10.1007/bf00041167 · Cited by 59

Structure and expression of the alkB gene of Escherichia coli related to the repair of alkylated DNA.

Kondo, H., Nakabeppu, Y., Kataoka, H. C., et al. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66785-7 · Cited by 58

Utilization of Sterol Carrier Protein-2 by Phytanoyl-CoA 2-Hydroxylase in the Peroxisomal α Oxidation of Phytanic Acid

Mukherji, M., Kershaw, N. J., Schofield, C. J., Wierzbicki, A. S., & Lloyd, M. D. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00139-4 · Cited by 58

Cloning and Characterization of a Sulfonate/α-Ketoglutarate Dioxygenase from Saccharomyces cerevisiae

Hogan, D. A., Auchtung, T. A., & Hausinger, R. P. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.18.5876-5879.1999 · Cited by 58

Inactivation of 1-Aminocyclopropane-1-carboxylate Oxidase Involves Oxidative Modifications

Barlow, J. N., Zhang, Z., John, P., Baldwin, J. E., & Schofield, C. J. (1997) · Biochemistry · doi:10.1021/bi962521y · Cited by 58

Detection of Novel Proline 3-Hydroxylase Activities in Streptomyces and Bacillus spp. by Regio- and Stereospecific Hydroxylation of l-Proline

Mori, H., Shibasaki, T., Uozaki, Y., et al. (1996) · Applied and Environmental Microbiology · doi:10.1128/aem.62.6.1903-1907.1996 · Cited by 58

Bovine liver aspartyl beta-hydroxylase. Purification and characterization

Wang, Q. P., VanDusen, W. J., Petroski, C. J., Garsky, V. M., Stern, A. M., & Friedman, P. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)92802-4 · Cited by 57

Cloning and characterization of the human gene encoding aspartyl β-hydroxylase

Korioth, F., Gieffers, C., & Frey, J. (1994) · Gene · doi:10.1016/0378-1119(94)90460-x · Cited by 57

Purification and some properties of a novel ethylene-forming enzyme produced by Penicillium digitatum

Fukuda, H., Kitajima, H., Fujii, T., et al. (1989) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1989.tb03072.x · Cited by 57

A fully active catalytic domain of bovine aspartyl (asparaginyl) beta-hydroxylase expressed in Escherichia coli: characterization and evidence for the identification of an active-site region in vertebrate alpha-ketoglutarate-dependent dioxygenases.

Jia, S., McGinnis, K., VanDusen, W. J., et al. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.7227 · Cited by 56

Separation of prolyl 3-hydroxylase and 4-hydroxylase activities and the 4-hydroxyproline requirement for synthesis of 3-hydroxyproline

Tryggvason, K., Risteli, J., & Kivirikko, K. I. (1977) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(77)90722-7 · Cited by 56

Aberrant activity of the DNA repair enzyme AlkB

Henshaw, T. F., Feig, M., & Hausinger, R. P. (2003) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2003.10.021 · Cited by 56

The role of iron and 2-oxoglutarate oxygenases in signalling

Hewitson, K. S., McNeill, L. A., Elkins, J. M., et al. (2003) · Biochemical Society Transactions · doi:10.1042/bst0310510 · Cited by 55

NMR studies of the active site of isopenicillin N synthase, a non-heme iron(II) enzyme

Ming, L. J., QUE, L. J., Kriauciunas, A., et al. (1991) · Biochemistry · doi:10.1021/bi00114a007 · Cited by 55

4-Hydroxyphenylpyruvate dioxygenase is an iron-tyrosinate protein.

Bradley, F. C., Lindstedt, S., Lipscomb, J. D., et al. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67299-0 · Cited by 54

Product-substrate engineering by bacteria: Studies on clavaminate synthase, a trifunctional dioxygenase

Lloyd, M. D., Merritt, K. D., Lee, V., et al. (1999) · Tetrahedron · doi:10.1016/s0040-4020(99)00547-5 · Cited by 54

Probing the Structure and Function of theEscherichia coliDNA Alkylation Repair AlkB Protein through Chemical Cross-Linking

Mishina, Y., & He, C. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034636c · Cited by 54

Carnitine Biosynthesis: Identification of the cDNA Encoding Human γ-Butyrobetaine Hydroxylase

Vaz, F. M., van Gool, S., Ofman, R., IJlst, L., & Wanders, R. J. A. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9343 · Cited by 54

Resolution of the Phytanic Acid α-Oxidation Pathway: Identification of Pristanal as Product of the Decarboxylation of 2-Hydroxyphytanoyl-CoA

Verhoeven, N. M., Schor, D. S. M., ten Brink, H. J., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7066 · Cited by 54

Interconversion of two oxidized forms of taurine/α-ketoglutarate dioxygenase, a non-heme iron hydroxylase: Evidence for bicarbonate binding

Ryle, M. J., Koehntop, K. D., Liu, A., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0636740100 · Cited by 53

Recent advances in gibberellin biosynthesis

Hedden, P. (1999) · Journal of Experimental Botany · doi:10.1093/jxb/50.334.553 · Cited by 53

Cloning and expression of a gibberellin 2 beta,3 beta-hydroxylase cDNA from pumpkin endosperm.

Lange, T., Robatzek, S., & Frisse, A. (1997) · The Plant Cell · doi:10.1105/tpc.9.8.1459 · Cited by 53

Partial reaction of prolyl hydroxylase. (Gly-PRO-Ala)n stimulates alpha-ketoglutarate decarboxylation without prolyl hydroxylation.

Rao, N. V., & Adams, E. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)46933-0 · Cited by 52

Mechanism of .alpha.-ketoglutarate oxidation in coupled enzymic oxygenations

Lindblad, B., Lindstedt, G., Tofft, M., et al. (1969) · Journal of the American Chemical Society · doi:10.1021/ja01044a082 · Cited by 52

Production of formyl‐CoA during peroxisomal α‐oxidation of 3‐methyl‐branched fatty acids

Croes, K., Veldhoven, P. P. V., Mannaerts, G. P., & Casteels, M. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00343-8 · Cited by 52

Resonance Raman evidence for the interconversion between an [FeIII–η1-OOH] 2+ and [FeIII–η2-O2]+ species and mechanistic implications thereof

Ho, R. Y. N., Que, L., Jr., Roelfes, G., et al. (1999) · Chemical Communications · doi:10.1039/a905535e · Cited by 52

Reversal of the Deoxyhypusine Synthesis Reaction

Park, J., Park, J.-H., Wolff, E. C., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304247200 · Cited by 52

Site-directed Mutagenesis of 2,4-Dichlorophenoxyacetic Acid/α-Ketoglutarate Dioxygenase

Hogan, D. A., Smith, S. R., Saari, E. A., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.17.12400 · Cited by 51

Resonance Raman Studies of the Iron(II)−α-Keto Acid Chromophore in Model and Enzyme Complexes

Ho, R. Y. N., Mehn, M. P., Hegg, E. L., Liu, A., Ryle, M. J., Hausinger, R. P., & QUE, L. J. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0041775 · Cited by 51

Molecular and Biochemical Characterization of Rat ε-N-Trimethyllysine Hydroxylase, the First Enzyme of Carnitine Biosynthesis

Vaz, F. M., Ofman, R., Westinga, K., Back, J. W., & Wanders, R. J. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105929200 · Cited by 50

Site-Directed Mutagenesis of Residues in a Conserved Region of Bovine Aspartyl (Asparaginyl) β-Hydroxylase: Evidence That Histidine 675 Has a Role in Binding Fe2+

McGinnis, K., Ku, G., VanDusen, W. J., Fu, J., Garsky, V. M., Stern, A. M., & Friedman, P. A. (1996) · Biochemistry · doi:10.1021/bi951520n · Cited by 50

The mechanism of alpha-ketoisocaproate oxygenase. Formation of beta-hydroxyisovalerate from alpha-ketoisocaproate.

Sabourin, P. J., & BIEBER, L. L. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34401-6 · Cited by 49

Novel Flavonol 2-Oxoglutarate Dependent Dioxygenase: Affinity Purification, Characterization, and Kinetic Properties

Anzellotti, D., & Ibrahim, R. K. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.2002 · Cited by 49

Purification and properties of the apple fruit ethylene-forming enzyme

Pirrung, M. C., Kaiser, L. M., & Chen, J. (1993) · Biochemistry · doi:10.1021/bi00080a015 · Cited by 49

X-ray absorption spectroscopic studies of the high-spin iron(II) active site of isopenicillin N synthase: evidence for iron-sulfur interaction in the enzyme-substrate complex

Scott, R. A., Wang, S., Eidsness, M. K., et al. (1992) · Biochemistry · doi:10.1021/bi00134a009 · Cited by 49

The oxidases of gibberellin biosynthesis: Their function and mechanism

Hedden, P. (1997) · Physiologia Plantarum · doi:10.1111/j.1399-3054.1997.tb01055.x · Cited by 49

The C-4 stereochemistry of leucocyanidin substrates for anthocyanidin synthase affects product selectivity

Turnbull, J. J., Nagle, M. J., Seibel, J., Welford, R. W. D., Grant, G. H., & Schofield, C. J. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(03)00711-x · Cited by 48

A mechanistic rationalisation for the substrate specificity of recombinant mammalian 4-hydroxyphenylpyruvate dioxygenase (4-HPPD)

Crouch, N. P., Adlington, R. M., Baldwin, J. E., Lee, M. H., & MacKinnon, C. H. (1997) · Tetrahedron · doi:10.1016/s0040-4020(97)00398-0 · Cited by 48

Formation of a 2‐methyl‐branched fatty aldehyde during peroxisomal α‐oxidation

Croes, K., Casteels, M., Asselberghs, S., Herdewijn, P. A., Mannaerts, G. P., & Veldhoven, P. P. V. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00856-9 · Cited by 48

Preparation of a cell-free ethylene-forming system from Penicillium digitatum.

Fukuda, H., FUJII, T., & Ogawa, T. (1986) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.50.977 · Cited by 48

Alternative oxidation by isopenicillin N synthase observed by X-ray diffraction

Ogle, J. M., Clifton, I. J., Rutledge, P. J., et al. (2001) · Chemistry & Biology · doi:10.1016/s1074-5521(01)00090-4 · Cited by 47

Identification and cloning of genes encoding viomycin biosynthesis from Streptomyces vinaceus and evidence for involvement of a rare oxygenase

Yin, X., O'Hare, T., Gould, S. J., et al. (2003) · Gene · doi:10.1016/s0378-1119(03)00617-6 · Cited by 46

Cofactor requirements of thymine 7-hydroxylase

Abbott, M. T., Schandl, E. K., Lee, R. F., et al. (1967) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(67)90177-5 · Cited by 46

Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874.

Lindstedt, S., & Rundgren, M. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33654-8 · Cited by 45

Purification and partial amino-acid sequence of gibberellin 20-oxidase from Cucurbita maxima L. endosperm

Lange, T. (1994) · Planta · doi:10.1007/bf00206298 · Cited by 45

Characterization of a dioxygenase from Trigonella foenum-graecum involved in 4-hydroxyisoleucine biosynthesis

Haefelé, C., Bonfils, C., & Sauvaire, Y. D. (1997) · Phytochemistry · doi:10.1016/s0031-9422(96)00620-6 · Cited by 45

The biosynthesis of the streptolidine moiety in streptothricin F

Martinkus, K. J., Tann, C., & Gould, S. J. (1983) · Tetrahedron · doi:10.1016/s0040-4020(01)88659-2 · Cited by 44

Steady-State Kinetics of Substrate Binding and Iron Release in Tomato ACC Oxidase

Thrower, J. S., Blalock, R., & Klinman, J. P. (2001) · Biochemistry · doi:10.1021/bi010329c · Cited by 44

Coordination chemistry of the metal binding site of isopenicillin N synthase

Ming, L. J., QUE, L. J., Kriauciunas, A., et al. (1990) · Inorganic Chemistry · doi:10.1021/ic00331a001 · Cited by 44

Purification and Characterization of Clavaminate Synthase from Streptomyces antibioticus

Janc, J. W., Egan, L. A., & Townsend, C. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5399 · Cited by 44

Phytanoyl-CoA hydroxylase: recognition of 3-methyl-branched acyl-CoAs and requirement for GTP or ATP and Mg2+ in addition to its known hydroxylation cofactors

Croes, K., Foulon, V., Casteels, M., Veldhoven, P. P. V., & Mannaerts, G. P. (2000) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)32411-1 · Cited by 44

Separation and characterisation of three 2-oxoglutarate-dependent dioxygenases from Cucurbita maxima L. endosperm involved in gibberellin biosynthesis

Lange, T., Schweimer, A., Ward, D. A., et al. (1994) · Planta · doi:10.1007/bf00206297 · Cited by 43

Glutamine‐330 is not essential for activity in isopenicillin N synthase from Aspergillus nidulans

Sami, M., Brown, T. J. N., Roach, P. L., et al. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00176-2 · Cited by 43

The active site of deoxyhypusyl hydroxylase: use of catecholpeptides and their component chelator and peptide moieties as molecular probes

Abbruzzese, A., Hanauske-Abel, H. M., Park, M. H., Henke, S., & Folk, J. E. (1991) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(91)90053-3 · Cited by 43

Functional Analysis of Conserved Histidine Residues in Cephalosporium acremonium Isopenicillin N Synthase by Site-directed Mutagenesis

Tan, D. S. H., & Sim, T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.2.889 · Cited by 43

Purification of Recombinant Flavanone 3β-Hydroxylase from Petunia hybrida and Assignment of the Primary Site of Proteolytic Degradation

Lukačin, R., Gröning, I., Schiltz, E., Britsch, L., & Matern, U. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1676 · Cited by 43

Expression and Purification of Two Isozymes of Clavaminate Synthase and Initial Characterization of the Iron Binding Site

Busby, R. W., Chang, M. D.-T., Busby, R. C., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.9.4262 · Cited by 41

Cloning of the α Subunit of Prolyl 4-Hydroxylase fromDrosophila and Expression and Characterization of the Corresponding Enzyme Tetramer with Some Unique Properties

Annunen, P., Koivunen, P., & Kivirikko, K. I. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6790 · Cited by 41

Characterization of the Ferrous Ion Binding Sites of Apple 1-Aminocyclopropane-1-carboxylate Oxidase by Site-Directed Mutagenesis

Shaw, J. F., Chou, Y.-S., Chang, R., et al. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1237 · Cited by 41

Novel Chiral Pyridine N-Oxide Ligands and Their Application in the Enantioselective Catalytic Reduction of Ketones and the Addition of Diethylzinc to Aldehydes

Derdau, V., Laschat, S., Hupe, E., König, W. Α., Dix, I., & Jones, P. G. (1999) · European Journal of Inorganic Chemistry · doi:10.1002/(sici)1099-0682(199906)1999:6 · Cited by 41

α-KETOGLUTARATE-COUPLED DIOXYGENASES

Abbott, M. T., & Udenfriend, S. (1974) · Elsevier eBooks · doi:10.1016/b978-0-12-333640-8.50010-1 · Cited by 41

Heterologous Expression and Site‐Directed Mutagenesis of the 1‐Aminocyclopropane‐1‐Carboxylate Oxidase from Kiwi Fruit

Lay, V. J., Prescott, A. G., Thomas, P. G., et al. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0228r.x · Cited by 40

Cloning, Sequencing, and Function of sanF : A Gene Involved in Nikkomycin Biosynthesis of Streptomyces ansochromogenes

Chen, W., Zeng, H., & Tan, H. (2000) · Current Microbiology · doi:10.1007/s002840010141 · Cited by 40

Deacetoxycephalosporin C hydroxylase of Streptomyces clavuligerus. Purification, characterization, bifunctionality, and evolutionary implication.

Baker, B. J., Dotzlaf, J. E., & Yeh, W. K. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67759-8 · Cited by 39

Site‐directed mutagenesis of the active site serine290 in flavanone 3β‐hydroxylase from Petunia hybrida

Lukačin, R., Gröning, I., Pieper, U., & Matern, U. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01064.x · Cited by 39

Biodegradation of the chlorophenoxy herbicide (R)-(+)-mecoprop by Alcaligenes denitrificans

Tett, V. A., Willetts, A., & Lappin-Scott, H. M. (1997) · Biodegradation · doi:10.1023/a:1008262901202 · Cited by 39

Purification and properties of calf liver γ-butyrobetaine hydroxylase

Kondo, A., Blanchard, J. S., & Englard, S. (1981) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(81)90374-x · Cited by 39

18O Studies of the 2-Ketoglutarate-dependent Sequential Oxygenation of Thymine to 5-Carboxyuracil

Holme, E., Lindstedt, G., Lindstedt, S., et al. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62229-x · Cited by 38

Partial purification and characterization of chick-embryo prolyl 3-hydroxylase

Tryggvason, K., Majamaa, K., Risteli, J., et al. (1979) · Biochemical Journal · doi:10.1042/bj1830303 · Cited by 37

Identification of arginine‐700 as the residue that binds the C‐5 carboxyl group of 2‐oxoglutarate in human lysyl hydroxylase 1

Passoja, K., Myllyharju, J., Pirskanen, A., et al. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00966-1 · Cited by 37

Purification and Characterisation of the Enantiospecific Dioxygenases from Delftia acidovorans MC1 Initiating the Degradation of Phenoxypropionate and Phenoxyacetate Herbicides

Westendorf, A., Müller, R., & Babel, W. (2003) · Acta Biotechnologica · doi:10.1002/abio.200390006 · Cited by 37

Alteration of the Co-substrate Selectivity of Deacetoxycephalosporin C Synthase

Lee, H., Lloyd, M. D., Clifton, I. J., Harlos, K., Dubus, A., Baldwin, J. E., Frère, J., & Schofield, C. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100085200 · Cited by 37

Controlling the Substrate Selectivity of Deacetoxycephalosporin/deacetylcephalosporin C Synthase

Lloyd, M. D., Lipscomb, S. J., Hewitson, K. S., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313928200 · Cited by 36

Incorporation of 18O-labelled water into oxygenated products produced by the enzyme deacetoxy/deacetylcephalosporin C synthase

Baldwin, J. E., Adlington, R. M., Crouch, N. P., et al. (1993) · Tetrahedron · doi:10.1016/s0040-4020(01)87226-4 · Cited by 36

Stereospecific degradation of the phenoxypropionate herbicide dichlorprop

Saari, R. E., Hogan, D. A., & Hausinger, R. P. (1999) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/s1381-1177(99)00008-9 · Cited by 35

Gene organization in the bleomycin-resistance region of the producer organism Streptomyces verticillus

Calcutt, M. J., & Schmidt, F. J. (1994) · Gene · doi:10.1016/0378-1119(94)90627-0 · Cited by 35

l-Arginine is essential for the formation in vitro of ethylene by an extract of Pseudomonas syringae

Nagahama, K., Ogawa, T., Fujii, T., et al. (1991) · Journal of General Microbiology · doi:10.1099/00221287-137-7-1641 · Cited by 35

The cell-free conversion of a deoxyribonucleoside to a ribonucleoside without detachment of the deoxyribose

Shaffer, P. M., McCroskey, R. P., Palmatier, R. D., et al. (1968) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(68)90232-5 · Cited by 35

Thymidine 2′-Hydroxylation in Neurospora crassa

Bankel, L., Lindstedt, G., & Lindstedt, S. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44773-x · Cited by 34

Electron spin echo envelope modulation studies of the copper(II)-substituted derivative of isopenicillin N synthase: a structural and spectroscopic model

Jiang, F., Peisach, J., Li, M., et al. (1991) · Biochemistry · doi:10.1021/bi00112a010 · Cited by 33

Metal Coordination Environment of a Cu(II)-Substituted α-Keto Acid-Dependent Dioxygenase That Degrades the Herbicide 2,4-D

Whiting, A. K., QUE, L. J., Saari, R. E., et al. (1997) · Journal of the American Chemical Society · doi:10.1021/ja964449x · Cited by 33

Structural studies on the reaction of isopenicillin N synthase with the substrate analogue delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-alpha-aminobutyrate

Long, A. J., Clifton, I. J., Roach, P. L., et al. (2003) · Biochemical Journal · doi:10.1042/bj20021627 · Cited by 33

Prolyl 4-hydroxylase from Volvox carteri. A low-Mr enzyme antigenically related to the α subunit of the vertebrate enzyme

Kaska, D. D., Myllylä, R., Günzler, V., et al. (1988) · Biochemical Journal · doi:10.1042/bj2560257 · Cited by 33

Isolation and Biochemical Characterization of Hypophosphite/ 2-Oxoglutarate Dioxygenase

White, A. K., & Metcalf, W. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204605200 · Cited by 31

‘Chemical co-substrate rescue’ of phytanoyl-CoA 2-hydroxylase mutants causing Refsum’s Disease

Mukherji, M., Kershaw, N. J., MacKinnon, C. H., et al. (2001) · Chemical Communications · doi:10.1039/b101039p · Cited by 31

Novel proline hydroxylase activities in the pneumocandin-producing fungus Glarea lozoyensis responsible for the formation of trans 3- and trans 4-hydroxyproline

Petersen, L., Olewinski, R., Salmon, P. J., et al. (2003) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-003-1264-0 · Cited by 30

The glutamine ligand in the ferrous iron active site of isopenicillin N synthase of Streptomyces jumonjinensis is not essential for catalysis

Landman, O., Borovok, I., Aharonowitz, Y., et al. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00180-4 · Cited by 30

Interaction of human and bacterial AlkB proteins with DNA as probed through chemical cross-linking studies

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The source of oxygen in the reaction catalysed by collagen lysyl hydroxylase

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