The Enzyme Database

Your query returned 7 entries.    printer_iconPrintable version



EC 1.14.15.3     
Accepted name: alkane 1-monooxygenase
Reaction: octane + 2 reduced rubredoxin + O2 + 2 H+ = 1-octanol + 2 oxidized rubredoxin + H2O
Other name(s): alkane 1-hydroxylase; ω-hydroxylase; fatty acid ω-hydroxylase; alkane monooxygenase; 1-hydroxylase; alkane hydroxylase
Systematic name: alkane,reduced-rubredoxin:oxygen 1-oxidoreductase
Comments: Some enzymes in this group are heme-thiolate proteins (P-450). Also hydroxylates fatty acids in the ω-position.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 9059-16-9
References:
1.  Cardini, G. and Jurtshuk, P. The enzymatic hydroxylation of n-octane by Corynebacterium sp. strain 7E1C. J. Biol. Chem. 245 (1970) 2789–2796. [PMID: 4317878]
2.  McKenna, E.J. and Coon, M.J. Enzymatic ω-oxidation. IV. Purification and properties of the ω-hydroxylase of Pseudomonas oleovorans. J. Biol. Chem. 245 (1970) 3882–3889. [PMID: 4395379]
3.  Peterson, J.A., Kusunose, M., Kusunose, E. and Coon, M.J. Enzymatic ω-oxidation. II. Function of rubredoxin as the electron carrier in ω-hydroxylation. J. Biol. Chem. 242 (1967) 4334–4340. [PMID: 4294330]
[EC 1.14.15.3 created 1972]
 
 
EC 1.14.15.30     
Accepted name: 3-ketosteroid 9α-monooxygenase
Reaction: androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9α-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Other name(s): KshA; 3-ketosteroid 9α-hydroxylase
Systematic name: androsta-1,4-diene-3,17-dione,[reduced ferredoxin]:oxygen oxidoreductase (9α-hydroxylating)
Comments: The enzyme is involved in the cholesterol degradation pathway of several bacterial pathogens, such as Mycobacterium tuberculosis. It forms a two-component system with a ferredoxin reductase (KshB). The enzyme contains a Rieske-type iron-sulfur center and non-heme iron. The product of the enzyme is unstable, and spontaneously converts to 3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD
References:
1.  Petrusma, M., Dijkhuizen, L. and van der Geize, R. Rhodococcus rhodochrous DSM 43269 3-ketosteroid 9α-hydroxylase, a two-component iron-sulfur-containing monooxygenase with subtle steroid substrate specificity. Appl. Environ. Microbiol. 75 (2009) 5300–5307. [DOI] [PMID: 19561185]
2.  Capyk, J.K., D'Angelo, I., Strynadka, N.C. and Eltis, L.D. Characterization of 3-ketosteroid 9α-hydroxylase, a Rieske oxygenase in the cholesterol degradation pathway of Mycobacterium tuberculosis. J. Biol. Chem. 284 (2009) 9937–9946. [DOI] [PMID: 19234303]
3.  Capyk, J.K., Casabon, I., Gruninger, R., Strynadka, N.C. and Eltis, L.D. Activity of 3-ketosteroid 9α-hydroxylase (KshAB) indicates cholesterol side chain and ring degradation occur simultaneously in Mycobacterium tuberculosis. J. Biol. Chem. 286 (2011) 40717–40724. [DOI] [PMID: 21987574]
[EC 1.14.15.30 created 2012 as EC 1.14.13.142, transferred 2018 to EC 1.14.15.30]
 
 
EC 1.14.15.31     
Accepted name: 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase
Reaction: 2-hydroxy-5-methyl-1-naphthoate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 2,7-dihydroxy-5-methyl-1-naphthoate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
For diagram of neocarzinostatin biosynthesis, click here
Other name(s): NcsB3
Systematic name: 2-hydroxy-5-methyl-1-naphthoate,reduced ferredoxin:oxygen oxidoreductase (7-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein involved in the synthesis of neocarzinostatin in the bacterium Streptomyces carzinostaticus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hang, V.T.T., Oh, T.J., Yamaguchi, T. and Sohng, J.K. In vivo characterization of NcsB3 to establish the complete biosynthesis of the naphthoic acid moiety of the neocarzinostatin chromophore. FEMS Microbiol. Lett. 311 (2010) 119–125. [DOI] [PMID: 20735485]
[EC 1.14.15.31 created 2014 as EC 1.14.99.49, transferred 2018 to EC 1.14.15.31]
 
 
EC 1.14.15.32     
Accepted name: pentalenene oxygenase
Reaction: pentalenene + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + 2 O2 = pentalen-13-al + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O (overall reaction)
(1a) pentalenene + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = pentalen-13-ol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1b) pentalen-13-ol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = pentalen-13-al + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
For diagram of humulene-based sequiterpenoid biosynthesis, click here
Other name(s): PtlI
Systematic name: pentalenene,reduced ferredoxin:oxygen 13-oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein found in the bacterium Streptomyces avermitilis. The enzyme is involved in the biosynthesis of pentalenolactone and related antibiotics.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Quaderer, R., Omura, S., Ikeda, H. and Cane, D.E. Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlI, a cytochrome P450 of Streptomyces avermitilis. J. Am. Chem. Soc. 128 (2006) 13036–13037. [DOI] [PMID: 17017767]
[EC 1.14.15.32 created 2011 as EC 1.14.13.133, transferred 2018 to EC 1.14.15.32]
 
 
EC 1.14.15.33     
Accepted name: pikromycin synthase
Reaction: (1) narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = pikromycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(2) narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = neopikromycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(3) narbomycin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + 2 O2 = novapikromyin + 4 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
(4) 10-deoxymethymycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = methymycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(5) 10-deoxymethymycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = neomethymycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(6) 10-deoxymethymycin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + 2 O2 = novamethymycin + 4 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
For diagram of pikromycin biosynthesis, click here
Other name(s): PikC; CYP107L1
Systematic name: narbomycin,reduced ferredoxin:oxygen oxidoreductase (pikromycin-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Involved in the biosynthesis of a number of bacterial macrolide antibiotics containing a desosamine glycoside unit. With narbomycin it hydroxylates at either C-12 to give pikromycin or C-14 to give neopikromycin or both positions to give narvopikromycin. With 10-deoxymethymycin it hydroxylates at either C-10 to give methymycin or C-12 to give neomethymycin or both positions to give novamethymycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Xue, Y., Wilson, D., Zhao, L., Liu Hw and Sherman, D.H. Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae. Chem. Biol. 5 (1998) 661–667. [DOI] [PMID: 9831532]
2.  Sherman, D.H., Li, S., Yermalitskaya, L.V., Kim, Y., Smith, J.A., Waterman, M.R. and Podust, L.M. The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae. J. Biol. Chem. 281 (2006) 26289–26297. [DOI] [PMID: 16825192]
3.  Li, S., Ouellet, H., Sherman, D.H. and Podust, L.M. Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae. J. Biol. Chem. 284 (2009) 5723–5730. [DOI] [PMID: 19124459]
[EC 1.14.15.33 created 2014 as EC 1.14.13.185, transferred 2018 to EC 1.14.15.33]
 
 
EC 1.14.15.34     
Accepted name: 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase
Reaction: 20-oxo-5-O-β-mycaminosyltylactone + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 5-O-β-mycaminosyltylonolide + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
For diagram of tylosin biosynthesis, click here
Glossary: tylactone = (4R,5S,6S,7S,9R,11E,13E,15S,16R)-7,16-diethyl-4,6-dihydroxy-5,9,13,15-tetramethyl-1-oxacyclohexadeca-11,13-diene-2,10-dione
α-D-mycaminose = 3-dimethylamino-3,6-dideoxy-α-D-glucopyranose
tylonolide = 2-[(4R,5S,6S,7R,9R,11E,13E,15R,16R)-16-ethyl-4,6-dihydroxy-15-(hydroxymethyl)-5,9,13-trimethyl-2,10-dioxo-1-oxacyclohexadeca-11,13-dien-7-yl]acetaldehyde
Other name(s): tylH1 (gene name)
Systematic name: 20-oxo-5-O-β-mycaminosyltylactone,reduced ferredoxin:oxygen oxidoreductase (23-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. Involved in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Baltz, R.H. and Seno, E.T. Properties of Streptomyces fradiae mutants blocked in biosynthesis of the macrolide antibiotic tylosin. Antimicrob. Agents Chemother. 20 (1981) 214–225. [PMID: 7283418]
2.  Reeves, C.D., Ward, S.L., Revill, W.P., Suzuki, H., Marcus, M., Petrakovsky, O.V., Marquez, S., Fu, H., Dong, S.D. and Katz, L. Production of hybrid 16-membered macrolides by expressing combinations of polyketide synthase genes in engineered Streptomyces fradiae hosts. Chem. Biol. 11 (2004) 1465–1472. [DOI] [PMID: 15489173]
[EC 1.14.15.34 created 2014 as EC 1.14.13.186, transferred 2018 to EC 1.14.15.34]
 
 
EC 1.14.15.35     
Accepted name: 6-deoxyerythronolide B hydroxylase
Reaction: 6-deoxyerythronolide B + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = erythronolide B + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
For diagram of erythromycin biosynthesis, click here
Other name(s): DEB hydroxylase; eryF (gene name); P450(eryF); CYP107A1
Systematic name: 6-deoxyerythronolide-B,reduced ferredoxin:oxygen oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the bacterium Saccharopolyspora erythraea. The enzyme is involved in the biosynthesis of the antibiotic erythromycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Weber, J.M., Leung, J.O., Swanson, S.J., Idler, K.B. and McAlpine, J.B. An erythromycin derivative produced by targeted gene disruption in Saccharopolyspora erythraea. Science 252 (1991) 114–117. [DOI] [PMID: 2011746]
2.  Shafiee, A. and Hutchinson, C.R. Macrolide antibiotic biosynthesis: isolation and properties of two forms of 6-deoxyerythronolide B hydroxylase from Saccharopolyspora erythraea (Streptomyces erythreus). Biochemistry 26 (1987) 6204–6210. [PMID: 2446657]
3.  Cupp-Vickery, J.R., Li, H. and Poulos, T.L. Preliminary crystallographic analysis of an enzyme involved in erythromycin biosynthesis: cytochrome P450eryF. Proteins: Struct., Funct., Bioinf. 20 (1994) 197–201. [DOI] [PMID: 7846029]
4.  Nagano, S., Cupp-Vickery, J.R. and Poulos, T.L. Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T: investigation of the proton transfer system in P450eryF. J. Biol. Chem. 280 (2005) 22102–22107. [DOI] [PMID: 15824115]
[EC 1.14.15.35 created 2014 as EC 1.14.13.188, transferred 2018 to EC 1.14.15.35]
 
 


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