EC number:1.14.15.35

Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.15.35
Description:6-deoxyerythronolide B hydroxylase.
Alternative Name: DEB hydroxylase.
CYP107A1.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.15.35
BRENDA Enzyme Link: BRENDA 1.14.15.35
KEGG Enzyme Link: KEGG1.14.15.35
BioCyc Enzyme Link: BioCyc 1.14.15.35
ExPASy Enzyme Link: ExPASy1.14.15.35
EC2PDB Enzyme Link: EC2PDB 1.14.15.35
ExplorEnz Enzyme Link: ExplorEnz 1.14.15.35
PRIAM enzyme-specific profiles Link: PRIAM 1.14.15.35
IntEnz Enzyme Link: IntEnz 1.14.15.35
MEDLINE Enzyme Link: MEDLINE 1.14.15.35

EC number:1.14.15.35

MSA:

1.14.15.35;
Phylogenetic Tree:

1.14.15.35;
Uniprot:
M-CSA:
RHEA:40299 6-deoxyerythronolide B + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = erythronolide B + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[*:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[C;H0;+0:8](-[*:9])-[CH2;+0:10]-[CH;+0:11]=[CH;+0:12]-1.[H+;H0:13].[O;H0;+0:14]=[O;H0;+0:15]>>[*:1]-[C;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:14].[*:5]-[n+;H0:6]1:[cH;+0:7]:[c;H0;+0:8](-[*:9]):[cH;+0:10]:[cH;+0:11]:[cH;+0:12]:1.[OH2;+0:15]
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References

TitleAuthorsDatePubMed ID
Macrolide antibiotic biosynthesis: isolation and properties of two forms of 6-deoxyerythronolide B hydroxylase from Saccharopolyspora erythraea (Streptomyces erythreus).Shafiee A, Hutchinson CR1987 Sep 222446657
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.Nagano S, Cupp-Vickery JR, Poulos TL2005 Jun 1015824115