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:1.14.15.34
Description:20-oxo-5-O-mycaminosyltylactone 23-monooxygenase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.15.34
BRENDA Enzyme Link: BRENDA 1.14.15.34
KEGG Enzyme Link: KEGG1.14.15.34
BioCyc Enzyme Link: BioCyc 1.14.15.34
ExPASy Enzyme Link: ExPASy1.14.15.34
EC2PDB Enzyme Link: EC2PDB 1.14.15.34
ExplorEnz Enzyme Link: ExplorEnz 1.14.15.34
PRIAM enzyme-specific profiles Link: PRIAM 1.14.15.34
IntEnz Enzyme Link: IntEnz 1.14.15.34
MEDLINE Enzyme Link: MEDLINE 1.14.15.34
MSA:

1.14.15.34;

Phylogenetic Tree:

1.14.15.34;

Uniprot:
M-CSA:
RHEA:24524 20-oxo-5-O-beta-D-mycaminosyltylonolide + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 5-O-beta-D-mycaminosyltylonolide + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
RULE(radius=1) [*:1]-[CH3;+0:2].[*:3]-[N;H0;+0:4]1-[CH;+0:5]=[C;H0;+0:6](-[*:7])-[CH2;+0:8]-[CH;+0:9]=[CH;+0:10]-1.[H+;H0:11].[O;H0;+0:12]=[O;H0;+0:13]>>[*:1]-[CH2;+0:2]-[OH;+0:12].[*:3]-[n+;H0:4]1:[cH;+0:5]:[c;H0;+0:6](-[*:7]):[cH;+0:8]:[cH;+0:9]:[cH;+0:10]:1.[OH2;+0:13]
Reaction
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References

TitleAuthorsDatePubMed ID
Properties of Streptomyces fradiae mutants blocked in biosynthesis of the macrolide antibiotic tylosin.Baltz RH, Seno ET1981 Aug7283418
Production of hybrid 16-membered macrolides by expressing combinations of polyketide synthase genes in engineered Streptomyces fradiae hosts.Reeves CD, Ward SL, Revill WP, Suzuki H, Marcus M, Petrakovsky OV, Marquez S, Fu H, Dong SD, Katz L2004 Oct15489173