KEGG   ENZYME: 1.14.15.34
Entry
EC 1.14.15.34               Enzyme                                 
Name
20-oxo-5-O-mycaminosyltylactone 23-monooxygenase;
tylH1 (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
20-oxo-5-O-beta-mycaminosyltylactone,reduced ferredoxin:oxygen oxidoreductase (23-hydroxylating)
Reaction(IUBMB)
20-oxo-5-O-beta-mycaminosyltylactone + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 5-O-beta-mycaminosyltylonolide + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O [RN:R10656]
Reaction(KEGG)
R10656
Substrate
20-oxo-5-O-beta-mycaminosyltylactone [CPD:C20760];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
5-O-beta-mycaminosyltylonolide;
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139];
H2O [CPD:C00001]
Comment
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.
History
EC 1.14.15.34 created 2014 as EC 1.14.13.186, transferred 2018 to EC 1.14.15.34
Pathway
ec00522  Biosynthesis of 12-, 14- and 16-membered macrolides
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K15991  20-oxo-5-O-mycaminosyltylactone 23-monooxygenase
Genes
STREGZL_03700
STRMM444_29910
Reference
1  [PMID:7283418]
  Authors
Baltz RH, Seno ET
  Title
Properties of Streptomyces fradiae mutants blocked in biosynthesis of the macrolide antibiotic tylosin.
  Journal
Antimicrob Agents Chemother 20:214-25 (1981)
DOI:10.1128/AAC.20.2.214
  Sequence
Reference
2  [PMID:15489173]
  Authors
Reeves CD, Ward SL, Revill WP, Suzuki H, Marcus M, Petrakovsky OV, Marquez S, Fu H, Dong SD, Katz L
  Title
Production of hybrid 16-membered macrolides by expressing combinations of polyketide synthase genes in engineered Streptomyces fradiae hosts.
  Journal
Chem Biol 11:1465-72 (2004)
DOI:10.1016/j.chembiol.2004.08.019
Other DBs
ExplorEnz - The Enzyme Database: 1.14.15.34
IUBMB Enzyme Nomenclature: 1.14.15.34
ExPASy - ENZYME nomenclature database: 1.14.15.34
BRENDA, the Enzyme Database: 1.14.15.34

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