KEGG   ENZYME: 1.14.13.154Help
Entry
EC 1.14.13.154              Enzyme                                 

Name
erythromycin 12-hydroxylase;
EryK
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
erythromycin-D,NADPH:oxygen oxidoreductase (12-hydroxylating)
Reaction(IUBMB)
erythromycin D + NADPH + H+ + O2 = erythromycin C + NADP+ + H2O [RN:R05522]
Reaction(KEGG)
R05522;
(other) R05521
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Substrate
erythromycin D [CPD:C06633];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
erythromycin C [CPD:C06616];
NADP+ [CPD:C00006];
H2O [CPD:C00001]
Comment
The enzyme is responsible for the C-12 hydroxylation of the macrolactone ring, one of the last steps in erythromycin biosynthesis. It shows 1200-1900-fold preference for erythromycin D over the alternative substrate erythromycin B [1].
History
EC 1.14.13.154 created 2012
Pathway
ec00522  Biosynthesis of 12-, 14- and 16-membered macrolides
ec01130  Biosynthesis of antibiotics
Orthology
K14370  erythromycin 12 hydroxylase
Genes
SEN: SACE_0713(eryK)
Taxonomy
Reference
1  [PMID:7849045]
  Authors
Lambalot RH, Cane DE, Aparicio JJ, Katz L
  Title
Overproduction and characterization of the erythromycin C-12 hydroxylase, EryK.
  Journal
Biochemistry 34:1858-66 (1995)
  Sequence
[sen:SACE_0713]
Reference
2  [PMID:19625248]
  Authors
Savino C, Montemiglio LC, Sciara G, Miele AE, Kendrew SG, Jemth P, Gianni S, Vallone B.
  Title
Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate.
  Journal
J Biol Chem 284:29170-9 (2009)
DOI:10.1074/jbc.M109.003590
  Sequence
[sen:SACE_0713]
Reference
3  [PMID:20845962]
  Authors
Montemiglio LC, Gianni S, Vallone B, Savino C
  Title
Azole drugs trap cytochrome P450 EryK in alternative conformational states.
  Journal
Biochemistry 49:9199-206 (2010)
DOI:10.1021/bi101062v
  Sequence
[sen:SACE_0713]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.154
IUBMB Enzyme Nomenclature: 1.14.13.154
ExPASy - ENZYME nomenclature database: 1.14.13.154
BRENDA, the Enzyme Database: 1.14.13.154

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