KEGG   ENZYME: 1.14.11.35Help
Entry
EC 1.14.11.35               Enzyme                                 

Name
1-deoxypentalenic acid 11beta-hydroxylase;
ptlH (gene name);
sav2991 (gene name);
pntH (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
BRITE hierarchy
Sysname
1-deoxypentalenic acid,2-oxoglutarate:oxygen oxidoreductase
Reaction(IUBMB)
1-deoxypentalenate + 2-oxoglutarate + O2 = 1-deoxy-11beta-hydroxypentalenate + succinate + CO2 [RN:R10157]
Reaction(KEGG)
Substrate
1-deoxypentalenate [CPD:C20404];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]
Product
1-deoxy-11beta-hydroxypentalenate [CPD:C20403];
succinate [CPD:C00042];
CO2 [CPD:C00011]
Comment
The enzyme requires Fe(II) and ascorbate. Isolated from the bacterium Streptomyces avermitilis. Part of the pathway for pentalenolactone biosynthesis.
History
EC 1.14.11.35 created 2012
Pathway
Biosynthesis of antibiotics
Orthology
K18056  
1-deoxypentalenic acid 11beta-hydroxylase
Genes
SMA: 
SAV_2991(ptlH)
SBH: 
SCI: 
SCW: 
Taxonomy
Reference
1  [PMID:16704250]
  Authors
You Z, Omura S, Ikeda H, Cane DE
  Title
Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlH, a non-heme iron dioxygenase of Streptomyces avermitilis.
  Journal
J. Am. Chem. Soc. 128 (2006) 6566-7.
  Sequence
[sma:SAV_2991]
Reference
2  [PMID:17942405]
  Authors
You Z, Omura S, Ikeda H, Cane DE, Jogl G
  Title
Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis.
  Journal
J. Biol. Chem. 282 (2007) 36552-60.
  Sequence
[sma:SAV_2991]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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