KEGG   ENZYME: 1.14.13.133Help
Entry
EC 1.14.13.133              Enzyme                                 

Name
pentalenene oxygenase;
PtlI
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
pentalenene,NADPH:oxygen 13-oxidoreductase
Reaction(IUBMB)
pentalenene + 2 NADPH + 2 H+ + 2 O2 = pentalen-13-al + 2 NADP+ + 3 H2O (overall reaction) [RN:R09814];
(1a) pentalenene + NADPH + H+ + O2 = pentalen-13-ol + NADP+ + H2O [RN:R09812];
(1b) pentalen-13-ol + NADPH + H+ + O2 = pentalen-13-al + NADP+ + 2 H2O [RN:R09813]
Reaction(KEGG)
Substrate
pentalenene [CPD:C01841];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007];
pentalen-13-ol [CPD:C19938]
Product
pentalen-13-al [CPD:C19939];
NADP+ [CPD:C00006];
H2O [CPD:C00001];
pentalen-13-ol [CPD:C19938]
Comment
A heme-thiolate protein (P-450). The enzyme is involved in the biosynthesis of pentalenolactone and related antibiotics.
History
EC 1.14.13.133 created 2011
Pathway
Sesquiterpenoid and triterpenoid biosynthesis
Orthology
K15907  
pentalenene oxygenase
Genes
SMA: 
SAV_2999(ptlI)
SCT: 
SCY: 
SBH: 
SBI_09680(cyp48)
SDV: 
SCI: 
SCW: 
KSK: 
Taxonomy
Reference
1  [PMID:17017767]
  Authors
Quaderer R, Omura S, Ikeda H, Cane DE
  Title
Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlI, a cytochrome P450 of Streptomyces avermitilis.
  Journal
J. Am. Chem. Soc. 128 (2006) 13036-7.
  Sequence
[sma:SAV_2999]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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