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
Biosynthesis of antibiotics
Orthology
K15907  
pentalenene oxygenase
Genes
SMA: 
SCT: 
SCY: 
SBH: 
SBI_09680(cyp48)
SDV: 
SCI: 
SCW: 
SLE: 
sle_13150(sle_13150)
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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