KEGG   ENZYME: 1.14.13.160Help
Entry
EC 1.14.13.160              Enzyme                                 

Name
(2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase;
2-oxo-Delta3-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase;
2-oxo-Delta3-4,5,5-trimethylcyclopentenylacetyl-CoA 1,2-monooxygenase;
OTEMO
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
[(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetyl-CoA,NADPH:oxygen oxidoreductase (1,5-lactonizing)
Reaction(IUBMB)
[(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetyl-CoA + O2 + NADPH + H+ = [(2R)-3,3,4-trimethyl-6-oxo-3,6-dihydro-1H-pyran-2-yl]acetyl-CoA + NADP+ + H2O [RN:R10044]
Reaction(KEGG)
Substrate
[(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetyl-CoA [CPD:C07160];
O2 [CPD:C00007];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Product
[(2R)-3,3,4-trimethyl-6-oxo-3,6-dihydro-1H-pyran-2-yl]acetyl-CoA [CPD:C20321];
NADP+ [CPD:C00006];
H2O [CPD:C00001]
Comment
A FAD dependent enzyme isolated from Pseudomonas putida. Forms part of the catabolism pathway of camphor. It acts on the CoA ester in preference to the free acid.
History
EC 1.14.13.160 created 2012
Orthology
K21730  (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase
Genes
BXE: Bxe_C0337
BXB: DR64_8098(pamO)
NAR: Saro_1480
SCH: Sphch_3071
SPMI: K663_18031
Taxonomy
Reference
1  [PMID:6848481]
  Authors
Ougham HJ, Taylor DG, Trudgill PW
  Title
Camphor revisited: involvement of a unique monooxygenase in metabolism of 2-oxo-delta 3-4,5,5-trimethylcyclopentenylacetic acid by Pseudomonas putida.
  Journal
J Bacteriol 153:140-52 (1983)
Reference
2  [PMID:22267661]
  Authors
Leisch H, Shi R, Grosse S, Morley K, Bergeron H, Cygler M, Iwaki H, Hasegawa Y, Lau PC
  Title
Cloning, Baeyer-Villiger biooxidations, and structures of the camphor pathway 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetyl-coenzyme A monooxygenase of Pseudomonas putida ATCC 17453.
  Journal
Appl Environ Microbiol 78:2200-12 (2012)
DOI:10.1128/AEM.07694-11
  Sequence
Reference
3  [PMID:22286514]
  Authors
Kadow M, Loschinski K, Sass S, Schmidt M, Bornscheuer UT
  Title
Completing the series of BVMOs involved in camphor metabolism of Pseudomonas putida NCIMB 10007 by identification of the two missing genes, their functional expression in E. coli, and biochemical characterization.
  Journal
Appl Microbiol Biotechnol (2012)
DOI:10.1007/s00253-011-3859-1
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.160
IUBMB Enzyme Nomenclature: 1.14.13.160
ExPASy - ENZYME nomenclature database: 1.14.13.160
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.160
BRENDA, the Enzyme Database: 1.14.13.160

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