EC number:1.14.14.108

Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.14.108
Description:2,5-diketocamphane 1,2-monooxygenase.
Alternative Name: Camphor ketolactonase I.
Camphor 1,2-monooxygenase.
2,5-diketocamphane lactonizing enzyme.
2,5-diketocamphane 1,2-monooxygenase oxygenating component.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.14.108
BRENDA Enzyme Link: BRENDA 1.14.14.108
KEGG Enzyme Link: KEGG1.14.14.108
BioCyc Enzyme Link: BioCyc 1.14.14.108
ExPASy Enzyme Link: ExPASy1.14.14.108
EC2PDB Enzyme Link: EC2PDB 1.14.14.108
ExplorEnz Enzyme Link: ExplorEnz 1.14.14.108
PRIAM enzyme-specific profiles Link: PRIAM 1.14.14.108
IntEnz Enzyme Link: IntEnz 1.14.14.108
MEDLINE Enzyme Link: MEDLINE 1.14.14.108

EC number:1.14.14.108

MSA:

1.14.14.108;
Phylogenetic Tree:

1.14.14.108;
Uniprot:
M-CSA:
RHEA:34415 (1R,4R)-bornane-2,5-dione + FMNH2 + O2 = (1R,4R)-5-oxo-1,2-campholide + FMN + H(+) + H2O
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])(-[*:4])-[C;H0;+0:5](=[*:6])-[*:7].[*:8]-[N;H0;+0:9]1-[CH;+0:10]=[C;H0;+0:11](-[*:12])-[CH2;+0:13]-[CH;+0:14]=[CH;+0:15]-1.[H+;H0:16].[O;H0;+0:17]=[O;H0;+0:18]>>[*:1]-[C;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:17]-[C;H0;+0:5](=[*:6])-[*:7].[*:8]-[n+;H0:9]1:[cH;+0:10]:[c;H0;+0:11](-[*:12]):[cH;+0:13]:[cH;+0:14]:[cH;+0:15]:1.[OH2;+0:18]
Reaction
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References

TitleAuthorsDatePubMed ID
The purification and crystallisation of 2,5-diketocamphane 1,2-monooxygenase and 3,6-diketocamphane 1,6-monooxygenase from Pseudomonas putida NCIMB 10007.McGhie EJ, Littlechild JA1996 Feb8674690
Diketocamphane enantiomer-specific 'Baeyer-Villiger' monooxygenases from camphor-grown Pseudomonas putida ATCC 17453.Jones KH, Smith RT, Trudgill PW1993 Apr8515237
Monoxygenases. VII. Camphor ketolactonase I and the role of three protein components.Yu CA, Gunsalus IC1969 Nov 254310834
Camphor revisited: studies of 2,5-diketocamphane 1,2-monooxygenase from Pseudomonas putida ATCC 17453.Taylor DG, Trudgill PW1986 Feb3944058
Recombinant expression and purification of the 2,5-diketocamphane 1,2-monooxygenase from the camphor metabolizing Pseudomonas putida strain NCIMB 10007.Kadow M, Saß S, Schmidt M, Bornscheuer UT2011 Jun 2321906366
Microbial oxidation of adamantanone by Pseudomonas putida carrying the camphor catabolic plasmid.Selifonov SA1992 Aug 141510672
RHEA:33923 (1R,4R)-5-oxo-1,2-campholide = [(1R)-2,2,3-trimethyl-2-oxocyclopent-3-en-1-yl]acetate + H(+)
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])(-[CH2;+0:4]-[*:5])-[O;H0;+0:6]-[*:7]>>([*:1]-[C;H0;+0:2](-[*:3])=[CH;+0:4]-[*:5].[*:7]-[OH;+0:6])
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Camphor pathway redux: functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions.Iwaki H, Grosse S, Bergeron H, Leisch H, Morley K, Hasegawa Y, Lau PC2013 May23524667
Diketocamphane enantiomer-specific 'Baeyer-Villiger' monooxygenases from camphor-grown Pseudomonas putida ATCC 17453.Jones KH, Smith RT, Trudgill PW1993 Apr8515237
Camphor revisited: studies of 2,5-diketocamphane 1,2-monooxygenase from Pseudomonas putida ATCC 17453.Taylor DG, Trudgill PW1986 Feb3944058
Recombinant expression and purification of the 2,5-diketocamphane 1,2-monooxygenase from the camphor metabolizing Pseudomonas putida strain NCIMB 10007.Kadow M, Saß S, Schmidt M, Bornscheuer UT2011 Jun 2321906366