KEGG ENZYME: 1.14.14.108

ENZYME: 1.14.14.108

Entry

EC 1.14.14.108              Enzyme

Name

2,5-diketocamphane 1,2-monooxygenase;
2,5-diketocamphane lactonizing enzyme;
ketolactonase I (ambiguous);
2,5-diketocamphane 1,2-monooxygenase oxygenating component;
2,5-DKCMO;
camP (gene name);
camphor 1,2-monooxygenase;
camphor ketolactonase I

Class

Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor

Sysname

(+)-bornane-2,5-dione,FMNH2:oxygen oxidoreductase (1,2-lactonizing)

Reaction(IUBMB)

(+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O [RN:R04102]

Reaction(KEGG)

R04102

Substrate

(+)-bornane-2,5-dione [CPD:C03037];
FMNH2 [CPD:C01847];
O2 [CPD:C00007]

Product

(+)-5-oxo-1,2-campholide [CPD:C02952];
FMN [CPD:C00061];
H2O [CPD:C00001]

Comment

A Baeyer-Villiger monooxygenase isolated from camphor-grown strains of Pseudomonas putida and encoded on the cam plasmid. Involved in the degradation of (+)-camphor. Requires a dedicated NADH-FMN reductase [cf. EC 1.5.1.42, FMN reductase (NADH)] [1-3]. Can accept several bicyclic ketones including (+)- and (-)-camphor [6] and adamantanone [4]. The product spontaneously converts to [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate.

History

EC 1.14.14.108 created 1972 as EC 1.14.15.2, transferred 2012 to EC 1.14.13.162, transferred 2018 to EC 1.14.14.108

Pathway

ec00907

Pinene, camphor and geraniol degradation

ec01120

Microbial metabolism in diverse environments

Orthology

K21731

2,5-diketocamphane 1,2-monooxygenase

Genes

PSET:

THL1_4143

NAR:

Saro_1468

SGI:	SGRAN_3255(camP) SGRAN_3282(camP2)

SBIN:

SBA_ch1_19340 SBA_ch1_19390 SBA_ch1_19500

Reference

1 [PMID:14253460]

Authors

CONRAD HE, DUBUS R, NAMTVEDT MJ, GUNSALUS IC.

Title

MIXED FUNCTION OXIDATION. II. SEPARATION AND PROPERTIES OF THE ENZYMES CATALYZING CAMPHOR LACTONIZATION.

Journal

J Biol Chem 240:495-503 (1965)

Reference

2 [PMID:4310834]

Authors

Yu CA, Gunsalus IC.

Title

Monoxygenases. VII. Camphor ketolactonase I and the role of three protein components.

Journal

J Biol Chem 244:6149-52 (1969)

Reference

3 [PMID:3944058]

Authors

Taylor DG, Trudgill PW

Title

Camphor revisited: studies of 2,5-diketocamphane 1,2-monooxygenase from Pseudomonas putida ATCC 17453.

Journal

J Bacteriol 165:489-97 (1986)
DOI:10.1128/JB.165.2.489-497.1986

Reference

4 [PMID:1510672]

Authors

Selifonov SA

Title

Microbial oxidation of adamantanone by Pseudomonas putida carrying the camphor catabolic plasmid.

Journal

Biochem Biophys Res Commun 186:1429-36 (1992)
DOI:10.1016/S0006-291X(05)81566-9

Reference

5 [PMID:8515237]

Authors

Jones KH, Smith RT, Trudgill PW

Title

Diketocamphane enantiomer-specific 'Baeyer-Villiger' monooxygenases from camphor-grown Pseudomonas putida ATCC 17453.

Journal

J Gen Microbiol 139:797-805 (1993)
DOI:10.1099/00221287-139-4-797

Reference

6 [PMID:21906366]

Authors

Kadow M, Sass S, Schmidt M, Bornscheuer UT

Title

Recombinant expression and purification of the 2,5-diketocamphane 1,2-monooxygenase from the camphor metabolizing Pseudomonas putida strain NCIMB 10007.

Journal

AMB Express 1:13 (2011)
DOI:10.1186/2191-0855-1-13

Sequence

[ag:AAR21560]

Reference

7 [PMID:23524667]

Authors

Iwaki H, Grosse S, Bergeron H, Leisch H, Morley K, Hasegawa Y, Lau PC

Title

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.

Journal

Appl Environ Microbiol 79:3282-93 (2013)
DOI:10.1128/AEM.03958-12

Other DBs

ExplorEnz - The Enzyme Database:

1.14.14.108

IUBMB Enzyme Nomenclature:

1.14.14.108

ExPASy - ENZYME nomenclature database:

1.14.14.108

BRENDA, the Enzyme Database:

1.14.14.108

DBGET integrated database retrieval system