KEGG ENZYME: 1.14.20.3

ENZYME: 1.14.20.3

Entry

EC 1.14.20.3                Enzyme

Name

(5R)-carbapenem-3-carboxylate synthase;
carC (gene name)

Class

Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and the other dehydrogenated

Sysname

(3S,5S)-carbapenam-3-carboxylate,2-oxoglutarate:oxygen oxidoreductase (dehydrating)

Reaction(IUBMB)

(3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2 = (5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O [RN:R10415]

Reaction(KEGG)

R10415

Substrate

(3S,5S)-carbapenam-3-carboxylate [CPD:C17367];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]

Product

(5R)-carbapen-2-em-3-carboxylate [CPD:C06669];
succinate [CPD:C00042];
CO2 [CPD:C00011];
H2O [CPD:C00001]

Comment

Requires Fe2+. The enzyme is involved in the biosynthesis of the carbapenem beta-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum. It catalyses a stereoinversion at C-5 and introduces a double bond between C-2 and C-3.

History

EC 1.14.20.3 created 2013

Pathway

ec00332

Carbapenem biosynthesis

ec01100

Metabolic pathways

ec01110

Biosynthesis of secondary metabolites

Orthology

K18315

(5R)-carbapenem-3-carboxylate synthase

Genes

PROD:

PCO85_15480

SERA:

Ser39006_009930

SERQ:

CWC46_09925

PARI:

I2D83_01760

PPAV:

LOZ86_02770

PCAC:

OI450_17085

PACB:

M9782_00165

DZE:	Dd1591_0211

DAQ:	DAQ1742_04176(cpmC)

PAO:	Pat9b_5315

PLU:	plu0184(cpmC)

PLUM:

A4R40_00890

PTT:	VY86_09605

PRG:	RB151_027400(carC)

PRJ:	NCTC6933_00419

VSR:	Vspart_02937

VRU:	RND59_08410

BGP:	BGL_2c27600

BPLA:

bpln_2g27640

» show all

Reference

1 [PMID:12611886]

Authors

Clifton IJ, Doan LX, Sleeman MC, Topf M, Suzuki H, Wilmouth RC, Schofield CJ

Title

Crystal structure of carbapenem synthase (CarC).

Journal

J Biol Chem 278:20843-50 (2003)
DOI:10.1074/jbc.M213054200

Reference

2 [PMID:12848554]

Authors

Stapon A, Li R, Townsend CA

Title

Carbapenem biosynthesis: confirmation of stereochemical assignments and the role of CarC in the ring stereoinversion process from L-proline.

Journal

J Am Chem Soc 125:8486-93 (2003)
DOI:10.1021/ja034248a

Reference

3 [PMID:15174175]

Authors

Sleeman MC, Smith P, Kellam B, Chhabra SR, Bycroft BW, Schofield CJ

Title

Biosynthesis of carbapenem antibiotics: new carbapenam substrates for carbapenem synthase (CarC).

Journal

Chembiochem 5:879-82 (2004)
DOI:10.1002/cbic.200300908

Other DBs

ExplorEnz - The Enzyme Database:

1.14.20.3

IUBMB Enzyme Nomenclature:

1.14.20.3

ExPASy - ENZYME nomenclature database:

1.14.20.3

BRENDA, the Enzyme Database:

1.14.20.3

DBGET integrated database retrieval system