ExplorEnz: EC 1.3.1.129

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1.3.1.129

Accepted name:

(2E)-2-enoyl-CoA carboxylase/reductase

Reaction:

a 2-carboxyacyl-CoA + NADP⁺ = a (2E)-2-enoyl-CoA + CO₂ + NADPH + H⁺

Glossary:

2-carboxyacyl-CoA = 2-alkylmalonyl-CoA

Other name(s):

divR (gene name); antE (gene name); revT (gene name); salG (gene name)

Systematic name:

2-carboxyacyl-CoA:NADP⁺ oxidoreductase (decarboxylating)

Comments:

This bacterial enzyme, which is similar to EC 1.3.1.85, crotonyl-CoA carboxylase/reductase, has a broad substrate range and participates in production of different 2-carboxyacyl-CoA products, which serve as unusual extender units for some polyketide synthases. The enzyme belongs to the medium-chain reductase/dehydrogenase (MDR) superfamily and requires an NADPH cosubstrate. The carboxylation reaction mechanism begins with the transfer of the hydride from NADPH onto the β-carbon of the enoyl-CoA to yield a thioester enolate, followed by the electrophilic attack of CO₂ at the α-carbon.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc

References:

1.	Liu, Y., Hazzard, C., Eustaquio, A.S., Reynolds, K.A. and Moore, B.S. Biosynthesis of salinosporamides from α,β-unsaturated fatty acids: implications for extending polyketide synthase diversity. J. Am. Chem. Soc. 131 (2009) 10376–10377. [DOI] [PMID: 19601645]
2.	Xu, Z., Ding, L. and Hertweck, C. A branched extender unit shared between two orthogonal polyketide pathways in an endophyte. Angew. Chem. Int. Ed. Engl. 50 (2011) 4667–4670. [DOI] [PMID: 21506215]
3.	Sandy, M., Rui, Z., Gallagher, J. and Zhang, W. Enzymatic synthesis of dilactone scaffold of antimycins. ACS Chem. Biol. 7 (2012) 1956–1961. [DOI] [PMID: 22971101]
4.	Miyazawa, T., Takahashi, S., Kawata, A., Panthee, S., Hayashi, T., Shimizu, T., Nogawa, T. and Osada, H. Identification of middle chain fatty acyl-CoA ligase responsible for the biosynthesis of 2-alkylmalonyl-CoAs for polyketide extender unit. J. Biol. Chem. 290 (2015) 26994–27011. [DOI] [PMID: 26378232]

[EC 1.3.1.129 created 2025]