EC Tree |
1. Oxidoreductases |
1.8 Acting on a sulfur group of donors |
1.8.1 With NAD+ or NADP+ as acceptor |
ID: | 1.8.1.5 |
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Description: | 2-oxopropyl-CoM reductase (carboxylating). |
Alternative Name: |
NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase. NADPH:2-(2-ketopropylthio)ethanesulfonate oxidoreductase/carboxylase. 2-KPCC. |
Cath: | 3.30.390.30; 3.40.50.720; 3.50.50.60; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 1.8.1.5 |
BRENDA Enzyme Link: | BRENDA 1.8.1.5 |
KEGG Enzyme Link: | KEGG1.8.1.5 |
BioCyc Enzyme Link: | BioCyc 1.8.1.5 |
ExPASy Enzyme Link: | ExPASy1.8.1.5 |
EC2PDB Enzyme Link: | EC2PDB 1.8.1.5 |
ExplorEnz Enzyme Link: | ExplorEnz 1.8.1.5 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.8.1.5 |
IntEnz Enzyme Link: | IntEnz 1.8.1.5 |
MEDLINE Enzyme Link: | MEDLINE 1.8.1.5 |
RHEA:16977 | acetoacetate + coenzyme M + NADP(+) = 2-oxopropyl-coenzyme M + CO2 + NADPH |
RULE(radius=1) | [*:1]-[SH;+0:2].[*:3]-[n+;H0:4]1:[cH;+0:5]:[cH;+0:6]:[cH;+0:7]:[c;H0;+0:8](-[*:9]):[cH;+0:10]:1.[*:11]=[C;H0;+0:12](-[OH;+0:13])-[CH2;+0:14]-[*:15]>>[*:3]-[N;H0;+0:4]1-[CH;+0:5]=[CH;+0:6]-[CH2;+0:7]-[C;H0;+0:8](-[*:9])=[CH;+0:10]-1.[*:1]-[S;H0;+0:2]-[CH2;+0:14]-[*:15].[*:11]=[C;H0;+0:12]=[O;H0;+0:13] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase. | Nocek B, Jang SB, Jeong MS, Clark DD, Ensign SA, Peters JW | 2002 Oct 29 | 12390015 |
Characterization of five catalytic activities associated with the NADPH:2-ketopropyl-coenzyme M [2-(2-ketopropylthio)ethanesulfonate] oxidoreductase/carboxylase of the Xanthobacter strain Py2 epoxide carboxylase system. | Clark DD, Allen JR, Ensign SA | 2000 Feb 15 | 10684609 |
A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation. | Allen JR, Clark DD, Krum JG, Ensign SA | 1999 Jul 20 | 10411892 |