2-oxopropyl-CoM reductase (carboxylating);
NADPH:2-(2-ketopropylthio)ethanesulfonate oxidoreductase/carboxylase;
NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase

Oxidoreductases;
Acting on a sulfur group of donors;
With NAD+ or NADP+ as acceptor

2-mercaptoethanesulfonate,acetoacetate:NADP+ oxidoreductase (decarboxylating)

2-mercaptoethanesulfonate + acetoacetate + NADP+ = 2-(2-oxopropylthio)ethanesulfonate + CO2 + NADPH [RN:R05713]

R05713

2-mercaptoethanesulfonate [CPD:C03576];
acetoacetate [CPD:C00164];
NADP+ [CPD:C00006]

Also acts on thioethers longer in chain length on the oxo side, e.g. 2-oxobutyl-CoM, but this portion must be attached to CoM (2-mercaptoethanesulfonate); no CoM analogs will substitute. This enzyme forms component II of a four-component enzyme system {comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]} that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.

1  [PMID:10411892]

Allen JR, Clark DD, Krum JG, Ensign SA.

A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation.

Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8432-7.

Xanthobacter sp.

2  [PMID:10684609]

Clark DD, Allen JR, Ensign SA.

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.

Biochemistry. 39 (2000) 1294-304.

Xanthobacter sp.