KEGG   ENZYME: 4.4.1.23Help
Entry
EC 4.4.1.23                 Enzyme                                 

Name
2-hydroxypropyl-CoM lyase;
epoxyalkane:coenzyme M transferase;
epoxyalkane:CoM transferase;
epoxyalkane:2-mercaptoethanesulfonate transferase;
coenzyme M-epoxyalkane ligase;
epoxyalkyl:CoM transferase;
epoxypropane:coenzyme M transferase;
epoxypropyl:CoM transferase;
EaCoMT;
2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming);
(R)-2-hydroxypropyl-CoM 2-mercaptoethanesulfonate lyase (cyclizing;
(R)-1,2-epoxypropane-forming)
Class
Lyases;
Carbon-sulfur lyases;
Carbon-sulfur lyases (only sub-subclass identified to date)
BRITE hierarchy
Sysname
(R)-[or (S)-]2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming)
Reaction(IUBMB)
(1) (R)-2-hydroxypropyl-CoM = (R)-1,2-epoxypropane + HS-CoM [RN:R05761 R05762];
(2) (S)-2-hydroxypropyl-CoM = (S)-1,2-epoxypropane + HS-CoM
Reaction(KEGG)
Substrate
(R)-2-hydroxypropyl-CoM [CPD:C11496];
(S)-2-hydroxypropyl-CoM [CPD:C11498]
Product
(R)-1,2-epoxypropane;
HS-CoM [CPD:C03576];
(S)-1,2-epoxypropane [CPD:C11507]
Comment
Requires zinc. Acts on both enantiomers of chiral epoxyalkanes to form the corresponding (R)- and (S)-2-hydroxyalkyl-CoM adducts. The enzyme will function with some other thiols (e.g., 2-sulfanylethanol) as the nucleophile. Uses short-chain epoxyalkanes from C2 (epoxyethane) to C6 (1,2-epoxyhexane). This enzyme forms component I 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.
History
EC 4.4.1.23 created 2001 as EC 4.2.99.19, transferred 2005 to EC 4.4.1.23
Reference
1  [PMID:10411892]
  Authors
Allen JR, Clark DD, Krum JG, Ensign SA.
  Title
A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8432-7.
Reference
2  [PMID:11939797]
  Authors
Krum JG, Ellsworth H, Sargeant RR, Rich G, Ensign SA.
  Title
Kinetic and microcalorimetric analysis of substrate and cofactor interactions in epoxyalkane:CoM transferase, a zinc-dependent epoxidase.
  Journal
Biochemistry. 41 (2002) 5005-14.
Reference
3  [PMID:12949106]
  Authors
Coleman NV, Spain JC.
  Title
Epoxyalkane: coenzyme M transferase in the ethene and vinyl chloride biodegradation pathways of mycobacterium strain JS60.
  Journal
J. Bacteriol. 185 (2003) 5536-45.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
244301-07-3

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