IUBMB Enzyme Nomenclature


Accepted name: 2-hydroxypropyl-CoM lyase

Reaction: (1) (R)-2-hydroxypropyl-CoM = (R)-1,2-epoxypropane + HS-CoM
(2) (S)-2-hydroxypropyl-CoM = (S)-1,2-epoxypropane + HS-CoM

For diagram click here.

coenzyme M (CoM) = 2-sulfanylethan-1-ol = 2-mercaptoethanesulfonate (deprecated)

Other name(s): 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)-[or (S)-]2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming); (R)-2-hydroxypropyl-CoM 2-mercaptoethanesulfonate lyase (cyclizing; (R)-1,2-epoxypropane-forming)

Systematic name: (R)-2-hydroxypropyl-CoM:2-sulfanylethanesulfonate lyase (cyclizing; (R)-1,2-epoxypropane-forming)

Comments: 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 (2-hydroxypropyl-CoM lyase; component I), EC [2-oxopropyl-CoM reductase (carboxylating); component II], EC [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]} that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.

Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 244301-07-3


1. Allen, J.R., Clark, D.D., Krum, J.G. and Ensign, S.A. A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation. Proc. Natl. Acad. Sci. USA 96 (1999) 8432-8437. [PMID: 10411892]

2. Krum, J.G., Ellsworth, H., Sargeant, R.R., Rich, G. and Ensign, S.A. Kinetic and microcalorimetric analysis of substrate and cofactor interactions in epoxyalkane:CoM transferase, a zinc-dependent epoxidase. Biochemistry 41 (2002) 5005-5014. [PMID: 11939797]

3. Coleman, N.V. and Spain, J.C. Epoxyalkane: coenzyme M transferase in the ethene and vinyl chloride biodegradation pathways of Mycobacterium strain JS60. J. Bacteriol. 185 (2003) 5536-5545. [PMID: 12949106]

[EC created 2001 as EC, transferred 2005 to EC]

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