EC 4.4.1.23 - 2-hydroxypropyl-CoM lyase

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IntEnz Enzyme Nomenclature
EC 4.4.1.23

Names

Accepted name:
2-hydroxypropyl-CoM lyase
Other names:
epoxyalkane:2-mercaptoethanesulfonate transferase
epoxyalkane:CoM transferase
epoxyalkane:coenzyme M 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)
Systematic name:
(R)-[or (S)-]2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming)

Reactions

Cofactor

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 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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UM-BBD , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050555
CAS Registry Number: 244301-07-3
UniProtKB/Swiss-Prot:

References

  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: 8432-8437 (1999). [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: 5005-5014 (2002). [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: 5536-5545 (2003). [PMID: 12949106]

[EC 4.4.1.23 created 2001 as EC 4.2.99.19, transferred 2005 to EC 4.4.1.23]