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The enzyme 2-hydroxypropyl-CoM lyase (EC 4.4.1.23, 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)) is an enzyme with systematic name (R)--2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming). This enzyme catalyses the following reaction:

(1) (R)-2-hydroxypropyl-CoM ${\displaystyle \rightleftharpoons }$ (R)-1,2-epoxypropane + HS-CoM

(2) (S)-2-hydroxypropyl-CoM ${\displaystyle \rightleftharpoons }$ (S)-1,2-epoxypropane + HS-CoM

This enzyme requires zinc.

References

1. Allen JR, Clark DD, Krum JG, Ensign SA (July 1999). "A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation". Proceedings of the National Academy of Sciences of the United States of America. 96 (15): 8432–7. Bibcode:1999PNAS...96.8432A. doi:10.1073/pnas.96.15.8432. PMC 17533. PMID 10411892.
2. Krum JG, Ellsworth H, Sargeant RR, Rich G, Ensign SA (April 2002). "Kinetic and microcalorimetric analysis of substrate and cofactor interactions in epoxyalkane:CoM transferase, a zinc-dependent epoxidase". Biochemistry. 41 (15): 5005–14. doi:10.1021/bi0255221. PMID 11939797.
3. Coleman NV, Spain JC (September 2003). "Epoxyalkane: coenzyme M transferase in the ethene and vinyl chloride biodegradation pathways of mycobacterium strain JS60". Journal of Bacteriology. 185 (18): 5536–45. doi:10.1128/jb.185.18.5536-5545.2003. PMC 193758. PMID 12949106.

External links

• 2-hydroxypropyl-CoM+lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

• Biology

• EC 4.4.1