2-hydroxypropyl-CoM lyase
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)-(or (S)-)2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming).[1][2][3] This enzyme catalyses the following chemical reaction
- (1) (R)-2-hydroxypropyl-CoM (R)-1,2-epoxypropane + HS-CoM
- (2) (S)-2-hydroxypropyl-CoM (S)-1,2-epoxypropane + HS-CoM
This enzyme requires zinc.
References
- ↑ Allen, J.R., Clark, D.D., Krum, J.G. and Ensign, S.A. (1999). "A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation". Proc. Natl. Acad. Sci. USA 96: 8432–8437. doi:10.1073/pnas.96.15.8432. PMC 17533. PMID 10411892.
- ↑ Krum, J.G., Ellsworth, H., Sargeant, R.R., Rich, G. and Ensign, S.A. (2002). "Kinetic and microcalorimetric analysis of substrate and cofactor interactions in epoxyalkane:CoM transferase, a zinc-dependent epoxidase". Biochemistry 41: 5005–5014. doi:10.1021/bi0255221. PMID 11939797.
- ↑ Coleman, N.V. and Spain, J.C. (2003). "Epoxyalkane: coenzyme M transferase in the ethene and vinyl chloride biodegradation pathways of Mycobacterium strain JS60". J. Bacteriol. 185: 5536–5545. doi:10.1128/jb.185.18.5536-5545.2003. PMID 12949106.
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