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
2-hydroxypropyl-CoM lyase
Identifiers
EC number4.4.1.23
CAS number244301-07-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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. 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.
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