2-hydroxypropyl-CoM lyase

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)-[or (S)]-2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming).[1][2][3] This enzyme catalyses the following reaction:

2-hydroxypropyl-CoM lyase
Identifiers
EC no.4.4.1.23
CAS no.244301-07-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
(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

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  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 10411892.8432-7&rft.date=1999-07&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC17533#id-name=PMC&rft_id=info:pmid/10411892&rft_id=info:doi/10.1073/pnas.96.15.8432&rft_id=info:bibcode/1999PNAS...96.8432A&rft.aulast=Allen&rft.aufirst=JR&rft.au=Clark, DD&rft.au=Krum, JG&rft.au=Ensign, SA&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC17533&rfr_id=info:sid/en.wikipedia.org:2-hydroxypropyl-CoM lyase" class="Z3988">
  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 11939797.5005-14&rft.date=2002-04&rft_id=info:doi/10.1021/bi0255221&rft_id=info:pmid/11939797&rft.aulast=Krum&rft.aufirst=JG&rft.au=Ellsworth, H&rft.au=Sargeant, RR&rft.au=Rich, G&rft.au=Ensign, SA&rfr_id=info:sid/en.wikipedia.org:2-hydroxypropyl-CoM lyase" class="Z3988">
  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 12949106.5536-45&rft.date=2003-09&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC193758#id-name=PMC&rft_id=info:pmid/12949106&rft_id=info:doi/10.1128/jb.185.18.5536-5545.2003&rft.aulast=Coleman&rft.aufirst=NV&rft.au=Spain, JC&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC193758&rfr_id=info:sid/en.wikipedia.org:2-hydroxypropyl-CoM lyase" class="Z3988">
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