Biology:2-hydroxypropyl-CoM lyase
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Short description: Class of enzymes
| 2-hydroxypropyl-CoM lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.4.1.23 | ||||||||
| CAS number | 244301-07-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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:
- (1) (R)-2-hydroxypropyl-CoM [math]\displaystyle{ \rightleftharpoons }[/math] (R)-1,2-epoxypropane + HS-CoM
- (2) (S)-2-hydroxypropyl-CoM [math]\displaystyle{ \rightleftharpoons }[/math] (S)-1,2-epoxypropane + HS-CoM
This enzyme requires zinc.
References
- ↑ "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. July 1999. doi:10.1073/pnas.96.15.8432. PMID 10411892. Bibcode: 1999PNAS...96.8432A.
- ↑ "Kinetic and microcalorimetric analysis of substrate and cofactor interactions in epoxyalkane:CoM transferase, a zinc-dependent epoxidase". Biochemistry 41 (15): 5005–14. April 2002. doi:10.1021/bi0255221. PMID 11939797.
- ↑ "Epoxyalkane: coenzyme M transferase in the ethene and vinyl chloride biodegradation pathways of mycobacterium strain JS60". Journal of Bacteriology 185 (18): 5536–45. September 2003. doi:10.1128/jb.185.18.5536-5545.2003. PMID 12949106.
External links
- 2-hydroxypropyl-CoM+lyase at the US National Library of Medicine Medical Subject Headings (MeSH)
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