Acetylene hydratase
In enzymology, an acetylene hydratase (EC 4.2.1.112) is a rare example of an enzyme containing tungsten. It catalyzes the hydration of acetylene to give acetaldehyde:[1]
- C2H2 + H2O → CH3CHO
| Acetylene hydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.2.1.112 | ||||||||
| 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 W centre is bound to two molybdopterin cofactors.[2] The mechanism is thought to involve attachment of acetylene to the metal followed by nucleophilic attack of water.[3]
This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is acetaldehyde hydro-lyase (acetylene-forming). Other names in common use include AH, and acetaldehyde hydro-lyase. Acetylene hydratase participates in tetrachloroethene degradation.
References
- Rosner BM, Schink B (1995). "Purification and characterization of acetylene hydratase of Pelobacter acetylenicus, a tungsten iron-sulfur protein". J. Bacteriol. 177 (20): 5767–72. PMC 177396. PMID 7592321.
- ten Brink, Felix (2014). "Chapter 2. Living on acetylene. A Primordial Energy Source". In Peter M.H. Kroneck and Martha E. Sosa Torres (ed.). The Metal-Driven Biogeochemistry of Gaseous Compounds in the Environment. Metal Ions in Life Sciences. 14. Springer. pp. 1–14. doi:10.1007/978-94-017-9269-1_2.
- Einsle O; Ullmann, GM; Messerschmidt, A; Schink, B; Kroneck, PM; Einsle, O (2007). "Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase" (PDF). Proc. Natl. Acad. Sci. U.S.A. 104 (9): 3073–7. doi:10.1073/pnas.0610407104. PMC 1805521. PMID 17360611.
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