Alkylmercury lyase
| alkylmercury lyase | |||||||||
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| Identifiers | |||||||||
| EC number | 4.99.1.2 | ||||||||
| CAS number | 72560-99-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, an alkylmercury lyase (EC 4.99.1.2) is an enzyme that catalyzes the chemical reaction
- an alkylmercury + H+
an alkane + Hg2+
Thus, the two substrates of this enzyme are alkylmercury and H+, whereas its two products are alkane and a mercury ion.
This enzyme belongs to the family of lyases, specifically the "catch-all" class of lyases that do not fit into any other sub-class. The systematic name of this enzyme class is alkylmercury mercuric-lyase (alkane-forming). Other names in common use include organomercury lyase, organomercurial lyase, and alkylmercury mercuric-lyase.
The enzyme converts methyl mercury to the much less toxic elemental form of the metal.
References
- ↑ Lafrance-Vanasse, J.; Lefebvre, M.; Di Lello, P.; Sygusch, J.; Omichinski, J. G. (2008). "Crystal Structures of the Organomercurial Lyase MerB in Its Free and Mercury-bound Forms: INSIGHTS INTO THE MECHANISM OF METHYLMERCURY DEGRADATION". Journal of Biological Chemistry 284 (2): 938–944. doi:10.1074/jbc.M807143200. PMID 19004822.
- Tezuka T, Tonomura K. "Purification and properties of an enzyme catalyzing the splitting of carbon-mercury linkages from mercury-resistant Pseudomonas K-62 strain. I. Splitting enzyme 1". J. (Tokyo). Biochem. (1): 79–87. PMID 9382.
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