Biology:Phosphonoacetaldehyde hydrolase
From HandWiki
| phosphonoacetaldehyde hydrolase | |||||||||
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| Identifiers | |||||||||
| EC number | 3.11.1.1 | ||||||||
| CAS number | 37289-42-2 | ||||||||
| 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 / QuickGO | ||||||||
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In enzymology, a phosphonoacetaldehyde hydrolase (EC 3.11.1.1) is an enzyme that catalyzes the chemical reaction
- phosphonoacetaldehyde + H2O [math]\displaystyle{ \rightleftharpoons }[/math] acetaldehyde + phosphate
Thus, the two substrates of this enzyme are phosphonoacetaldehyde and H2O, whereas its two products are acetaldehyde and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-phosphorus bonds. The systematic name of this enzyme class is 2-oxoethylphosphonate phosphonohydrolase. Other names in common use include phosphonatase, and 2-phosphonoacetylaldehyde phosphonohydrolase. This enzyme participates in aminophosphonate metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1SWV and 1SWW.
References
- "The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus". Biochim. Biophys. Acta 165 (3): 438–47. 1968. doi:10.1016/0304-4165(68)90223-7. PMID 4982500.
- "The enzymic cleavage of the carbon-phosphorus bond: purification and properties of phosphonatase". Biochim. Biophys. Acta 212 (2): 332–50. 1970. doi:10.1016/0005-2744(70)90214-7. PMID 4989158.
- "Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase". Biochem. J. 165 (2): 409–11. 1977. doi:10.1042/bj1650409. PMID 200222.
- "Investigation of the Bacillus cereus phosphonoacetaldehyde hydrolase. Evidence for a Schiff base mechanism and sequence analysis of an active-site peptide containing the catalytic lysine residue". Biochemistry 27 (6): 2229–34. 1988. doi:10.1021/bi00406a063. PMID 3132206.
- "Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis". Biochemistry 37 (26): 9305–15. 1998. doi:10.1021/bi972677d. PMID 9649311.
External links
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