| phosphonoacetaldehyde hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.11.1.1 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
In enzymology, a phosphonoacetaldehyde hydrolase ( EC 3.11.1.1) is an enzyme that catalyzes the chemical reaction
- phosphonoacetaldehyde + H2O 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
- La Nauze JM, Rosenberg H (1968). "The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus". Biochim. Biophys. Acta. 165 (3): 438–47. doi: 10.1016/0304-4165(68)90223-7. PMID 4982500.
- La Nauze JM, Rosenberg H, Shaw DC (1970). "The enzymic cleavage of the carbon-phosphorus bond: purification and properties of phosphonatase". Biochim. Biophys. Acta. 212 (2): 332–50. doi: 10.1016/0005-2744(70)90214-7. PMID 4989158.
- La Nauze JM, Coggins JR, Dixon HB (1977). "Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase". Biochem. J. 165 (2): 409–11. doi: 10.1042/bj1650409. PMC 1164914. PMID 200222.
- Olsen DB, Hepburn TW, Moos M, Mariano PS, Dunaway-Mariano D (1988). "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. doi: 10.1021/bi00406a063. PMID 3132206.
- Martin BM, Dunaway-Mariano D (1998). "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. doi: 10.1021/bi972677d. PMID 9649311.
External links
-
Media related to
Phosphonoacetaldehyde hydrolase at Wikimedia Commons
 | This hydrolase article is a stub. You can help Wikipedia by expanding it. |
| phosphonoacetaldehyde hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.11.1.1 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
In enzymology, a phosphonoacetaldehyde hydrolase ( EC 3.11.1.1) is an enzyme that catalyzes the chemical reaction
- phosphonoacetaldehyde + H2O 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
- La Nauze JM, Rosenberg H (1968). "The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus". Biochim. Biophys. Acta. 165 (3): 438–47. doi: 10.1016/0304-4165(68)90223-7. PMID 4982500.
- La Nauze JM, Rosenberg H, Shaw DC (1970). "The enzymic cleavage of the carbon-phosphorus bond: purification and properties of phosphonatase". Biochim. Biophys. Acta. 212 (2): 332–50. doi: 10.1016/0005-2744(70)90214-7. PMID 4989158.
- La Nauze JM, Coggins JR, Dixon HB (1977). "Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase". Biochem. J. 165 (2): 409–11. doi: 10.1042/bj1650409. PMC 1164914. PMID 200222.
- Olsen DB, Hepburn TW, Moos M, Mariano PS, Dunaway-Mariano D (1988). "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. doi: 10.1021/bi00406a063. PMID 3132206.
- Martin BM, Dunaway-Mariano D (1998). "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. doi: 10.1021/bi972677d. PMID 9649311.
External links
-
Media related to
Phosphonoacetaldehyde hydrolase at Wikimedia Commons
|
| This hydrolase article is a stub. You can help Wikipedia by expanding it. |