释义 |
- References
{{enzyme | Name = Phosphonopyruvate decarboxylase | EC_number = 4.1.1.82 | CAS_number = | IUBMB_EC_number = 4/1/1/82 | GO_code = | image = | width = | caption = }}In enzymology, a phosphonopyruvate decarboxylase ({{EC number|4.1.1.82}}) is an enzyme that catalyzes the chemical reaction 3-phosphonopyruvate 2-phosphonoacetaldehyde + CO2 Hence, this enzyme has one substrate, 3-phosphonopyruvate, and two products, 2-phosphonoacetaldehyde and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming). This enzyme is also called 3-phosphonopyruvate carboxy-lyase. This enzyme participates in aminophosphonate metabolism. References- {{cite journal | vauthors = Zhang G, Dai J, Lu Z, Dunaway-Mariano D | date = 2003 | title = The phosphonopyruvate decarboxylase from Bacteroides fragilis | journal = J. Biol. Chem. | volume = 278 | pages = 41302–8 | pmid = 12904299 | doi = 10.1074/jbc.M305976200 | issue = 42 }}
- {{cite journal | vauthors = Seidel HM, Knowles JR | date = 1994 | title = Interaction of inhibitors with phosphoenolpyruvate mutase: implications for the reaction mechanism and the nature of the active site | journal = Biochemistry | volume = 33 | pages = 5641–6 | pmid = 8180189 | doi = 10.1021/bi00184a037 | issue = 18 }}
- {{cite journal | vauthors = Nakashita H, Watanabe K, Hara O, Hidaka T, Seto H | location = Tokyo | title = Studies on the biosynthesis of bialaphos. Biochemical mechanism of C-P bond formation: discovery of phosphonopyruvate decarboxylase which catalyzes the formation of phosphonoacetaldehyde from phosphonopyruvate | journal = J. Antibiot. | pages = 212–9 | pmid = 9127192 | issue = 3 | volume=50 | date=March 1997 | doi=10.7164/antibiotics.50.212}}
{{Carbon-carbon lyases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{4.1-enzyme-stub}} 2 : EC 4.1.1|Enzymes of unknown structure |