Phosphoenolpyruvate carboxykinase (ATP)
Appearance
(Redirected from ATP:oxaloacetate carboxy-lyase (transphosphorylating))
Phosphoenolpyruvate carboxykinase (ATP) | |||||||||
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Identifiers | |||||||||
EC no. | 4.1.1.49 | ||||||||
CAS no. | 9073-94-3 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Phosphoenolpyruvate carboxykinase (ATP) (EC 4.1.1.49, phosphopyruvate carboxylase (ATP), phosphoenolpyruvate carboxylase, phosphoenolpyruvate carboxykinase, phosphopyruvate carboxykinase (adenosine triphosphate), PEP carboxylase, PEP carboxykinase, PEPCK (ATP), PEPK, PEPCK, phosphoenolpyruvic carboxylase, phosphoenolpyruvic carboxykinase, phosphoenolpyruvate carboxylase (ATP), phosphopyruvate carboxykinase, ATP:oxaloacetate carboxy-lyase (transphosphorylating)) is an enzyme with systematic name ATP:oxaloacetate carboxy-lyase (transphosphorylating; phosphoenolpyruvate-forming).[1][2][3] This enzyme catalyses the following chemical reaction
- ATP + oxaloacetate ADP + phosphoenolpyruvate + CO2
See also
[edit]References
[edit]- ^ Cannata JJ (February 1970). "Phosphoenolpyruvate carboxykinase from bakers' yeast. Isolation of the enzyme and study of its physical properties". The Journal of Biological Chemistry. 245 (4): 792–8. PMID 5416663.
- ^ Cannata JJ, Stoppani AO (April 1963). "Phosphopyruvate carboxylase from baker's yeast. I. Isolation, purification, and characterization". The Journal of Biological Chemistry. 238: 1196–207. PMID 14018315.
- ^ Cannata JJ, Stoppani AO (April 1963). "Phosphopyruvate carboxylase from baker's yeast. II. Properties of enzyme". The Journal of Biological Chemistry. 238: 1208–12. PMID 14018316.
External links
[edit]- Phosphoenolpyruvate+carboxykinase+(ATP) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)