Oximinotransferase
Appearance
oximinotransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.6.3.1 | ||||||||
CAS no. | 9030-49-3 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, an oximinotransferase (EC 2.6.3.1) is an enzyme that catalyzes the chemical reaction
- pyruvate oxime + acetone pyruvate + acetone oxime
Thus, the two substrates of this enzyme are pyruvate oxime and acetone, whereas its two products are pyruvate and acetone oxime.
This enzyme belongs to the family of transferases, specifically those transferring nitrogenous groups oximinotransferases. The systematic name of this enzyme class is pyruvate-oxime:acetone oximinotransferase. Other names in common use include transoximinase, oximase, pyruvate-acetone oximinotransferase, and transoximase.
References
- Yamafuji K; Eto, M (1954). "Chromatographic study of transoximase". Enzymologia. 16: 247–255.
- Yamafuji K, Omura H, Miura K (1953). "On the transoximase". Enzymologia. 16: 75–80.
- Yamafuji K, Shimamura M, Omura H (1956). "Measurement of transoximase action". Enzymologia. 17: 359–362.