| phenylpyruvate tautomerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.3.2.1 | ||||||||
| CAS no. | 9023-54-5 | ||||||||
| 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, phenylpyruvate tautomerase or Macrophage migration inhibitory factor (EC 5.3.2.1) is an enzyme that catalyzes the chemical reaction
- keto-phenylpyruvate enol-phenylpyruvate
Phenylpyruvate tautomerase has also been found to exhibit the same keto-enol tautomerism for 4-Hydroxyphenylpyruvic acid, which is structurally similar to phenylpyruvate but contains an additional hydroxyl moiety in the para position of the aromatic ring.[1]
This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting keto- and enol-groups. The systematic name of this enzyme class is phenylpyruvate keto---enol-isomerase. This enzyme is also called phenylpyruvic keto-enol isomerase. This enzyme participates in tyrosine metabolism and phenylalanine metabolism.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1GYJ, 1GYX, 1GYY, 2GDG, 2OOH, 2OOW, and 2OOZ.
References
- Blasi F, Fragomele F, Covelli I (1969). "Thyroidal phenylpyruvate tautomerase. Isolation and characterization". J. Biol. Chem. 244 (18): 4864–70. PMID 5824560.
- Knox WE (1955). "p-Hydroxyphenylpyruvate enol-keto tautomerase". Methods Enzymol. 2: 289–295. doi:10.1016/s0076-6879(55)02202-7.
- KNOX WE, PITT BM (1957). "Enzymic catalysis of the keto-enol tautomerization of phenylpyruvic acids". J. Biol. Chem. 225 (2): 675–88. PMID 13416270.