Aspartate-prephenate aminotransferase

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In enzymology, an aspartate-prephenate aminotransferase (EC 2.6.1.78) is an enzyme that catalyzes the chemical reaction

L-arogenate + oxaloacetate prephenate + L-aspartate

Thus, the two substrates of this enzyme are L-arogenate and oxaloacetate, whereas its two products are prephenate and L-aspartate.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-arogenate:oxaloacetate aminotransferase. Other names in common use include prephenate transaminase (ambiguous), PAT (ambiguous), prephenate aspartate aminotransferase, and L-aspartate:prephenate aminotransferase.

[edit] References

• IUBMB entry for 2.6.1.78
• BRENDA references for 2.6.1.78 (Recommended.)
• PubMed references for 2.6.1.78
• PubMed Central references for 2.6.1.78
• Google Scholar references for 2.6.1.78
• De-Eknamkul W, Ellis BE (1988). "Purification and characterization of prephenate aminotransferase from Anchusa officinalis cell cultures". Arch. Biochem. Biophys. 267: 87–94. doi:10.1016/0003-9861(88)90011-2. PMID 3196038. 

[edit] External links

• IUBMB entry for 2.6.1.78

• KEGG entry for 2.6.1.78

• BRENDA entry for 2.6.1.78

• NiceZyme view of 2.6.1.78

• EC2PDB: PDB structures for 2.6.1.78

• PRIAM entry for 2.6.1.78

• PUMA2 entry for 2.6.1.78

• IntEnz: Integrated Enzyme entry for 2.6.1.78

• MetaCyc entry for 2.6.1.78

• Atomic-resolution structures of enzymes belonging to this class