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2.6.1.79 |
| Description |
Glutamate--prephenate aminotransferase |
| Alternative names |
prephenate transaminase (ambiguous);
PAT (ambiguous);
L-glutamate:prephenate aminotransferase;
L-arogenate:2-oxoglutarate aminotransferase. |
| Catalyzed reaction |
L-arogenate + 2-oxoglutarate = prephenate + L-glutamate |
| Cofactor |
Pyridoxal-phosphate. |
| Comments |
A pyridoxal-phosphate protein. Aspartate can also act as the amino donor, but more slowly (cf. EC 2.6.1.78, aspartate--prephenate aminotransferase).
The enzyme from higher plants shows a marked preference for prephenate as substrate compared to pyruvate, phenylpyruvate or 4-hydroxyphenylpyruvate. |
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In bacteria, the reaction is carried out (as a promiscuous activity) by enzymes with aspartate aminotransferase, branched-chain amino acid aminotransferase and N-succinyldiaminopymelate aminotransferase activities. |
| PDB |
5WMH; |
| Organisms |
-Eubacteria -Plants |
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| Links |
Enzyme (activities) 2.6.1.79
BRENDA (activities) 2.6.1.79
KEGG (pathways) 2.6.1.79
PLPMDB (PLP mutants) 2.6.1.79
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| References |
Giustini C, Graindorge M, Cobessi D, Crouzy S, Robin A, Curien G, Matringe M (2019) Tyrosine metabolism: identification of a key residue in the acquisition of prephenate aminotransferase activity by 1β aspartate aminotransferase FEBS J 286 2118-2134. Holland CK, Berkovich DA, Kohn ML, Maeda H, Jez JM (2018) Structural basis for substrate recognition and inhibition of prephenate aminotransferase from Arabidopsis Plant J 94 304-314. de la Torre F, El-Azaz J, Avila C, Cánovas FM (2014) Deciphering the role of aspartate and prephenate aminotransferase activities in plastid nitrogen metabolism Plant Physiol 164 92-104. Graindorge M, Giustini C, Kraut A, Moyet L, Curien G, Matringe (2014) Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms J Biol Chem 289 3198-208. Graindorge M, Giustini C, Jacomin AC, Kraut A, Curien G, Matringe M. (2010) Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: The last homeless enzyme of aromatic amino acids biosynthesis FEBS Lett 584 4357-60. Maeda H, Yoo H, Dudareva N. (2010) Prephenate aminotransferase directs plant phenylalanine biosynthesis via arogenate Nat Chem Biol 7 19-21. Bonner, C.; Jensen, R. (1985) Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris Arch Biochem Biophys 238 237-46. |
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| last changed |
2019/06/21 13:05 |
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