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B6db activities: 2.6.1.79

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.
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
 

Family 

2.6.1.79 (0)
 
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
 
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.

Articles on 2.6.1.79
 
last changed 2019/06/21 13:05

B6db activities