2.6.1.79: glutamate-prephenate aminotransferase
This is an abbreviated version!
For detailed information about glutamate-prephenate aminotransferase, go to the full flat file.
Reaction
Synonyms
1beta AAT, 1beta AAT prephenate aminotransferase, 1beta aspartate aminotransferase, aatA, aspartate aminotransferase A, aspartate/prephenate aminotransferase, AspB2, AT-C, Ath-PAT, AtPAT, bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase, class Ibeta AAT, IlvE, More, Pat, prephenate aminotransferase, prephenate: glutamate aminotransferase, Rme-AAT, Rme-AAT/PAT
ECTree
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Subunits
Subunits on EC 2.6.1.79 - glutamate-prephenate aminotransferase
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homodimer
AtPAT crystallizes as a homodimer. Each monomer of AtPAT consists of 15 alpha-helices and 9 beta-strands divided between two structural domains. The N-terminal domain (Lys115-Leu353) contains two sets of three a-helices surrounding six parallel and one anti-parallel beta-strand. Two additional alpha-helices in the PLP-binding pocket, as well as the a-helix connecting the N- and C-terminal domains, complete the N-terminal domain. The smaller C-terminal domain contains part of the N-terminal region (Ser71-Pro114) and residues Gly354 through Leu469, totaling five alpha-helices and two beta-strands. The N-terminal flexible loop (Ser71-Ser82) and features of the N-terminal domain form the dimer interface