2.6.1.78: aspartate-prephenate aminotransferase
This is an abbreviated version!
For detailed information about aspartate-prephenate aminotransferase, go to the full flat file.
Word Map on EC 2.6.1.78
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2.6.1.78
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pat
-
transamination
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l-tyrosine
-
l-phenylalanine
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aminotransferases
-
shikimate
-
plastid
-
l-glutamate
-
phenylpropanoids
-
4-hydroxyphenylpyruvate
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branched-chain
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prokaryotic-type
-
chorismate
-
lignin
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mutase
-
l-aspartate
-
phenylpyruvate
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hybrida
-
silvestris
-
sorghum
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rosmarinic
-
7-phosphate
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monofunctional
-
acid-producing
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cyclohexadienyl
-
officinalis
-
bicolor
-
uncomplicated
-
anchusa
-
petunia
- 2.6.1.78
- pat
-
transamination
- l-tyrosine
- l-phenylalanine
- aminotransferases
- shikimate
- plastid
- l-glutamate
-
phenylpropanoids
- 4-hydroxyphenylpyruvate
-
branched-chain
-
prokaryotic-type
- chorismate
- lignin
- mutase
- l-aspartate
- phenylpyruvate
- hybrida
- silvestris
- sorghum
-
rosmarinic
- 7-phosphate
-
monofunctional
-
acid-producing
-
cyclohexadienyl
- officinalis
- bicolor
-
uncomplicated
- anchusa
- petunia
Reaction
Synonyms
1beta AAT, 1beta AAT prephenate aminotransferase, 1beta aspartate aminotransferase, aatA, aspartate/prephenate aminotransferase, aspC, Ath-PAT, AtPAT, bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase, class Ibeta AAT, More, Pat, prephenate aminotransferase, Rme-AAT, Tth-PAT
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Subunits
Subunits on EC 2.6.1.78 - aspartate-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