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Information on EC 2.6.1.78 - aspartate-prephenate aminotransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SIE1
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2.6.1.78 aspartate-prephenate aminotransferaseIUBMB Comments
A pyridoxal-phosphate protein. Glutamate can also act as the amino donor, but more slowly (cf. EC 2.6.1.79, glutamate---prephenate aminotransferase).
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Word Map
- 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
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
UniProt
additional information
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-arogenate + oxaloacetate = prephenate + L-aspartate
catalytic reaction mechanism, overview
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
L-arogenate:oxaloacetate aminotransferase
A pyridoxal-phosphate protein. Glutamate can also act as the amino donor, but more slowly (cf. EC 2.6.1.79, glutamate---prephenate aminotransferase).
CAS REGISTRY NUMBER
COMMENTARY
53230-13-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arogenate + oxaloacetate
L-aspartate + prephenate
-
-
-
r
additional information
?
-
no substrates: 4-hydroxyphenylpyruvate, phenylpyruvate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arogenate + oxaloacetate
L-aspartate + prephenate
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
PLP, dependent on, PLP is bound in the active site of each chain in the wild-type structure. In the AtPAT crystal structure, PLP is covalently linked to the epsilon-nitrogen of Lys306 to form the internal aldimine (i.e. Schiff base). Trp193 and Ile274 position the ring of PLP through pi-pi stacking and van der Waals interactions, respectively. The pyridine ring nitrogen of PLP forms a charge-charge interaction with the side chain of Asp272
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetics analysis
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.56
cysteine
Arabidopsis thaliana
versus 2-oxoglutarate, pH 7.5, 25°C, recombinant wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
SwissProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme is involved in the tyrosine/phenylalanine biosynthesis pathway, overview
additional information
additional information
key residues, such as Glu108, are involved in both keto acid and amino acid substrate specificities and probably contribute to the evolution of PAT activity among class Ibeta AAT enzymes, ligand binding study, molecular mechanisms underlying recognition of keto acid and amino acid substrates, overview. Lys306 is the catalytic Lys in AtPAT
additional information
modeling and molecular dynamic simulations. Identification of a molecular determinant of PAT activity in the flexible N-terminal loop of 1beta AAT. A Lys/Arg/Gln residue in position 12 (numbering according to Thermus thermophilus 1beta AAT), present only in PAT competent enzymes, can interact with the 4-hydroxyl group of the prephenate substrate, probably playing a central role in the acquisition of PAT activity by 1beta AAT. PAT enzyme structures comparisons, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PAT_ARATH
475
0
51000
Swiss-Prot
Chloroplast (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AtPAT wild-type enzyme and K306A, T84V, and T84V/K169V mutant enzymes in complex with either 2-oxoglutarate or pyridoxamine 5'-phosphate and glutamate, X-ray diffraction structure determination and analysis at 1.4-3.0 A resolution, molecular replacement
purified recombinant enzyme, crystallization from 0.1 M Na-citrate, pH 4.0, 11% PEG 4000, 20°C, X-ray diffraction structure determination and analysis at 1.7 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A168G
site-directed mutagenesis, altered substrate binding kinetics compared to wild-type
E108K
site-directed mutagenesis, altered substrate binding kinetics compared to wild-type
K169S
site-directed mutagenesis, inactive with aspartate and glutamate
K169V
site-directed mutagenesis, inactive with glutamate, altered substrate binding kinetics compared to wild-type
K306A
site-directed mutagenesis, structure comparison with wild-type, overview. The alanine substitution of Lys306 prevents Schiff base formation with the cofactor, inactive mutant
T84V
site-directed mutagenesis, altered substrate binding kinetics compared to wild-type
T84V/K169V
site-directed mutagenesis, altered substrate binding kinetics compared to wild-type
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aat, recombinant expression in Escherichia coli strain BL21 (DE3) Rosetta2
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Graindorge, M.; Giustini, C.; Jacomin, A.C.; Kraut, A.; Curien, G.; Matringe, M.
Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: the last homeless enzyme of aromatic amino acids biosynthesis
FEBS Lett.
584
4357-4360
2010
Arabidopsis thaliana (Q9SIE1)
Giustini, C.; Graindorge, M.; Cobessi, D.; Crouzy, S.; Robin, A.; Curien, G.; Matringe, M.
Tyrosine metabolism identification of a key residue in the acquisition of prephenate aminotransferase activity by 1beta aspartate aminotransferase
FEBS J.
286
2118-2134
2019
Sinorhizobium meliloti (Q02635), Thermus thermophilus (Q56232), Arabidopsis thaliana (Q9SIE1), Thermus thermophilus DSM 579 (Q56232), Thermus thermophilus ATCC 27634 (Q56232)
EXTERNAL LINKS (specific for EC-Number 2.6.1.78)
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