HOME
login
history
all enzymes
BRENDA home
History
Information on EC 2.6.1.78 - aspartate-prephenate aminotransferase
for references in articles please use BRENDA:EC2.6.1.78Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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).
Specify your search results
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 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
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1beta AAT
1beta AAT prephenate aminotransferase
1beta aspartate aminotransferase
aspartate/prephenate aminotransferase
aspC
bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
UniProt
Pat
prephenate aminotransferase
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-arogenate + oxaloacetate = prephenate + L-aspartate
-
-
-
-
L-arogenate + oxaloacetate = prephenate + L-aspartate
catalytic reaction mechanism, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
53230-13-0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
4-hydroxyphenylpyruvate + L-aspartate
L-tyrosine + oxaloacetate
-
-
-
-
?
prephenate + L-glutamate
L-arogenate + 2-oxoglutarate
-
transamination, L-glutamate is about 3fold less effective than L-aspartate
-
-
?
L-arogenate + oxaloacetate
L-aspartate + prephenate
-
-
-
r
L-arogenate + oxaloacetate
L-aspartate + prephenate
-
-
-
r
L-arogenate + oxaloacetate
L-aspartate + prephenate
-
-
-
r
L-aspartate + prephenate
L-arogenate + oxaloacetate
-
-
-
r
L-aspartate + prephenate
L-arogenate + oxaloacetate
-
-
-
r
prephenate + L-aspartate
L-arogenate + oxaloacetate
-
transamination
-
-
?
additional information
?
-
-
substrate specificity, highest activity with 2-oxoglutarate and L-aspartate as substrates, low activity with indolepyruvate and glyoxylate
-
-
?
additional information
?
-
no substrates: 4-hydroxyphenylpyruvate, phenylpyruvate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
prephenate + L-aspartate
L-arogenate + oxaloacetate
-
transamination
-
-
?
L-arogenate + oxaloacetate
L-aspartate + prephenate
-
-
-
r
L-arogenate + oxaloacetate
L-aspartate + prephenate
-
-
-
r
L-arogenate + oxaloacetate
L-aspartate + prephenate
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme shows substrate inhibition, but no feedback inhibition by L-phenylalanine and L-tyrosine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetics analysis
-
additional information
additional information
Michaelis-Menten steady-state kinetics analysis
-
additional information
additional information
Michaelis-Menten steady-state kinetics analysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
one PAT incompetent 1beta AAT mutant K12G from Rhizobium meliloti is detected (UniProt ID P58350)
metabolism
physiological function
-
suppression of prephenate aminotransferase leads to a severe reduction in growth and strong chlorosis symptoms. Prephenate aminotransferase silenced plants exhibit extremely reduced levels of asparagine and are greatly affected in their phenylalanine metabolism and lignin deposition. Prephenate aminotransferase suppression triggers a transcriptional reprogramming in plastid nitrogen metabolism. The enzyme is essential for plant growth and development
additional information
metabolism
the enzyme is involved in the tyrosine/phenylalanine biosynthesis pathway, overview
metabolism
the enzyme is involved in the tyrosine/phenylalanine biosynthesis pathway, overview
metabolism
the enzyme is involved in the tyrosine/phenylalanine biosynthesis pathway, overview
metabolism
-
the enzyme is involved in the tyrosine/phenylalanine biosynthesis pathway, overview
-
metabolism
-
the enzyme is involved in the tyrosine/phenylalanine biosynthesis pathway, overview
-
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
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
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. Lys12 plays a specific role in prephenate binding by PAT competent 1beta AAT
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). AAPAT_THET8
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
385
0
42051
Swiss-Prot
-
PAT_ARATH
475
0
51000
Swiss-Prot
Chloroplast (Reliability: 1)
PAT_PETHY
479
0
51743
Swiss-Prot
Chloroplast (Reliability: 2)
AAPAT_CHLTE
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
400
0
44007
Swiss-Prot
-
A0A251S9V0_HELAN
481
0
51608
TrEMBL
Chloroplast (Reliability: 1)
A0A1Z5JBV6_FISSO
435
0
46960
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2I0B401_9ASPA
432
0
46761
TrEMBL
Chloroplast (Reliability: 1)
A0A2G9HKC5_9LAMI
479
0
51526
TrEMBL
Chloroplast (Reliability: 1)
A0A2H9ZU16_9ASPA
395
0
43499
TrEMBL
other Location (Reliability: 3)
A0A2G9HKB5_9LAMI
480
0
51727
TrEMBL
Chloroplast (Reliability: 1)
A0A1Z5JQG7_FISSO
435
0
46744
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2G9IAH1_9LAMI
476
0
51217
TrEMBL
Chloroplast (Reliability: 1)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
purified recombinant enzyme, Rme-AAT/PAT crystals are obtained from 0.2 M ammonium formate, 19% PEG 3350, and Rme-AAT grow from 0.1 M Na acetate pH 4.5, 5% PEG 4000, protein concentration is 10 mg/ml, at 20°C, X-ray diffraction structure determination and analysis at 1.79-1.9 A resolution
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
K12G
additional information
site-directed mutagenesis, modeling, and molecular dynamics simulations reveal that K/R/Q12 residue (numbering according to Thermus thermophilus 1beta AAT) is a signature of the PAT function of 1bta AAT. It is present in the N-terminal flexible loop only in PAT competent 1beta-AAT and has a possible role in stabilizing prephenate by interacting with its 4-hydroxy group
K12G
naturally occuring mutant, the incompetent PATs of Rhizobium meliloti (UniProt ID P58350) has a G instead of K12 and shows reduced PAT activity at prephenate concentrations up to 2.5 mM using a coupled assay method. The mutant shows reduced activity and altered kinetics compared to the wild-type
K12G
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type
K12G
-
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type
-
K12G
-
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, purified enzyme, 50 mM Tris-HCl, pH 8.2, 5 mM 2-mercaptoethanol, 150 mM sucrose, 1 mM EDTA, stable for at least 5 months
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 41fold to homogeneity by anion exchange chromatography, chromatofocusing using the major active fraction with an isoelectric point of 5.4, and gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aat, recombinant expression in Escherichia coli strain BL21 (DE3) Rosetta2
gene aat, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Rosetta2
gene aat, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Rosetta2
gene aat, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Rosetta2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
De-Eknamkul, W.; Ellis, B.E.
Purification and characterization of prephenate aminotransferase from Anchusa officinalis cell cultures
Arch. Biochem. Biophys.
267
87-94
1988
Anchusa officinalis
brenda
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)
brenda
de la Torre, F.; El-Azaz, J.; Avila, C.; Canovas, F.M.
Deciphering the role of aspartate and prephenate aminotransferase activities in plastid nitrogen metabolism
Plant Physiol.
164
92-104
2014
Nicotiana benthamiana
brenda
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)
brenda
Holland, C.K.; Berkovich, D.A.; Kohn, M.L.; Maeda, H.; Jez, J.M.
Structural basis for substrate recognition and inhibition of prephenate aminotransferase from Arabidopsis
Plant J.
94
304-314
2018
Arabidopsis thaliana (Q9SIE1)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.6.1.78)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
