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Information on EC 2.6.1.1 - aspartate transaminase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SIE1
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2.6.1.1 aspartate transaminaseIUBMB Comments
A pyridoxal-phosphate protein. Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. Aspartate transaminase activity can be formed from the aromatic-amino-acid transaminase (EC 2.6.1.57) of Escherichia coli by controlled proteolysis , some EC 2.6.1.57 activity can be found in this enzyme from other sources ; indeed the enzymes are identical in Trichomonas vaginalis .
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- 2.6.1.1
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alt
- bilirubin
- cholesterol
- creatinine
- necrosis
- albumin
- triglyceride
- dismutase
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hepatotoxicity
- malondialdehyde
- catalase
-
hepatoprotective
- hepatocytes
- wistar
- sod
- fibrosis
- hemoglobin
- platelet
-
glutamic-pyruvic
- myocardial
- lipoprotein
-
postoperative
- bile
-
hematological
- transpeptidase
-
tetrachloride
- ccl4
- infarct
- cirrhosis
- gg
-
gamma-glutamyl
-
uric
-
admission
- transaminases
-
phosphokinase
-
albino
-
jaundice
-
ccl4-induced
- nafld
-
c-reactive
- prothrombin
-
glutamyl
- globulin
- gamma-glutamyltransferase
-
corpuscular
-
tetrachloride-induced
- silymarin
-
hematocrit
- synthesis
-
kinase-mb
- medicine
- biotechnology
-
elastography
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
aspartate transaminase, asat, glutamic oxaloacetic transaminase, glutamate oxaloacetate transaminase, glutamic-oxaloacetic transaminase, asp at, aspat, aspartate at, glutamic-oxalacetic transaminase, aat-2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
UniProt
2-oxoglutarate-glutamate aminotransferase
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AAT
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aminotransferase, aspartate
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aspartate alpha-ketoglutarate transaminase
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aspartate aminotransferase
aspartate-2-oxoglutarate transaminase
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aspartate:2-oxoglutarate aminotransferase
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aspartic acid aminotransferase
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aspartic aminotransferase
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aspartyl aminotransferase
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AspT
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AST
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glutamate oxaloacetate transaminase
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glutamate-oxalacetate aminotransferase
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glutamate-oxalate transaminase
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glutamic oxalic transaminase
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glutamic-aspartic aminotransferase
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glutamic-aspartic transaminase
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glutamic-oxalacetic transaminase
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glutamic-oxaloacetic transaminase
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GOT (enzyme)
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L-aspartate transaminase
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L-aspartate-2-ketoglutarate aminotransferase
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L-aspartate-2-oxoglutarate aminotransferase
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L-aspartate-2-oxoglutarate-transaminase
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L-aspartate-alpha-ketoglutarate transaminase
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L-aspartic aminotransferase
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oxaloacetate transferase
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oxaloacetate-aspartate aminotransferase
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transaminase A
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aspartate aminotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
catalytic reaction mechanism, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Alanine, aspartate and glutamate metabolism, Arginine and proline metabolism, Arginine biosynthesis, Biosynthesis of secondary metabolites, Carbon fixation in photosynthetic organisms, Cysteine and methionine metabolism, Isoquinoline alkaloid biosynthesis, Microbial metabolism in diverse environments, Novobiocin biosynthesis, Phenylalanine metabolism, Phenylalanine, tyrosine and tryptophan biosynthesis, Tropane, piperidine and pyridine alkaloid biosynthesis, Tyrosine metabolism
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-aspartate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. Aspartate transaminase activity can be formed from the aromatic-amino-acid transaminase (EC 2.6.1.57) of Escherichia coli by controlled proteolysis [7], some EC 2.6.1.57 activity can be found in this enzyme from other sources [8]; indeed the enzymes are identical in Trichomonas vaginalis [6].
CAS REGISTRY NUMBER
COMMENTARY
9000-97-9
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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
additional information
?
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no enzyme activity is detectable in the presence of glutamine, asparagine, alanine, histidine, leucine, methionine, lysine, arginine, tryptophan, tyrosine, phenylalanine or kynureine
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-
?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
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?, r
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
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
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additional information
additional information
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steady-state kinetics analysis
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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activity of recombinant isozymes from different E. coli host strains
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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nuclear-encoded protein that is translated on cytosolic ribosomes and subsequently imported into plastids
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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
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 alpha-helices surrounding six parallel and one anti-parallel beta-strand. Two additional alpha-helices in the PLP-binding pocket, as well as the alpha-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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no difference in thermostability between plants of genotypes acclimated at 4 different thermoperiods
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
aspartate aminotransferase construct consists of the Arabidopsis thaliana ASP5 coding region followed by mGFP5. This construct is designated SP5:GFP. GFP is fused to the carboxy-terminus of ASP5 to preserve the cleavage site between the ASP5 transit peptide and mature protein, thus ensuring proper plastid import and processing. A five amino acid linker peptide (GSGGG) is inserted between ASP5 and GFP to promote proper folding and activity of both proteins. The constructs are introduced into Nicotiana tabacum cv. Samsun NN via Agrobacterium-mediated transformation of leaf strips. ASP5:GFP is present in stromules of Nicotiana tabacum. Arabidopsis thaliana ASP5, with GFP fused to its carboxy-terminus, can interact with itself and with the Nicotiana tabacum AAT3 to form enzymes that are functional in vitro
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Potvin, C.; Simon, J.P.; Blanchard, M.H.
Thermal properties of NAD malate dehydrogenase and glutamate oxaloacetate transaminase in two genotypes of Arabidopsis thaliana (Cruciferae) from contrasting environments
Plant Sci. Lett.
31
35-47
1983
Arabidopsis thaliana
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Wilkie, S.E.; Warren, M.J.
Recombinant expression, purification, and characterization of three isoenzymes of aspartate aminotransferase from Arabidopsis thaliana
Protein Expr. Purif.
12
381-389
1998
Arabidopsis thaliana
Kwok, E.Y.; Hanson, M.R.
GFP-labelled Rubisco and aspartate aminotransferase are present in plastid stromules and traffic between plastids
J. Exp. Bot.
55
595-604
2004
Arabidopsis thaliana
de la Torre, F.; De Santis, L.; Suarez, M.F.; Crespillo, R.; Canovas, F.M.
Identification and functional analysis of a prokaryotic-type aspartate aminotransferase: implications for plant amino acid metabolism
Plant J.
46
414-425
2006
Oryza sativa, Pinus pinaster (Q5F4K8), Arabidopsis thaliana (Q9SIE1)
Schlueter, U.; Braeutigam, A.; Droz, J.M.; Schwender, J.; Weber, A.P.M.
The role of alanine and aspartate aminotransferases in C4 photosynthesis
Plant Biol.
21 Suppl 1
64-76
2019
Amaranthus caudatus, Arabidopsis thaliana, Atriplex rosea, Flaveria bidentis, Oryza sativa, Megathyrsus maximus, Panicum miliaceum, Setaria italica, Setaria viridis, Sorghum bicolor, Zea mays, Flaveria robusta, Atriplex prostrata, Panicum virgatum, Gynandropsis gynandra, Tarenaya hassleriana, Dichanthelium clandestinum, Alloteropsis semialata subsp. eckloniana, Alloteropsis semialata
EXTERNAL LINKS (specific for EC-Number 2.6.1.1)
Transporter Classification Database (TCDB): 9.A.70.1.1
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