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Information on EC 2.6.1.1 - aspartate transaminase and Organism(s) Thermus thermophilus and UniProt Accession Q56232

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.1 aspartate transaminase
IUBMB 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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This record set is specific for:
Thermus thermophilus
UNIPROT: Q56232
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The taxonomic range for the selected organisms is: Thermus thermophilus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-oxoglutarate-glutamate aminotransferase
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AAT
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aminotransferase, aspartate
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-
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aspartate alpha-ketoglutarate transaminase
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-
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aspartate aminotransferase
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-
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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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protein TT0402
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transaminase A
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additional information
aspartate aminotransferases are divided into 2 subgroups: subgroup Ia, inclusive the enzyme of Escherichia coli, posses Arg292 for substrate binding and show a specificity for acidic substrates only, subgroup Ib, inclusive the enzyme of Thermus thermophilus, can utilize acidic as well as neutral substrates
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
active site structure, substrate recognition mechanism
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
show the reaction diagram
bi bi ping pong reaction kinetic
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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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 hide
9000-97-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-alanine + 2-oxoglutarate
pyruvate + L-glutamate
show the reaction diagram
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r
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
L-glutamate + 2-oxoglutarate
2-oxoglutarate + L-glutamate
show the reaction diagram
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-
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
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?
L-aspartate + 2-oxoglutarate
oxaloacetate + L-glutamate
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-methyl-DL-aspartate
binds to the pyridoxal 5'-phosphate form of the enzyme, formation of an external aldimine complex
Maleate
binds noncovalently to the pyridoxal 5'-phosphate form of the enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4
2-oxoglutarate
wild-type, pH 8.0, 25°C
1.7
L-aspartate
wild-type, pH 8.0, 25°C
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
120
2-oxoglutarate
wild-type, pH 8.0, 25°C
120
L-aspartate
wild-type, pH 8.0, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
112.1
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purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native and selenomethionine-substituted TT0402 proteins are crystallized in hanging drops at 4°C
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K109S
site-directed mutagenesis, loss of activity towards acidic substrates, increased activity towards the neutral substrate alanine, increase in pKa value
K109V
site-directed mutagenesis, loss of activity towards acidic substrates, increased activity towards the neutral substrate alanine
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
-
stable up to
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant from overproducing Escherichia coli AB1157 cells, 66fold
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aspC, expression of wild-type and K109 mutants in Escherichia coli BL21(DE3)
cloning, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli AB1157
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expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okamoto, A.; Kato, R.; Masui, R.; Yamagishi, A.; Oshima, T.; Kuramitsu, S.
An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8
J. Biochem.
119
135-144
1996
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Manually annotated by BRENDA team
Nobe, Y.; Kawaguchi, S.; Ura, H.; Nakai, T.; Hirotsu, K.; Kato, R.; Kuramitsu, S.
The novel substrate recognition mechanism utilized by aspartate aminotransferase of the extreme thermophile Thermus thermophilus HB8
J. Biol. Chem.
273
29554-29564
1998
Escherichia coli, Thermus thermophilus (Q56232), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q56232)
Manually annotated by BRENDA team
Ktasura, Y.; Shirouzu, M.; Yamaguchi, H.; Ishitani, R.; Nureki, O.; Kuramitsu, S.; Hayashi, H.; Yokoyama, S.
Crystal structure of a putative aspartate aminotransferase belonging to subgroup IV
Proteins Struct. Funct. Bioinform.
55
487-492
2004
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Manually annotated by BRENDA team