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Literature summary for 2.6.1.1 extracted from

  • 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 (1998), J. Biol. Chem., 273, 29554-29564.
    View publication on PubMed
Search for more literature for 2.6.1.1

Cloned(Commentary)

Cloned (Comment) Organism
gene aspC, expression of wild-type and K109 mutants in Escherichia coli BL21(DE3) Thermus thermophilus

Protein Variants

Protein Variants Comment Organism
K109S site-directed mutagenesis, loss of activity towards acidic substrates, increased activity towards the neutral substrate alanine, increase in pKa value Thermus thermophilus
K109V site-directed mutagenesis, loss of activity towards acidic substrates, increased activity towards the neutral substrate alanine Thermus thermophilus

Inhibitors

Inhibitors Comment Organism Structure
2-methyl-DL-aspartate binds to the pyridoxal 5'-phosphate form of the enzyme, formation of an external aldimine complex Thermus thermophilus
Maleate binds noncovalently to the pyridoxal 5'-phosphate form of the enzyme Thermus thermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics Escherichia coli
additional information
-
 additional information kinetics Thermus thermophilus
additional information
-
 additional information wild-type and mutants Escherichia coli
additional information
-
 additional information wild-type and mutants Thermus thermophilus
1.7
-
 L-aspartate wild-type, pH 8.0, 25°C Thermus thermophilus
2.4
-
 2-oxoglutarate wild-type, pH 8.0, 25°C Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate + 2-oxoglutarate Escherichia coli
-
 oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate Thermus thermophilus
-
 oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
 oxaloacetate + L-glutamate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Thermus thermophilus Q56232
-
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q56232
-
-

Reaction

Reaction Comment Organism Reaction ID
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate active site structure, substrate recognition mechanism Escherichia coli
a
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate active site structure, substrate recognition mechanism Thermus thermophilus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine + 2-oxoglutarate
-
 Thermus thermophilus pyruvate + L-glutamate
-
 r
L-alanine + 2-oxoglutarate
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 pyruvate + L-glutamate
-
 r
L-aspartate + 2-oxoglutarate
-
 Escherichia coli oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate
-
 Escherichia coli oxaloacetate + L-glutamate
-
 r
L-aspartate + 2-oxoglutarate
-
 Thermus thermophilus oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate enzyme can also act on neutral amino acid substrates due to a substrate-binding pocket with a more flexible conformation, Lys109 is the major determinant for the acidic substrate specificity Thermus thermophilus oxaloacetate + L-glutamate
-
 r
L-aspartate + 2-oxoglutarate
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate enzyme can also act on neutral amino acid substrates due to a substrate-binding pocket with a more flexible conformation, Lys109 is the major determinant for the acidic substrate specificity Thermus thermophilus HB8 / ATCC 27634 / DSM 579 oxaloacetate + L-glutamate
-
 r

Synonyms

Synonyms Comment Organism
AspAT
-
 Escherichia coli
AspAT
-
 Thermus thermophilus
More 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 Escherichia coli
More 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 Thermus thermophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
120
-
 2-oxoglutarate wild-type, pH 8.0, 25°C Thermus thermophilus
120
-
 L-aspartate wild-type, pH 8.0, 25°C Thermus thermophilus