Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ouchi, T.; Tomita, T.; Miyagawa, T.; Kuzuyama, T.; Nishiyama, M.
    Dual roles of a conserved pair, Arg23 and Ser20, in recognition of multiple substrates in alpha-aminoadipate aminotransferase from Thermus thermophilus (2009), Biochem. Biophys. Res. Commun., 388, 21-27.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.39 expressed in Escherichia coli BL21(DE3) cells Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.39 complexed with N-(5'-phosphopyridoxyl)-L-glutamate, vapor diffusion method, using 16% (w/v) PEG3350, 100 mM HEPES, pH 7.0, and 200 mM calcium acetate, at 20°C Thermus thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
2.6.1.39 R23A the mutation causes 4.1fold increase in the Km value for L-2-aminoadipate, the Km value for L-Glu increases 546fold, the Km value for L-Leu is not greatly affected Thermus thermophilus
2.6.1.39 R23Q the mutation causes 13.7fold increase in the Km value for L-2-aminoadipate, the Km value for L-Glu increases 134fold, the Km value for L-Leu is not greatly affected Thermus thermophilus
2.6.1.39 S20E the mutant shows decreased kcat values compared to the wild type enzyme Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.39 0.048
-
2-oxoisocaproate mutant enzyme R23A, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.05
-
2-oxoisocaproate mutant enzyme S20E, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.091
-
2-oxoisocaproate mutant enzyme R23Q, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.2
-
L-leucine mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.27
-
2-oxoglutarate wild type enzyme, using L-leucine as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.3
-
2-oxoglutarate wild type enzyme, using L-2-aminoadipate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.39
-
L-leucine mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.4
-
2-oxoglutarate mutant enzyme S20E, using L-leucine as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.41
-
2-oxoglutarate mutant enzyme S20E, using L-2-aminoadipate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.42
-
2-oxoglutarate mutant enzyme R23Q, using L-2-aminoadipate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.43
-
2-oxoisocaproate wild type enzyme, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.46
-
L-glutamate wild type enzyme, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.54
-
2-oxoglutarate mutant enzyme R23A, using L-2-aminoadipate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.55
-
2-oxoglutarate mutant enzyme R23Q, using L-leucine as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.61
-
2-oxoglutarate mutant enzyme R23A, using L-leucine as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.81
-
L-2-aminoadipate wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.88
-
L-leucine mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.95
-
L-leucine wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 3.3
-
L-2-aminoadipate mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 7
-
L-2-aminoadipate mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 11
-
L-2-aminoadipate mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 62
-
L-glutamate mutant enzyme R23Q, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 82
-
L-glutamate mutant enzyme S20E, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 250
-
L-glutamate mutant enzyme R23A, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.39 Thermus thermophilus Q72LL6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.39 ammonium sulfate precipitation and Superdex 200 gel filtration Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.39 2-oxoisocaproate + L-glutamate
-
Thermus thermophilus ?
-
?
2.6.1.39 L-2-aminoadipate + 2-oxoglutarate
-
Thermus thermophilus 2-oxoadipate + L-glutamate
-
?
2.6.1.39 L-leucine + 2-oxoglutarate
-
Thermus thermophilus 4-methyl-2-oxopentanoate + L-glutamate
-
?
2.6.1.39 additional information negligible activity is observed for L-Asp Thermus thermophilus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.6.1.39 AAA-AT
-
Thermus thermophilus
2.6.1.39 alpha-aminoadipate aminotransferase
-
Thermus thermophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.39 0.009
-
L-leucine mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.011
-
L-2-aminoadipate mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.023
-
L-leucine mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.04
-
L-2-aminoadipate mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.05
-
L-leucine mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.083
-
L-2-aminoadipate mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.23
-
L-glutamate mutant enzyme R23A, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.5
-
L-glutamate mutant enzyme R23Q, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 1.2
-
L-glutamate mutant enzyme S20E, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 5.1
-
L-leucine wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 6.7
-
L-2-aminoadipate wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 16
-
L-glutamate wild type enzyme, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.39 pyridoxal 5'-phosphate
-
Thermus thermophilus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.6.1.39 0.0009
-
L-glutamate mutant enzyme R23A, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.0033
-
L-2-aminoadipate mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.0057
-
L-2-aminoadipate mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.0075
-
L-2-aminoadipate mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.0081
-
L-glutamate mutant enzyme R23Q, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.014
-
L-glutamate mutant enzyme S20E, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.015
-
2-oxoglutarate mutant enzyme R23A, using L-leucine as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.021
-
2-oxoglutarate mutant enzyme R23A, using L-2-aminoadipate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.023
-
L-leucine mutant enzyme R23A, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.057
-
L-leucine mutant enzyme R23Q, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.06
-
2-oxoglutarate mutant enzyme S20E, using L-leucine as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.091
-
2-oxoglutarate mutant enzyme R23Q, using L-leucine as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.097
-
2-oxoglutarate mutant enzyme S20E, using L-2-aminoadipate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.12
-
L-leucine mutant enzyme S20E, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 0.2
-
2-oxoglutarate mutant enzyme R23Q, using L-2-aminoadipate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 4.8
-
2-oxoisocaproate mutant enzyme R23A, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 5.4
-
L-leucine wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 5.5
-
2-oxoisocaproate mutant enzyme R23Q, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 8.2
-
L-2-aminoadipate wild type enzyme, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 19
-
2-oxoglutarate wild type enzyme, using L-leucine as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 22
-
2-oxoglutarate wild type enzyme, using L-2-aminoadipate as cosubstrate, in 50 mM HEPES-NaOH buffer, pH 8.0, 50 mM KCl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 24
-
2-oxoisocaproate mutant enzyme S20E, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 34
-
2-oxoisocaproate wild type enzyme, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus
2.6.1.39 37
-
L-glutamate wild type enzyme, using 2-oxoisocaproate as cosubstrate, in 50 mM HEPES–NaOH buffer, pH 8.0, containing 50 mM NH4Cl, 0.15 mM pyridoxal 5'-phosphate, at 45°C Thermus thermophilus