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Literature summary for 2.6.1.1 extracted from

  • Wu, H.J.; Yang, Y.; Wang, S.; Qiao, J.Q.; Xia, Y.F.; Wang, Y.; Wang, W.D.; Gao, S.F.; Liu, J.; Xue, P.Q.; Gao, X.W.
    Cloning, expression and characterization of a new aspartate aminotransferase from Bacillus subtilis B3 (2011), FEBS J., 278, 1345-1357.
    View publication on PubMed
Search for more literature for 2.6.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
D232N mutant shows no activity Bacillus subtilis
K270H mutant shows no activity Bacillus subtilis
R403Y mutant shows no activity Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.3
-
 2-oxoglutarate pH 8.0, 45°C Bacillus subtilis
0.6
-
 oxaloacetate pH 8.0, 45°C Bacillus subtilis
6.7
-
 L-aspartate pH 8.0, 45°C Bacillus subtilis
8
-
 L-glutamate pH 8.0, 45°C Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
CaCl2 1 mM relative activity: 115.5% Bacillus subtilis
CoCl2 1 mM relative activity: 122.1% Bacillus subtilis
CuSO4 1 mM relative activity: 84.3% Bacillus subtilis
EDTA 1 mM relative activity: 106.4% Bacillus subtilis
MgCl2 1 mM relative activity: 96.9% Bacillus subtilis
MnSO4 1 mM relative activity: 90.1% Bacillus subtilis
ZnSO4 1 mM relative activity: 99.7% Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
49100
-
 calculated from cDNA Bacillus subtilis
55000
-
 SDS-PAGE Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis Q939C9
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate relative activity L-aspartate: 100% Bacillus subtilis oxaloacetate + L-glutamate
-
 ?
L-aspartate + oxaloacetate relative activity compared to 2-oxoglutarate: 81.5% Bacillus subtilis ?
-
 ?
L-glutamate + 2-oxoglutarate relative activity compared to L-aspartate: 46.7% Bacillus subtilis 2-oxoglutarate + L-glutamate
-
 ?
L-phenylalanine + 2-oxoglutarate relative activity compared to L-aspartate: 0.3% Bacillus subtilis 2-oxo-3-phenylpropionic acid + L-glutamate
-
 ?
L-tryptophan + 2-oxoglutarate relative activity compared to L-aspartate: 1.7% Bacillus subtilis 3-indole-2-oxopropionic acid + L-glutamate
-
 ?
L-tyrosine + 2-oxoglutarate relative activity compared to L-aspartate: 0.4 Bacillus subtilis 3-(4-hydroxyphenyl)-2-oxopropionic acid + L-glutamate
-
 ?

Subunits

Subunits Comment Organism
monomer
-
 Bacillus subtilis

Synonyms

Synonyms Comment Organism
aatB3
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 enzyme stable up to 50°C Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
14
-
 L-glutamate pH 8.0, 45°C Bacillus subtilis
22
-
 oxaloacetate pH 8.0, 45°C Bacillus subtilis
27
-
 2-oxoglutarate pH 8.0, 45°C Bacillus subtilis
30
-
 L-aspartate pH 8.0, 45°C Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
7 9 relatively high activity in alkaline range Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Bacillus subtilis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.75
-
 L-glutamate pH 8.0, 45°C Bacillus subtilis
4.5
-
 L-aspartate pH 8.0, 45°C Bacillus subtilis
36.67
-
 oxaloacetate pH 8.0, 45°C Bacillus subtilis
84.38
-
 2-oxoglutarate pH 8.0, 45°C Bacillus subtilis