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Literature summary for 2.6.1.19 extracted from

  • Liu, W.; Peterson, P.E.; Langston, J.A.; Jin, X.; Zhou, X.; Fisher, A.J.; Toney, M.D.
    Kinetic and crystallographic analysis of active site mutants of Escherichia coli gamma-aminobutyrate aminotransferase (2005), Biochemistry, 44, 2982-2992.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant I50Q, V241A, E211S Escherichia coli

Protein Variants

Protein Variants Comment Organism
E211S crystallization data, decrease in kcat, decrease in Km-value for 2-oxoglutarate Escherichia coli
E211S/I50G drastic decrease in kcat-value Escherichia coli
E211S/I50G/C77K 10fold increase in decarboxylation activity Escherichia coli
E211S/I50G/C77R drastic decrease in kcat-value Escherichia coli
E211S/I50H/V80D 10fold increase in decarboxylation activity, change of reaction specificity to that of a decarboxylase Escherichia coli
E211S/I50H/V80T decrease in kcat, decrease in Km-value for 2-oxoglutarate Escherichia coli
E211S/I50N/V80D drastic decrease in kcat-value Escherichia coli
E211S/I50N/V80T drastic decrease in kcat-value Escherichia coli
E211S/I50Q/G295Y/V241A drastic decrease in kcat-value Escherichia coli
I50Q crystallization data, decrease in kcat, increase in Km-values Escherichia coli
I50Q/G295Y decrease in kcat, decrease in Km-value for 2-oxoglutarate Escherichia coli
V241A crystallization data, decrease in kcat, decrease in Km-value for 2-oxoglutarate Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2-oxoglutarate substrate inhibition Escherichia coli
Aminooxyacetate
-
Escherichia coli
Glutarate
-
Escherichia coli
Maleate
-
Escherichia coli
additional information no substrate inhibition: 4-aminobutanoate Escherichia coli
succinate
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0021
-
2-oxoglutarate mutant E211S, 25°C, pH 7.8 Escherichia coli
0.063
-
2-oxoglutarate mutant E211S/I50H/V80T, 25°C, pH 7.8 Escherichia coli
0.13
-
2-oxoglutarate mutant V241A, 25°C, pH 7.8 Escherichia coli
0.72
-
2-oxoglutarate mutant E211S/I50G/C77K, 25°C, pH 7.8 Escherichia coli
0.78
-
2-oxoglutarate mutant I50Q/G295Y, 25°C, pH 7.8 Escherichia coli
1.07
-
2-oxoglutarate wild-type, 25°C, pH 7.8 Escherichia coli
4.7
-
4-aminobutanoate mutant I50Q/G295Y, 25°C, pH 7.8 Escherichia coli
5.8
-
4-aminobutanoate wild-type, 25°C, pH 7.8 Escherichia coli
5.9
-
4-aminobutanoate mutant E211S/I50G/C77K, 25°C, pH 7.8 Escherichia coli
30
-
4-aminobutanoate mutant V241A, 25°C, pH 7.8 Escherichia coli
46
-
2-oxoglutarate mutant I50Q, 25°C, pH 7.8 Escherichia coli
68
-
4-aminobutanoate mutant I50Q, 25°C, pH 7.8 Escherichia coli
86
-
4-aminobutanoate mutant E211S, 25°C, pH 7.8 Escherichia coli
146
-
4-aminobutanoate mutant E211S/I50H/V80T, 25°C, pH 7.8 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P22256
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-aminobutanoate + 2-oxoglutarate
-
Escherichia coli 4-oxobutanoate + L-glutamate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00023
-
4-aminobutanoate mutant E211S/I50H/V80D, 25°C, pH 7.8 Escherichia coli
0.0005
-
4-aminobutanoate mutant E211S/I50G/C77R, 25°C, pH 7.8 Escherichia coli
0.003
-
4-aminobutanoate mutant E211S/I50G, 25°C, pH 7.8 Escherichia coli
0.004
-
4-aminobutanoate mutant E211S/I50Q/G295Y/V241A, 25°C, pH 7.8 Escherichia coli
0.0058
-
4-aminobutanoate mutant E211S/I50N/V80T, 25°C, pH 7.8 Escherichia coli
0.0075
-
4-aminobutanoate mutant E211S/I50N/V80D, 25°C, pH 7.8 Escherichia coli
0.028
-
4-aminobutanoate mutant I50Q/G295Y, 25°C, pH 7.8 Escherichia coli
0.106
-
4-aminobutanoate mutant E211S/I50H/V80T, 25°C, pH 7.8 Escherichia coli
0.25
-
4-aminobutanoate mutant E211S/I50G/C77K, 25°C, pH 7.8 Escherichia coli
0.56
-
4-aminobutanoate mutant E211S, 25°C, pH 7.8 Escherichia coli
1.93
-
4-aminobutanoate mutant V241A, 25°C, pH 7.8 Escherichia coli
13.5
-
4-aminobutanoate mutant I50Q, 25°C, pH 7.8 Escherichia coli
47.4
-
4-aminobutanoate wild-type, 25°C, pH 7.8 Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.24
-
Aminooxyacetate
-
Escherichia coli
0.62
-
Aminooxyacetate wild-type, pH 7.8, 25°C Escherichia coli
1.13
-
Aminooxyacetate mutant V241A, pH 7.8, 25°C Escherichia coli
3.9
-
Maleate wild-type, pH 7.8, 25°C Escherichia coli
19
-
Glutarate wild-type, pH 7.8, 25°C Escherichia coli
27
-
succinate wild-type, pH 7.8, 25°C Escherichia coli
46
-
Maleate mutant I50Q, pH 7.8, 25°C Escherichia coli
140
-
Glutarate mutant V241A, pH 7.8, 25°C Escherichia coli
197
-
succinate mutant I50Q, pH 7.8, 25°C Escherichia coli
233
-
Glutarate mutant I50Q, pH 7.8, 25°C Escherichia coli
720
-
succinate mutant V241A, pH 7.8, 25°C Escherichia coli
780
-
Maleate mutant V241A, pH 7.8, 25°C Escherichia coli