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Literature summary for 4.1.1.15 extracted from

  • Pennacchietti, E.; Lammens, T.M.; Capitani, G.; Franssen, M.C.; John, R.A.; Bossa, F.; De Biase, D.
    Mutation of His465 alters the pH-dependent spectroscopic properties of Escherichia coli glutamate decarboxylase and broadens the range of its activity toward more alkaline pH (2009), J. Biol. Chem., 284, 31587-31596.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
H465A the mutant is active at pH well above 5.7 and shows 78% of wild type specific activity in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C in the presence of 0.1 mM pyridoxal 5'-phosphate Escherichia coli
additional information the mutant GadBDELTAHT (His465 of GadB is deleted together with the last residue in the polypeptide chain, Thr466) is active at pH well above 5.7 and shows 52% of wild type specific activity in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C in the presence of 0.1 mM pyridoxal 5'-phosphate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.51
-
 L-glutamate mutant enzyme H465A, in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C Escherichia coli
1.61
-
 L-glutamate mutant enzyme DELTAHT, in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C Escherichia coli
2.32
-
 L-glutamate wild type enzyme, in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P69910
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-Sepharose column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate
-
 Escherichia coli 4-aminobutanoate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
GadB
-
 Escherichia coli
Glutamic acid decarboxylase
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
16.24
-
 L-glutamate mutant enzyme DELTAHT, in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C Escherichia coli
20.75
-
 L-glutamate mutant enzyme H465A, in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C Escherichia coli
24.85
-
 L-glutamate wild type enzyme, in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.8 4.6 at mildly alkaline pH GadB is inactive Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
10.08
-
 L-glutamate mutant enzyme DELTAHT, in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C Escherichia coli
10.71
-
 L-glutamate wild type enzyme, in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C Escherichia coli
13.74
-
 L-glutamate mutant enzyme H465A, in 0.2 M pyridine/HCl buffer, pH 4.6, at 37°C Escherichia coli