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Literature summary for 4.1.1.15 extracted from

  • Capitani, G.; De Biase, D.; Aurizi, C.; Gut, H.; Bossa, F.; Grutter, M.G.
    Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase (2003), EMBO J., 22, 4027-4037.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.15

Crystallization (Commentary)

Crystallization (Comment) Organism
isoform GadB, native and reduced, vapour diffusion method Escherichia coli

Protein Variants

Protein Variants Comment Organism
K276A no decarboxylation of L-Glu. Transition temperature is 11°C higher than that of the wild-type enzyme. Limited proteolysis by trypsin shows that the mutant enzyme is more resistant to proteolytic degradation than the wild-type enzyme. Mutant enzyme contains very little pyridoxal 5'-phosphate Escherichia coli
K276H no decarboxylation of L-Glu. Transition temperature is 4°C higher than that of the wild-type enzyme. Mutant enzyme contains no pyridoxal 5'-phosphate Escherichia coli

General Stability

General Stability Organism
limited proteolysis by trypsin shows that the mutant enzyme is more resistant to proteolytic degradation than the wild-type enzyme Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm localized exclusively in cytoplasm at neutral pH, but is recruited to the membrane when the pH falls Escherichia coli 5737
-
membrane localized exclusively in cytoplasm at neutral pH, but is recruited to the membrane when the pH falls Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli GadB together with the antiporter gadC constitutes the gad acid resistance system, which confers the ability for bacterial survival for at least 2 h in a strongly acidic environment ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
mutant enzymes K276A and K276H Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Glu
-
 Escherichia coli 4-Aminobutanoate + CO2
-
 ?
additional information GadB together with the antiporter gadC constitutes the gad acid resistance system, which confers the ability for bacterial survival for at least 2 h in a strongly acidic environment Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
hexamer
-
 Escherichia coli

Synonyms

Synonyms Comment Organism
GadB
-
 Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
51
-
 transition temperature of wild-type enzyme Escherichia coli
55
-
 transition temperature of mutant enzyme K276H Escherichia coli
62
-
 transition temperature of mutant enzyme K276A Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate the inactive mutant enzyme k276A contains very little pyridoxal 5'-phosphate, the inactive mutant enzyme K276H contains no pyridoxal 5'-phosphate Escherichia coli