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Literature summary for 4.1.1.15 extracted from

  • Sankar, B.; Kishore, S.; Saurav, D.; Madhumita, B.
    Structural and functional analysis of glutamate decarboxylase system in Bacillus aryabhattai (2016), Res. J. Biotechnol., 11, 1-11 .
No PubMed abstract available
Search for more literature for 4.1.1.15

Cloned(Commentary)

Cloned (Comment) Organism
gene gad, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree Priestia aryabhattai

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Priestia aryabhattai
2.02
-
 L-glutamate pH 5.6, 35°C Priestia aryabhattai

Localization

Localization Comment Organism GeneOntology No. Textmining
intracellular
-
 Priestia aryabhattai 5622
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate Priestia aryabhattai
-
 4-aminobutanoate + CO2
-
 ?
L-glutamate Priestia aryabhattai B8W22
-
 4-aminobutanoate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Priestia aryabhattai
-
 strain AM is isolated from acidic soil of Golaghat district of Assam, India, and shows 99.86% sequence similarity with strain B8W22
-
Priestia aryabhattai B8W22
-
 strain AM is isolated from acidic soil of Golaghat district of Assam, India, and shows 99.86% sequence similarity with strain B8W22
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme by gel filtration, two different steps of anion exchange chromatography, and ultrafiltration Priestia aryabhattai

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate
-
 Priestia aryabhattai 4-aminobutanoate + CO2
-
 ?
L-glutamate
-
 Priestia aryabhattai B8W22 4-aminobutanoate + CO2
-
 ?
additional information enzyme activity detection by rapid pH indicator method. No activity with D-glutamic acid and 2-methyl-DL-glutamic acid Priestia aryabhattai ?
-
 ?
additional information enzyme activity detection by rapid pH indicator method. No activity with D-glutamic acid and 2-methyl-DL-glutamic acid Priestia aryabhattai B8W22 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 53000, SDS-PAGE Priestia aryabhattai

Synonyms

Synonyms Comment Organism
GAD
-
 Priestia aryabhattai

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Priestia aryabhattai

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
15 60 activity range, profile overview Priestia aryabhattai

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
-
 Priestia aryabhattai

pH Range

pH Minimum pH Maximum Comment Organism
2.5 7.5 activity range, profile overview Priestia aryabhattai

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on Priestia aryabhattai

pI Value

Organism Comment pI Value Maximum pI Value
Priestia aryabhattai sequence calculation
-
 4.87

General Information

General Information Comment Organism
evolution different morphological, biochemical and chemotaxonomic characteristics of the strains AM and strain B8W22 Priestia aryabhattai
additional information enzyme three-dimensional structure modelling, overview Priestia aryabhattai
physiological function the activity of glutamate decarboxylase (GAD) has the ability to confer tolerance to various stress conditions including soil acidity. This pyridoxal 5'-phosphate based enzyme plays an important role in pH homeostasis by catalysing the decarboxylation of glutamate to gamma-aminobutyrate Priestia aryabhattai