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Literature summary for 4.1.1.15 extracted from

  • Xiong, Q.; Xu, Z.; Xu, L.; Yao, Z.; Li, S.; Xu, H.
    Efficient production of gamma-GABA using recombinant E. coli expressing glutamate decarboxylase (GAD) derived from eukaryote Saccharomyces cerevisiae (2017), Appl. Biochem. Biotechnol., 183, 1390-1400 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene gad, DNA and amino acid sequence determination and analysis, sequence comparisons, functional recombinant expression of soluble His-tagged enzyme in Escherichia coli strain BL21(DE3) Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information optimization of bioproduction of gamma-GABA using recombinant Escherichia coli expressing a GAD enzyme derived from eukaryote. The optimal medium for Escherichia coli-ScGAD cultivation and expression is 10 g/l lactose, 5 g/l glycerol, 20 g/l yeast extract, and 10 g/l sodium chloride, resulting in an activity of 55 U/ml medium, three times higher than that of using Luria-Bertani (LB) medium. The maximal concentration of gamma-GABA is 245 g/l whereas L-glutamic acid is near completely converted Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
11.4
-
L-glutamate pH 4.2, 37°C, recombinant enzyme Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate Saccharomyces cerevisiae
-
4-aminobutanoate + CO2
-
?
L-glutamate Saccharomyces cerevisiae NX-1
-
4-aminobutanoate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae NX-1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration, to homogeneity Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate
-
Saccharomyces cerevisiae 4-aminobutanoate + CO2
-
?
L-glutamate
-
Saccharomyces cerevisiae NX-1 4-aminobutanoate + CO2
-
?

Subunits

Subunits Comment Organism
? x * 66000, recombinant His-tagged enzyme, SDS-PAGE, x * 65986, sequence calculation Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
GAD
-
Saccharomyces cerevisiae
ScGAD
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.537
-
L-glutamate pH 4.2, 37°C, recombinant enzyme Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2
-
-
Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
additional information the cofactor of ScGAD is verified to be either pyridoxal 5'-phosphate (PLP) or pyridoxal. The optimal concentration of either cofactor is 50 mg/l. GAD requires a coenzyme for activity while inactive apo-GAD forms a GAD-PLP complex (holo-GAD) to obtain its activity Saccharomyces cerevisiae
pyridoxal 5'-phosphate
-
Saccharomyces cerevisiae