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Literature summary for 4.1.1.15 extracted from

  • Su, L.; Huang, Y.; Wu, J.
    Enhanced production of recombinant Escherichia coli glutamate decarboxylase through optimization of induction strategy and addition of pyridoxine (2015), Biores. Technol., 198, 63-69 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene gad, recombinant lactose-induced overexpression of enzyme GAD in Escherichia coli strain BL21(DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information enhanced production of recombinant Escherichia coli glutamate decarboxylase through optimization of induction strategy and addition of pyridoxine, different induction strategies are investigated, induction is optimal when the temperature is maintained at 30°C, the inducer lactose is fed at a rate of 0.2 g/l/h, and protein expression is induced when the cell density (OD600) reaches 50. Under these conditions, the GAD activity of 1273.8 U/ml is achieved. The supplementing the medium with 2 mM pyridoxine hydrochloride (PN), a cheap and stable PLP precursor, at the initiation of protein expression, and then again 10 h later, results in very high GAD activity of 3193.4 U/ml. Fed-batch cultivation in a 3.6-L fermentor at 37°C and pH 7.0 Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P69910
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
GAD
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.8
-
assay at Escherichia coli

Cofactor

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