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Literature summary for 4.1.1.15 extracted from

  • Wang, Q.; Xin, Y.; Zhang, F.; Feng, Z.; Fu, J.; Luo, L.; Yin, Z.
    Enhanced ?-aminobutyric acid-forming activity of recombinant glutamate decarboxylase (gadA) from Escherichia coli (2011), World J. Microbiol. Biotechnol., 27, 693-700.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

General Stability

General Stability Organism
by entrapping Escherichia coli glutamate decarboxylase into sodium alginate and carrageenan gel beads, the activity of immobilized GAD remains 85% during the initial five batches and the activity still remains 50% at the tenth batch Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ maximum (174%) activity in the presence of 0.6 mM Ca2+ Escherichia coli
Mn2+ the optimal concentration (7.5 mM) of Mn2+ can also improve the activity of recombinant enzyme (164%), but the co-effect of Ca2+ and Mn2+ exhibits antagonism effect when added simultaneously Escherichia coli

Organism

Organism UniProt Comment Textmining
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
GAD
-
Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.8
-
-
Escherichia coli

Cofactor

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