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Glutaminase (EC 3.5.1.2, glutaminase I, L-glutaminase, glutamine aminohydrolase) is an amidohydrolase enzyme that generates glutamate from glutamine. Glutaminase has tissue-specific isoenzymes. Glutaminase has an important role in glial cells. Glutaminase catalyzes the following reaction: Glutamine + H 2 O → glutamate + NH + 4
Examples of foods made using transglutaminase include imitation crabmeat, and fish balls. It is produced by Streptomyces mobaraensis fermentation in commercial quantities ( P81453 ) or extracted from animal blood, [ 13 ] and is used in a variety of processes, including the production of processed meat and fish products.
Glutamine synthetase catalyzed reaction. Glutamine synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. [4] The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites. [5] Other reactions may take place via GS.
Catalyzing enzyme: glutaminase (EC 3.5.1.2) 2. Glutamate can be excreted or can be further metabolized to α-ketoglutarate. For the conversion of glutamate to α-ketoglutarate three different reactions are possible: Catalyzing enzymes: glutamate dehydrogenase (GlDH), EC 1.4.1.2
In enzymology, a NAD + synthase (glutamine-hydrolysing) (EC 6.3.5.1) is an enzyme that catalyzes the chemical reaction. ATP + deamido-NAD + + L-glutamine + H 2 O AMP + diphosphate + NAD + + L-glutamate. In eukaryotes, this enzyme contains a glutaminase domain related to nitrilase. [1]
In enzymology, a glutamine-pyruvate transaminase (EC 2.6.1.15) is an enzyme that catalyzes the chemical reaction. L-glutamine + pyruvate 2-oxoglutaramate + L-alanine. Thus, the two substrates of this enzyme are L-glutamine and pyruvate, whereas its two products are 2-oxoglutaramate and L-alanine.
In enzymology, a protein-glutamine glutaminase (EC 3.5.1.44) is an enzyme that catalyzes the chemical reaction. protein L-glutamine + H 2 O protein L-glutamate + NH 3. Thus, the two substrates of this enzyme are protein L-glutamine and H 2 O, whereas its two products are protein L-glutamate and NH 3.
Tissue transglutaminase (abbreviated as tTG or TG2) is a 78-kDa, calcium-dependent enzyme (EC 2.3.2.13) of the protein-glutamine γ-glutamyltransferases family (or simply transglutaminase family).