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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
21817 Ensembl ENSG00000198959 ENSMUSG00000037820 UniProt P21980 P21981 RefSeq (mRNA) NM_004613 NM_198951 NM_001323316 NM_001323317 NM_001323318 NM_009373 RefSeq (protein) NP_001310245 NP_001310246 NP_001310247 NP_004604 NP_945189 NP_033399 Location (UCSC) Chr 20: 38.13 – 38.17 Mb Chr 2: 157.96 – 157.99 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Protein-glutamine gamma ...
The upper reaction shows how a transaminase combines with a glutamine residue, releasing ammonia, and then the combination reacts with the amine group of a lysine residue of another protein, setting the enzyme free again. Nine transglutaminases have been characterised in humans, [5] eight of which catalyse transamidation reactions.
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
The first part of the mechanism occurs in the active site of the glutaminase domain and releases an ammonia group from glutamine by hydrolysis. The ammonia released by the first reaction is then transferred to the active site of the phosphoribosyltransferase domain via a 20 Å channel, where it then binds to PRPP to form PRA.
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.
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.
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.