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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
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 ammonia produced in neurons is fixed into α-ketoglutarate by the glutamate-dehydrogenase reaction to form glutamate, then transaminated by alanine aminotransferase into lactate-derived pyruvate to form alanine, which is exported to astrocytes. In the astrocytes, this process is then reversed, and lactate is transported in the other direction.
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 ...
GLS2 is a part of the glutaminase family. The protein encoded by this gene is a mitochondrial phosphate-activated glutaminase that catalyzes the hydrolysis of glutamine to stoichiometric amounts of glutamate and ammonia. Originally thought to be liver-specific, this protein has been found in other tissues as well.
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.
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.
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]