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In enzymology, a L-glutamate oxidase (EC 1.4.3.11) is an enzyme that catalyzes the chemical reaction L-glutamate + O 2 + H 2 O ⇌ {\displaystyle \rightleftharpoons } 2-oxoglutarate + NH 3 + H 2 O 2 The 3 substrates of this enzyme are L-glutamate , O 2 , and H 2 O , whereas its 3 products are 2-oxoglutarate , NH 3 , and H 2 O 2 .
Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the GSR gene.Glutathione reductase (EC 1.8.1.7) catalyzes the reduction of glutathione disulfide to the sulfhydryl form glutathione (), which is a critical molecule in resisting oxidative stress and maintaining the reducing environment of the cell.
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
Glutaric acidemia type 2 has an autosomal recessive pattern of inheritance. Mutations in the ETFA, ETFB, and ETFDH genes cause glutaric acidemia type II. Mutations in these genes result in a deficiency in one of two enzymes that normally work together in the mitochondria, which are the energy-producing centers of cells.
Several isozymes are encoded by different genes, which vary in cellular location and substrate specificity. Glutathione peroxidase 1 (GPx1) is the most abundant version, found in the cytoplasm of nearly all mammalian tissues, whose preferred substrate is hydrogen peroxide.
The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteine:glycine ligase (ADP-forming). Other names in common use include glutathione synthetase, and GSH synthetase. This enzyme participates in glutamate metabolism and glutathione metabolism. At least one compound, Phosphinate is known to inhibit this enzyme. [citation needed]
The first committed step is the reaction of PRPP, glutamine and water to 5'-phosphoribosylamine (PRA), glutamate, and pyrophosphate - catalyzed by amidophosphoribosyltransferase, which is activated by PRPP and inhibited by AMP, GMP and IMP. PRPP + L-Glutamine + H 2 O → PRA + L-Glutamate + PPi
Glutamine (symbol Gln or Q) [3] is an α-amino acid that is used in the biosynthesis of proteins.Its side chain is similar to that of glutamic acid, except the carboxylic acid group is replaced by an amide.