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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 .
The molecular and clinical spectrum of AAAC deficiency is heterogeneous. The first case of AADC deficiency was described in twin brothers 1990. Patients can be treated with dopamine agonists, MAO inhibitors, and pyridoxine (vitamin B 6). [15] Clinical phenotype and response to treatment is variable and the long-term and functional outcome is ...
The manifestations of histamine intolerance are usually systemic, affecting the entire body; still, these symptoms are often sporadic and non-specific. [5] [6] [7] The onset of symptoms is usually shortly (within a few hours) after specific food or drink consumption, and subsequent remission usually happens in 4-8 weeks of dieting, [8] that is excluding food that causes the onset of symptoms.
Glutamate decarboxylase or glutamic acid decarboxylase (GAD) is an enzyme that catalyzes the decarboxylation of glutamate to gamma-aminobutyric acid (GABA) and carbon dioxide (CO 2). GAD uses pyridoxal-phosphate (PLP) as a cofactor .
L-Gulonolactone oxidase (EC 1.1.3.8) is an enzyme that produces vitamin C. It is expressed in most mammals, but is non-functional in Haplorrhini (a suborder of primates, including humans), in some bats , and in guinea pigs .
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.
Chronic granulomatous disease (CGD), also known as Bridges–Good syndrome, chronic granulomatous disorder, and Quie syndrome, [1] is a diverse group of hereditary diseases in which certain cells of the immune system have difficulty forming the reactive oxygen compounds (most importantly the superoxide radical due to defective phagocyte NADPH oxidase) used to kill certain ingested pathogens. [2]
Tyrosine hydroxylase or tyrosine 3-monooxygenase is the enzyme responsible for catalyzing the conversion of the amino acid L-tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA). [ 5 ] [ 6 ] It does so using molecular oxygen (O 2 ), as well as iron (Fe 2+ ) and tetrahydrobiopterin as cofactors .