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Glutaric acidemia type 1 (GA1) is an inherited disorder in which the body is unable to completely break down the amino acids lysine, hydroxylysine and tryptophan.Excessive levels of their intermediate breakdown products (glutaric acid, glutaryl-CoA, 3-hydroxyglutaric acid, glutaconic acid) can accumulate and cause damage to the brain (and also other organs [1]), but particularly the basal ...
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.
Glutamic acid ball and stick model spinning. Glutamic acid (symbol Glu or E; [4] known as glutamate in its anionic form) is an α-amino acid that is used by almost all living beings in the biosynthesis of proteins. It is a non-essential nutrient for humans, meaning that the human body can synthesize enough for its use.
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. The reaction proceeds as follows: HOOC−CH 2 −CH 2 −CH(NH 2)−COOH → CO 2 + HOOC−CH 2 −CH 2 −CH 2 NH 2
Formiminoglutamic acid (FIGLU; conjugate base, formiminoglutamate) is an intermediate in the catabolism of L-histidine to L-glutamic acid. It thus is also a biomarker for intracellular levels of folate. The FIGLU test is used to identify vitamin B₁₂ deficiency, folate deficiency, and liver failure or liver disease.
Carbamoyl phosphate synthase 1, abbreviated as CPS1, is activated by its natural activator N-acetyl glutamate, which in turn is synthesized from acetyl-CoA and glutamic acid in the reaction catalyzed by N-acetyl glutamate synthase, commonly called NAGS. N-acetyl glutamate is required for the urea cycle to take place.
Triose phosphate isomerase deficiency is characterized by chronic hemolytic anemia. While there are various mutations that cause this disease, most include the replacement of glutamic acid at position 104 with an aspartic acid. [1]
2677 56316 Ensembl ENSG00000115486 ENSMUSG00000053460 UniProt P38435 Q9QYC7 RefSeq (mRNA) NM_000821 NM_001142269 NM_001311312 NM_019802 RefSeq (protein) NP_000812 NP_001135741 NP_001298241 NP_062776 Location (UCSC) Chr 2: 85.54 – 85.56 Mb n/a PubMed search Wikidata View/Edit Human View/Edit Mouse Gamma-glutamyl carboxylase is an enzyme that in humans is encoded by the GGCX gene, located on ...