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GLUD1
May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate. Homohexamer. Subject to allosteric regulation. Activated by ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding site and activate the enzyme. Belongs to the Glu/Leu/Phe/Val dehydrogenases family. Note: This description may include information from UniProtKB.
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| Protein type: Amino Acid Metabolism - alanine, aspartate and glutamate; Amino Acid Metabolism - arginine and proline; EC 1.4.1.3; Energy Metabolism - nitrogen; Mitochondrial; Other Amino Acids Metabolism - D-Glutamine and D-glutamate; Oxidoreductase |
| Chromosomal Location of Human Ortholog: 10q23.2 |
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Cellular Component:
cytoplasm; mitochondrial matrix; mitochondrion
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Molecular Function:
ADP binding; ATP binding; glutamate dehydrogenase (NAD+) activity; glutamate dehydrogenase [NAD(P)+] activity; GTP binding; identical protein binding; leucine binding; NAD+ binding; protein binding
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Biological Process:
cellular amino acid biosynthetic process; glutamate biosynthetic process; glutamate catabolic process; glutamine metabolic process; oxidation-reduction process; positive regulation of insulin secretion; tricarboxylic acid metabolic process
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Disease: Hyperinsulinemic Hypoglycemia, Familial, 6
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Reference #:
P00367
(UniProtKB)
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Alt. Names/Synonyms: DHE3; GDH; GDH 1; GDH1; GLUD; GLUD1; glutamate dehydrogenase (NAD(P)+); glutamate dehydrogenase 1; Glutamate dehydrogenase 1, mitochondrial; MGC132003
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Gene Symbols: GLUD1
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Molecular weight:
61,398 Da
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Basal Isoelectric point:
7.66
Predict pI for various phosphorylation states
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Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®
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