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UniProt functional annotation for P00366 | ||
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| UniProt code: P00366. |
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| Organism: | |
Bos taurus (Bovine). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos. |
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| Function: | |
Mitochondrial glutamate dehydrogenase that converts L- glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle (PubMed:4365183, PubMed:14659072). Plays a role in insulin homeostasis (By similarity). May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity). {ECO:0000250|UniProtKB:P00367, ECO:0000250|UniProtKB:P10860, ECO:0000269|PubMed:14659072, ECO:0000269|PubMed:4365183}. |
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| Catalytic activity: | |
Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.3; Evidence={ECO:0000269|PubMed:14659072, ECO:0000269|PubMed:4365183}; |
| Catalytic activity: | |
Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.3; Evidence={ECO:0000250|UniProtKB:P00367}; |
| Activity regulation: | |
Subject to allosteric regulation. Activated by ADP (PubMed:14659072). Inhibited by GTP and ATP (PubMed:14659072). ADP can occupy the NADH binding site and activate the enzyme. Inhibited by SIRT4 (By similarity). Inhibited by HADH (By similarity). {ECO:0000250|UniProtKB:P00367, ECO:0000250|UniProtKB:P26443, ECO:0000269|PubMed:14659072}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.1 mM for NAD(+) {ECO:0000269|PubMed:14659072}; Vmax=100 umol/min/mg enzyme with NAD(+)as substrate {ECO:0000269|PubMed:14659072}; |
| Subunit: | |
Homohexamer (PubMed:11254391, PubMed:12653548). Interacts with HADH; this interaction inhibits the activation of GLUD1 (By similarity). {ECO:0000250|UniProtKB:P26443, ECO:0000269|PubMed:11254391, ECO:0000269|PubMed:12653548}. |
| Subcellular location: | |
Mitochondrion {ECO:0000250|UniProtKB:P00367}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P00367}. Note=Mostly translocates into the mitochondria, only a small amount of the protein localizes to the endoplasmic reticulum. {ECO:0000250|UniProtKB:P00367}. |
| Ptm: | |
ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity. Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer. {ECO:0000250|UniProtKB:P00367}. |
| Similarity: | |
Belongs to the Glu/Leu/Phe/Val dehydrogenases family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.