| Subfamily: | GLUTAMATE DEHYDROGENASE (PTHR11606:SF2) | ||
| Family: | GLUTAMATE DEHYDROGENASE | ||
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| Abstract: |
Glutamate, leucine, phenylalanine and valine dehydrogenases are structurally and functionally related. They contain a Gly-rich region containing a conserved Lys residue, which has been implicated in the catalytic activity, in each case a reversible oxidative deamination reaction. Glutamate dehydrogenases (EC: 1.4.1.2, EC: 1.4.1.3, and EC: 1.4.1.4) (GluDH) are enzymes that catalyze the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate [PMID:1358610, PMID:8315654]. GluDH isozymes are generally involved with either ammonia assimilation or glutamate catabolism. Two separate enzymes are present in yeasts: the NADP-dependent enzyme, which catalyses the amination of alpha-ketoglutarate to L-glutamate; and the NAD-dependent enzyme, which catalyses the reverse reaction [PMID:2989290] - this form links the L-amino acids with the Krebs cycle, which provides a major pathway for metabolic interconversion of alpha-amino acids and alpha- keto acids [PMID:3368458]. Leucine dehydrogenase (EC: 1.4.1.9) (LeuDH) is a NAD-dependent enzyme that catalyzes the reversible deamination of leucine and several other aliphatic amino acids to their keto analogues [PMID:3069133]. Each subunit of this octameric enzyme from Bacillus sphaericus contains 364 amino acids and folds into two domains, separated by a deep cleft. The nicotinamide ring of the NAD+ cofactor binds deep in this cleft, which is thought to close during the hydride transfer step of the catalytic cycle. |
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| InterPro Accession: | IPR006095 | ||
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| Training Sequences: |
55
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| HMM Length | 479 | ||
| Downloads: | HMM (HMMER format) |
| Total | Celera | FlyBase | NCBI | |
| H. sapiens | 7 | 4 | 0 | 3 |
| M. musculus | 6 | 2 | 0 | 4 |
| R. norvegicus | 2 | 1 | 0 | 1 |
| D. melanogaster | 2 | 0 | 2 | 0 |




