| Description | Glutamate dehydrogenases ( , , and ) (GluDH) are enzymes that catalyse the NAD- or NADP-dependent reversible deamination of glutamate into alpha-ketoglutarate [ ]. GluDH isozymes are generally involved with either ammonia assimilation or glutamate catabolism.Leucine dehydrogenase ( ) (LeuDH) is a NAD-dependent enzyme that catalyses the reversible deamination of leucine and several other aliphatic amino acids to their keto analogues [ ].Phenylalanine dehydrogenase ( ) (PheDH) is a NAD-dependent enzyme that catalyses the reversible deamidation of L-phenylalanine into phenyl- pyruvate [].Valine dehydrogenase ( ) (ValDH) is a NADP-dependent enzyme that catalyses the reversible deamidation of L-valine into 3-methyl-2-oxobutanoate [ ].These dehydrogenases are structurally and functionally related. A conserved lysine residue located in a glycine-rich region has been implicated in the catalytic mechanism. This entry represents the conserved region around this residue. | Name | Leu/Phe/Val dehydrogenases active site |
| Short Name | Glu/Leu/Phe/Val_DH_AS | Type | Active_site |
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