Description

IPR006096 is a Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, C-terminal.

<p>Glutamate, leucine, phenylalanine, valine and tryptophan 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.</p> <p>Glutamate dehydrogenases ([ec:1.4.1.2], [ec:1.4.1.3], and [ec:1.4.1.4]) (GluDH) are enzymes that catalyse the NAD-and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate [[cite:PUB00001430], [cite:PUB00003424]]. 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 [[cite:PUB00002418]] -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 [[cite:PUB00004656]]. In rice, glutamate dehydrogenase 3 is mitochondrial.</p> <p>Leucine dehydrogenase ([ec:1.4.1.9]) (LeuDH) is a NAD-dependent enzyme that catalyses the reversible deamination of leucine and several other aliphatic amino acids to their keto analogues [[cite:PUB00000302]]. 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.</p> <p>Phenylalanine dehydrogenase ([ec:1.4.1.20]) (PheDH) is na NAD-dependent enzyme that catalyses the reversible deamidation of L-phenylalanine into phenyl-pyruvate [[cite:PUB00002347]].</p> <p>Valine dehydrogenase ([ec:1.4.1.8]) (ValDH) is an NADP-dependent enzyme that catalyses the reversible deamidation of L-valine into 3-methyl-2-oxobutanoate [[cite:PUB00002221]].</p> <p>L-tryptophan dehydrogenase catalyses the reversible oxidative deamination of L-tryptophan to indole-3-pyruvate in the presence of NAD+ [[cite:PUB00101896], [cite:PUB00101895]].</p> <p>This entry represents the C-terminal domain of these proteins.</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 28

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: