InterPro : IPR006096

Name  Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal Short Name  Glu/Leu/Phe/Val_DH_C
Type  Domain Description  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 (, , and ) (GluDH) are enzymes that catalyse the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate [, ]. 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 []- 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 [].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 []. Each subunit of this octameric enzyme from Bacillus sphaericuscontains 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.Phenylalanine dehydrogenase () (PheDH) is na NAD-dependent enzyme that catalyses the reversible deamidation of L-phenylalanine into phenyl-pyruvate [].Valine dehydrogenase () (ValDH) is an NADP-dependent enzyme that catalyses the reversible deamidation of L-valine into 3-methyl-2-oxobutanoate [].This entry represents the C-terminal domain of these proteins.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

4 Found In

Id Name Short Name Type
IPR006095 Glutamate/phenylalanine/leucine/valine dehydrogenase Glu/Leu/Phe/Val_DH Family
IPR016210 NAD-dependent glutamate dehydrogenase, eukaryotes NAD-GDH_euk Family
IPR016211 Glutamate/phenylalanine/leucine/valine dehydrogenase, bacterial/archaeal Glu/Phe/Leu/Val_DH_bac/arc Family
IPR014362 Glutamate dehydrogenase Glu_DH Family

1 Parent Features

Id Name Short Name Type
IPR016040 NAD(P)-binding domain NAD(P)-bd_dom Domain

7 Publications

First Author Title Year Journal Volume Pages
Nagata S Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases. 1988 Biochemistry 27 9056-62
Britton KL Structural relationship between the hexameric and tetrameric family of glutamate dehydrogenases. 1992 Eur J Biochem 209 851-9
Tang L Sequence, transcriptional, and functional analyses of the valine (branched-chain amino acid) dehydrogenase gene of Streptomyces coelicolor. 1993 J Bacteriol 175 4176-85
Takada H Thermostable phenylalanine dehydrogenase of Thermoactinomyces intermedius: cloning, expression, and sequencing of its gene. 1991 J Biochem 109 371-6
Moye WS Nucleotide sequence of yeast GDH1 encoding nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenase. 1985 J Biol Chem 260 8502-8
Benachenhou-Lahfa N Evolution of glutamate dehydrogenase genes: evidence for two paralogous protein families and unusual branching patterns of the archaebacteria in the universal tree of life. 1993 J Mol Evol 36 335-46
Mavrothalassitis G Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family. 1988 Proc Natl Acad Sci U S A 85 3494-8



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)