Active Site

Leu/Phe/Val dehydrogenases active site (IPR033524)

Short name: Glu/Leu/Phe/Val_DH_AS

Description

  • 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- or NADP-dependent reversible deamination of glutamate into alpha-ketoglutarate [PMID: 1358610]. GluDH isozymes are generally involved with either ammonia assimilation or glutamate catabolism.
  • 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].
  • Phenylalanine dehydrogenase (EC:1.4.1.20) (PheDH) is a NAD-dependent enzyme that catalyzes the reversible deamidation of L-phenylalanine into phenyl- pyruvate [PMID: 1880121].
  • Valine dehydrogenase (EC:1.4.1.8) (ValDH) is a NADP-dependent enzyme that catalyzes the reversible deamidation of L-valine into 3-methyl-2-oxobutanoate [PMID: 8320231].

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.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns