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PROSITE documentation PDOC00071

Glu / Leu / Phe / Val dehydrogenases active site

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 α-ketoglutarate [1,2]. 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 [3].
  • Phenylalanine dehydrogenase (EC 1.4.1.20) (PheDH) is a NAD-dependent enzyme that catalyzes the reversible deamidation of L-phenylalanine into phenyl- pyruvate [4].
  • 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 [5].

These dehydrogenases are structurally and functionally related. A conserved lysine residue located in a glycine-rich region has been implicated in the catalytic mechanism. The conservation of the region around this residue allows the derivation of a signature pattern for such type of enzymes.

Note:

All known sequences from this family have Pro in the last position of the pattern with the exception of yeast GluDH which as Leu.

Last update:

November 1997 / Pattern and text revised.

Technical section:

PROSITE method (with tools and information) covered by this documentation:

GLFV_DEHYDROGENASE, PS00074; Glu / Leu / Phe / Val dehydrogenases active site  (PATTERN)
Consensus pattern: [LIV]-x(2)-G-G-[SAG]-K-x-[GV]-x(3)-[DNST]-[PL]
K is the active site residue
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
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Matching PDB structures: 1AUP 1B26 1B3B 1BGV ... [ALL]

References:

1 AuthorsBritton K.L., Baker P.J., Rice D.W., Stillman T.J.
TitleStructural relationship between the hexameric and tetrameric family of glutamate dehydrogenases.
SourceEur. J. Biochem. 209:851-859(1992).
PubMed ID1358610
2 AuthorsBenachenhou-Lahfa N., Forterre P., Labedan B.
SourceJ. Mol. Evol. 36:335-346(1993).
3 AuthorsNagata S., Tanizawa K., Esaki N., Sakamoto Y., Ohshima T., Tanaka H., Soda K.
TitleGene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases.
SourceBiochemistry 27:9056-9062(1988).
PubMed ID3069133
4 AuthorsTakada H., Yoshimura T., Ohshima T., Esaki N., Soda K.
TitleThermostable phenylalanine dehydrogenase of Thermoactinomyces intermedius: cloning, expression, and sequencing of its gene.
SourceJ. Biochem. 109:371-376(1991).
PubMed ID1880121
5 AuthorsTang L., Hutchinson C.R.
TitleSequence, transcriptional, and functional analyses of the valine (branched-chain amino acid) dehydrogenase gene of Streptomyces coelicolor.
SourceJ. Bacteriol. 175:4176-4185(1993).
PubMed ID8320231

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