Glutamate dehydrogenases (EC 126.96.36.199, EC 188.8.131.52, and EC 184.108.40.206) (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 220.127.116.11) (LeuDH) is a NAD-dependent enzyme that
catalyzes the reversible deamination of leucine and several other aliphatic
amino acids to their keto analogues .
Phenylalanine dehydrogenase (EC 18.104.22.168) (PheDH) is a NAD-dependent enzyme
that catalyzes the reversible deamidation of L-phenylalanine into phenyl-
Valine dehydrogenase (EC 22.214.171.124) (ValDH) is a NADP-dependent enzyme that
catalyzes the reversible deamidation of L-valine into 3-methyl-2-
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.
All known sequences from this family have Pro in the last position of
the pattern with the exception of yeast GluDH which as Leu.
November 1997 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
Britton K.L., Baker P.J., Rice D.W., Stillman T.J.
Structural relationship between the hexameric and tetrameric family of glutamate dehydrogenases.
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