PROSITE documentation PDOC00569
Dihydrodipicolinate synthase signatures


Dihydrodipicolinate synthase (EC (DHDPS) [1] catalyzes, in higher plants chloroplast and in many bacteria (gene dapA), the first reaction specific to the biosynthesis of lysine and of diaminopimelate. DHDPS is responsible for the condensation of aspartate semialdehyde and pyruvate by a ping-pong mechanism in which pyruvate first binds to the enzyme by forming a Schiff-base with a lysine residue.

Three other proteins are structurally related to DHDPS and probably also act via a similar catalytic mechanism:

  • Escherichia coli N-acetylneuraminate lyase (EC (gene nanA), which catalyzes the condensation of N-acetyl-D-mannosamine and pyruvate to form N-acetylneuraminate.
  • Rhizobium meliloti protein mosA [3], which is involved in the biosynthesis of the rhizopine 3-o-methyl-scyllo-inosamine.
  • Escherichia coli hypothetical protein yjhH.

We have developed two signature patterns for these enzymes. The first one is centered on highly conserved region in the N-terminal part of these proteins. The second signature contains a lysine residue which has been shown, in Escherichia coli dapA [2], to be the one that forms a Schiff-base with the substrate.

Last update:

December 2004 / Pattern and text revised.


Technical section

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

DHDPS_1, PS00665; Dihydrodipicolinate synthase signature 1  (PATTERN)

DHDPS_2, PS00666; Dihydrodipicolinate synthase signature 2  (PATTERN)


1AuthorsKaneko T. Hashimoto T. Kumpaisal R. Yamada Y.
TitleMolecular cloning of wheat dihydrodipicolinate synthase.
SourceJ. Biol. Chem. 265:17451-17455(1990).
PubMed ID2211639

2AuthorsLaber B. Gomis-Ruth F.-X. Romao M.J. Huber R.
TitleEscherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization.
SourceBiochem. J. 288:691-695(1992).
PubMed ID1463470

3AuthorsMurphy P.J. Trenz S.P. Grzemski W. De Bruijn F.J. Schell J.
TitleThe Rhizobium meliloti rhizopine mos locus is a mosaic structure facilitating its symbiotic regulation.
SourceJ. Bacteriol. 175:5193-5204(1993).
PubMed ID8349559

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