|PROSITE documentation PDOC00569 [for PROSITE entry PS00666]|
Dihydrodipicolinate synthase (EC 220.127.116.11) (DHDPS)  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:
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 , to be the one that forms a Schiff-base with the substrate.Last update:
December 2004 / Pattern and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Kaneko T. Hashimoto T. Kumpaisal R. Yamada Y.|
|Title||Molecular cloning of wheat dihydrodipicolinate synthase.|
|Source||J. Biol. Chem. 265:17451-17455(1990).|
|2||Authors||Laber B. Gomis-Ruth F.-X. Romao M.J. Huber R.|
|Title||Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization.|
|Source||Biochem. J. 288:691-695(1992).|
|3||Authors||Murphy P.J. Trenz S.P. Grzemski W. De Bruijn F.J. Schell J.|
|Title||The Rhizobium meliloti rhizopine mos locus is a mosaic structure facilitating its symbiotic regulation.|
|Source||J. Bacteriol. 175:5193-5204(1993).|