{PDOC00569}
{PS00665; DHDPS_1}
{PS00666; DHDPS_2}
{BEGIN}
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* Dihydrodipicolinate synthase signatures *
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Dihydrodipicolinate synthase  (EC  4.2.1.52)  (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 4.1.3.3) (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.

-Consensus pattern: [GSA]-[LIVM]-[LIVMFY]-x(2)-G-[ST]-[TG]-G-E-[GASNF]-x(6)-
                    [EQ]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: Y-[DNSAH]-[LIVMFAN]-P-x(2)-[STAV]-x(2,3)-[LIVMFT]-
                    x(13,14)-[LIVMCF]-x-[SGA]-[LIVMFNS]-K-[DEQAFYH]-[STACI]
                    [K is involved in Schiff-base formation]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: December 2004 / Pattern and text revised.

[ 1] Kaneko T., Hashimoto T., Kumpaisal R., Yamada Y.
     "Molecular cloning of wheat dihydrodipicolinate synthase."
     J. Biol. Chem. 265:17451-17455(1990).
     PubMed=2211639
[ 2] Laber B., Gomis-Ruth F.-X., Romao M.J., Huber R.
     "Escherichia coli dihydrodipicolinate synthase. Identification of the
     active site and crystallization."
     Biochem. J. 288:691-695(1992).
     PubMed=1463470
[ 3] Murphy P.J., Trenz S.P., Grzemski W., De Bruijn F.J., Schell J.
     "The Rhizobium meliloti rhizopine mos locus is a mosaic structure
     facilitating its symbiotic regulation."
     J. Bacteriol. 175:5193-5204(1993).
     PubMed=8349559

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{END}