Dihydrodipicolinate synthase

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dihydrodipicolinate synthase
Identifiers
EC number 4.3.3.7
CAS number 9055-59-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Dihydrodipicolinate synthetase family
PDB 1xky EBI.jpg
crystal structure of dihydrodipicolinate synthase dapa-2 (ba3935) from bacillus anthracis at 1.94a resolution.
Identifiers
Symbol DHDPS
Pfam PF00701
Pfam clan CL0036
InterPro IPR002220
PROSITE PDOC00569
SCOP 1dhp
SUPERFAMILY 1dhp
CDD cd00950

In enzymology, a dihydrodipicolinate synthase (EC 4.3.3.7) is an enzyme that catalyzes the chemical reaction

L-aspartate 4-semialdehyde + pyruvate \rightleftharpoons (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O

Thus, the two substrates of this enzyme are L-aspartate 4-semialdehyde and pyruvate, whereas its two products are (S)-2,3-dihydropyridine-2,6-dicarboxylate and H2O.

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-aspartate-4-semialdehyde hydro-lyase [adding pyruvate and cyclizing; (S)-2,3-dihydropyridine-2,6-dicarboxylate-forming]. Other names in common use include dihydropicolinate synthetase (DHDPS), dihydrodipicolinic acid synthase, L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and, and cyclizing). This enzyme participates in lysine biosynthesis.

Dihydropicolinate synthase is the key enzyme in lysine biosynthesis via the diaminopimelate pathway of prokaryotes, some phycomycetes, and higher plants. The enzyme catalyses the condensation of L-aspartate-beta-semialdehyde and pyruvate to dihydropicolinic acid via a ping-pong mechanism in which pyruvate binds to the enzyme by forming a Schiff base with a lysine residue.[1] Three other proteins are structurally related to DHDPS and probably also act via a similar catalytic mechanism. These are Escherichia coli N-acetylneuraminate lyase (EC 4.1.3.3) (protein NanA), which catalyses the condensation of N-acetyl-D-mannosamine and pyruvate to form N-acetylneuraminate; Rhizobium meliloti (Sinorhizobium meliloti) protein MosA,[2] which is involved in the biosynthesis of the rhizopine 3-O-methyl-scyllo-inosamine; and E. coli hypothetical protein YjhH. The sequences of DHDPS from different sources are well-conserved. The structure takes the form of a homotetramer, in which 2 monomers are related by an approximate 2-fold symmetry.[1] Each monomer comprises 2 domains: an 8-fold alpha-/beta-barrel, and a C-terminal alpha-helical domain. The fold resembles that of N-acetylneuraminate lyase. The active site lysine is located in the barrel domain, and has access via 2 channels on the C-terminal side of the barrel.

Structural studies[edit]

As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes 1DHP, 1O5K, 1S5T, 1S5V, 1S5W, 1XKY, 1XL9, 1XXX, 1YXC, 1YXD, 2A6L, 2A6N, 2ATS, 2D5K, 2EHH, and 2PCQ.

References[edit]

  1. ^ a b Mirwaldt C, Korndorfer I, Huber R (February 1995). "The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution". J. Mol. Biol. 246 (1): 227–39. doi:10.1006/jmbi.1994.0078. PMID 7853400. 
  2. ^ Murphy PJ, Trenz SP, Grzemski W, De Bruijn FJ, Schell J (August 1993). "The Rhizobium meliloti rhizopine mos locus is a mosaic structure facilitating its symbiotic regulation". J. Bacteriol. 175 (16): 5193–204. PMC 204987. PMID 8349559. 

Further reading[edit]

  • Shedlarski JG, Gilvarg C (1970). "The pyruvate-aspartic semialdehyde condensing enzyme of Escherichia coli". J. Biol. Chem. 245 (6): 1362–73. PMID 4910051. 
  • Yugari Y, Gilvarg C (1965). "The condensation step in diaminopimelate synthesis". J. Biol. Chem. 240 (12): 4710–6. PMID 5321309. 

This article incorporates text from the public domain Pfam and InterPro IPR002220