Conserved Site

Dihydrodipicolinate synthetase, conserved site (IPR020624)

Short name: Dihydrodipicolinate_synth_CS

Description

Dihydrodipicolinate synthase (EC 4.2.1.52) (DHDPS) catalyses, in higher plants, some fungi and bacteria (gene dapA), the first reaction specific to the biosynthesis of lysine and of diaminopimelate [PMID: 22949190]. 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 [PMID: 1463470, PMID: 20025926].

Other proteins are structurally related to DHDPS and probably also act via a similar catalytic mechanism [PMID: 9047371]:

  • Escherichia coli N-acetylneuraminate lyase (EC 4.1.3.3) (gene nanA), which catalyses the condensation of N-acetyl-D-mannosamine and pyruvate to form N-acetylneuraminate.
  • Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase.
  • D-4-deoxy-5-oxoglucarate dehydratase.
  • Rhizobium meliloti protein mosA [PMID: 8349559], which is involved in the biosynthesis of the rhizopine 3-o-methyl-scyllo-inosamine.
  • Thermoproteus tenax 2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase (KdgA) [PMID: 18186475].

This entry represents a highly conserved region in the N-terminal part of these proteins.

GO terms

Biological Process

GO:0008152 metabolic process

Molecular Function

GO:0016829 lyase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns