4-hydroxy-tetrahydrodipicolinate synthase, DapA (IPR005263)

Short name: DapA

Overlapping homologous superfamilies

Family relationships


4-hydroxy-tetrahydrodipicolinate synthase dapA is a homotetrameric enzyme of lysine biosynthesis. It catalyses the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) [PMID: 9559056]. E. coli has several paralogs closely related to dihydrodipicoline synthase, as well as the more distant N-acetylneuraminate lyase.

It is worth noting that despite the real product of this enzyme being 4-hydroxy-2,3,4,5-tetrahydro-L,L-dipicolinic acid, it is still known in most publications as dihydropicolinate synthase (DHDPS).

The sequences of dapA 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 [PMID: 7853400]. 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 [PMID: 15066435].

GO terms

Biological Process

GO:0009089 lysine biosynthetic process via diaminopimelate

Molecular Function

GO:0008840 4-hydroxy-tetrahydrodipicolinate synthase

Cellular Component

No terms assigned in this category.

Contributing signatures

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