1 Child Features
| DB identifier | Type | Name |
|---|---|---|
| IPR012691 | Family | 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase variant |
| Type: | Family | Name: | 4-hydroxy-tetrahydrodipicolinate synthase, DapA |
| Description: | 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) []. 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 arerelated by an approximate 2-fold symmetry []. 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 []. | Short Name: | DapA |
| DB identifier | Type | Name |
|---|---|---|
| IPR012691 | Family | 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase variant |
