| Primary Identifier | IPR020625 | Type | Active_site |
| Short Name | Schiff_base-form_aldolases_AS |
| description | This entry represents an active site found in members of a structural superfamily of Schiff base-forming aldolases that catalyse reactions indifferent biological pathways. This superfamily includes members such as dihydrodipicolinate synthase (DHDPS), N-acetylneuraminate lyase (NAL) and 2-keto-3-deoxygluconate aldolase (KDG aldolase) []. One of the Escherichia coli proteins containing this site, dapA (), was first identified as dihydrodipicolinate synthase (DHDPS) []. Later, it has been identified as 4-hydroxy-tetrahydrodipicolinate synthases () []. Among the putative DHDPS genes annotated in the A. tumefaciens genome, dapA7 gene product has been shown to possess DHDPS enzyme activity and is allosterically inhibited by lysine []. |
