Structure and characterisation of CMP-Kdn synthetase from the haptophyte microalgae <i>Prymnesium parvum</i>.

ABSTRACT: Sialic acids - 9-carbon ulosonic acids - are implicated in many cell-cell and host-pathogen interactions due to their prevalent location at the non-reducing end of glycoconjugates. Sialic acids have recently been observed in microalgae, including the toxic bloom-forming Prymnesium parvum, which produces the deaminated sialic acid, ketodeoxynonulosonic acid (Kdn), through de novo biosynthesis. Here we report on the key CMP-sialic acid synthetase enzyme (CMAS), PpNeuA, which activates Kdn to its sugar nucleotide congener, CMP-Kdn. In the present study, the X-ray crystal structure of PpNeuA was determined to 1.8 Å resolution and shows that it adopts a similar overall fold to that of other sialic acid synthetase enzymes, with which it shares ca 30% amino acid sequence identity. P

SUBMITTER: Morley C 

PROVIDER: S-EPMC12934254 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature