{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Morley C"],"pubmed_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 <i>Prymnesium parvum</i>, which produces the deaminated sialic acid, ketodeoxynonulosonic acid (Kdn), through <i>de novo</i> 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"],"journal":["RSC chemical biology"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12934254"],"repository":["biostudies-literature"],"pubmed_title":["Structure and characterisation of CMP-Kdn synthetase from the haptophyte microalgae &lt;i&gt;Prymnesium parvum&lt;/i&gt;."],"pmcid":["PMC12934254"],"pubmed_authors":["Levy CW","Munro-Clark AJ","Dubinskaya E","Ivanova I","Morley C","Field RA","Wagstaff BA","Rostock A","Ortmayer M"],"additional_accession":[]},"is_claimable":false,"name":"Structure and characterisation of CMP-Kdn synthetase from the haptophyte microalgae &lt;i&gt;Prymnesium parvum&lt;/i&gt;.","description":"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 <i>Prymnesium parvum</i>, which produces the deaminated sialic acid, ketodeoxynonulosonic acid (Kdn), through <i>de novo</i> 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","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Feb","modification":"2026-07-16T22:11:37.599Z","creation":"2026-07-14T03:03:53.703Z"},"accession":"S-EPMC12934254","cross_references":{"pubmed":["41756713"],"doi":["10.1039/d5cb00285k"]}}