N-acylneuraminate cytidylyltransferase

In enzymology, a N-acylneuraminate cytidylyltransferase (EC 2.7.7.43) is an enzyme that catalyzes the chemical reaction

N-acylneuraminate cytidylyltransferase
N-acylneuraminate cytidylyltransferase dimer, Neisseria meningitidis
Identifiers
EC no.2.7.7.43
CAS no.9067-82-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
CTP + N-acylneuraminate diphosphate + CMP-N-acylneuraminate

Thus, the two substrates of this enzyme are CTP and N-acylneuraminate, whereas its two products are diphosphate and CMP-N-acylneuraminate.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:N-acylneuraminate cytidylyltransferase. Other names in common use include CMP-sialate pyrophosphorylase, CMP-sialate synthase, cytidine 5'-monophosphosialic acid synthetase, CMP-Neu5Ac synthetase, CMP-NeuAc synthetase, acylneuraminate cytidyltransferase, CMP-N-acetylneuraminate synthetase, CMP-N-acetylneuraminate synthase, CMP-N-acetylneuraminic acid synthase, CMP-NANA synthetase, CMP-sialate synthetase, CMP-sialic synthetase, cytidine 5'-monophospho-N-acetylneuraminic acid synthetase, cytidine 5-monophosphate N-acetylneuraminic acid synthetase, cytidine monophosphosialic acid synthetase, cytidine monophosphoacetylneuraminic synthetase, cytidine monophosphosialate pyrophosphorylase, cytidine monophosphosialate synthetase, and acetylneuraminate cytidylyltransferase. This enzyme participates in aminosugars metabolism.

Structural studies

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As of late 2007, three structures have been solved for this class of enzymes, with PDB accession codes 1EYR, 1EZI, and 1QWJ.

References

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  • Kean EL, Roseman S (1966). "The sialic acids. X. Purification and properties of cytidine 5'-monophosphosialic acid synthetase". J. Biol. Chem. 241 (23): 5643–50. doi:10.1016/S0021-9258(18)96393-3. PMID 4288894.