Characterization of a bifunctional cytidine 5'-monophosphate N-acetylneuraminic acid synthetase cloned from Streptococcus agalactiae

Biotechnol Lett. 2006 Jan;28(2):107-13. doi: 10.1007/s10529-005-4955-z.

Abstract

Recombinant CMP-sialic acid synthetase, cloned from Streptococcus agalactiae serotype V strain 2603 V/R, is bifunctional having both CMP-sialic acid synthetase and acetylhydrolase (acylesterase) activities. The enzyme is active over a wide pH range with an optimal CMP-sialic acid synthetase activity at pH 9.0 and an optimal acetylhydrolase activity at pH 8.0. A metal cofactor (either Mg(2+) or Mn(2+)) is required for the CMP-sialic acid synthetase activity but is not for acetylhydrolase activity. Both catalytic functions, however, are impaired by high concentrations of Mn(2+).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalysis
  • Cloning, Molecular
  • Coenzymes / chemistry
  • Hydrogen-Ion Concentration
  • Magnesium / chemistry
  • Manganese / chemistry
  • N-Acylneuraminate Cytidylyltransferase / chemistry*
  • N-Acylneuraminate Cytidylyltransferase / genetics
  • Streptococcus agalactiae / enzymology*
  • Streptococcus agalactiae / genetics

Substances

  • Coenzymes
  • Manganese
  • N-Acylneuraminate Cytidylyltransferase
  • Magnesium