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

Hui Yu, Wesley Ryan, Hai Yu, Xi Chen

Research output: Contribution to journalArticle

19 Citations (Scopus)

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 Mg2+ or Mn2+) 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 Mn2+.

Original languageEnglish (US)
Pages (from-to)107-113
Number of pages7
JournalBiotechnology Letters
Volume28
Issue number2
DOIs
StatePublished - Jan 2006

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N-Acylneuraminate Cytidylyltransferase
Cytidine Monophosphate N-Acetylneuraminic Acid
Cytidine
Streptococcus agalactiae
N-Acetylneuraminic Acid
Ligases
Acids
Enzymes
Metals

Keywords

  • Acetylhydrolase
  • Acylesterase
  • CMP-sialic acid synthetase
  • Group B Streptococcus
  • Streptococcus agalactiae

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Microbiology
  • Bioengineering

Cite this

Characterization of a bifunctional cytidine 5′-monophosphate N-acetylneuraminic acid synthetase cloned from Streptococcus agalactiae. / Yu, Hui; Ryan, Wesley; Yu, Hai; Chen, Xi.

In: Biotechnology Letters, Vol. 28, No. 2, 01.2006, p. 107-113.

Research output: Contribution to journalArticle

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