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Characterization of a Bifunctional Cytidine 5′-Monophosphate N-acetylneuraminic acid Synthetase Cloned from Streptococcus Agalactiae

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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+.

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References

  • CC Akoh GC Lee YC Liaw TH Huang JF Shaw (2004) ArticleTitleGDSL family of serine esterases/lipases Prog. Lipid Res. 43 534–552 Occurrence Handle15522763 Occurrence Handle1:CAS:528:DC%2BD2cXptFKqs7k%3D Occurrence Handle10.1016/j.plipres.2004.09.002

    Article  PubMed  CAS  Google Scholar 

  • H Cho JE Cronan SuffixJr (1993) ArticleTitle Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme J. Biol. Chem. 268 9238–9245 Occurrence Handle8098033 Occurrence Handle1:CAS:528:DyaK3sXkvFSjsr0%3D

    PubMed  CAS  Google Scholar 

  • RF Haft MR Wessels (1994) ArticleTitleCharacterization of CMP-N-acetylneuraminic acid synthetase of group B streptococci J. Bacteriol. 176 7372–7374 Occurrence Handle7961510 Occurrence Handle1:STN:280:DyaK2M%2FltVehsA%3D%3D

    PubMed  CAS  Google Scholar 

  • RF Haft MR Wessels MF Mebane N Conaty CE Rubens (1996) ArticleTitleCharacterization of cpsF and its product CMP-N-acetylneuraminic acid synthetase, a group B streptococcal enzyme that can function in K1 capsular polysaccharide biosynthesis in Escherichia coli Mol. Microbiol. 19 555–563 Occurrence Handle8830246 Occurrence Handle10.1046/j.1365-2958.1996.395931.x Occurrence Handle1:CAS:528:DyaK28Xht1Shtbg%3D

    Article  PubMed  CAS  Google Scholar 

  • EL Kean (1991) ArticleTitleSialic acid activation Glycobiology 1 441–447 Occurrence Handle1668304 Occurrence Handle1:CAS:528:DyaK38XnvV2nsw%3D%3D

    PubMed  CAS  Google Scholar 

  • YL Lee JC Chen JF Shaw (1997) ArticleTitleThe thioesterase I of Escherichia coli has arylesterase activity and shows stereospecificity for protease substrates Biochem. Biophys. Res. Commun. 231 452–456 Occurrence Handle9070299 Occurrence Handle1:CAS:528:DyaK2sXhsVegtbw%3D

    PubMed  CAS  Google Scholar 

  • AL Lewis V Nizet A Varki (2004) ArticleTitleDiscovery and characterization of sialic acid O-acetylation in group B Streptococcus Proc. Natl. Acad. Sci. USA 101 11123–11128 Occurrence Handle15263085 Occurrence Handle1:CAS:528:DC%2BD2cXmsVCmtb8%3D

    PubMed  CAS  Google Scholar 

  • G Liu C Jin C Jin (2004) ArticleTitleCMP-N-acetylneuraminic acid synthetase from Escherichia coli K1 is a bifunctional enzyme: identification of minimal catalytic domain for synthetase activity and novel functional domain for platelet-activating factor acetylhydrolase activity J. Biol. Chem. 279 17738–17749 Occurrence Handle14960566 Occurrence Handle1:CAS:528:DC%2BD2cXjt1Gnuro%3D

    PubMed  CAS  Google Scholar 

  • A Molgaard S Kauppinen S Larsen (2000) ArticleTitleRhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases Structure Fold. Des. 8 373–383 Occurrence Handle10801485 Occurrence Handle1:CAS:528:DC%2BD3cXivFSisrY%3D

    PubMed  CAS  Google Scholar 

  • H Yu H Yu R Karpel X Chen (2004) ArticleTitleChemoenzymatic synthesis of CMP-sialic acid derivatives by a one-pot two-enzyme system: comparison of substrate flexibility of three microbial CMP-sialic acid synthetases Bioorg. Med. Chem. 12 6427–6435 Occurrence Handle15556760 Occurrence Handle1:CAS:528:DC%2BD2cXhtVSnsrrK

    PubMed  CAS  Google Scholar 

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Authors and Affiliations

  1. Department of Chemistry, University of California, Davis, CA, 95616, USA

    Hui Yu, Wesley Ryan, Hai Yu & Xi Chen

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  1. Hui Yu
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  2. Wesley Ryan
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  3. Hai Yu
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  4. Xi Chen
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Correspondence to Xi Chen.

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Received 10 August 2005; Revisions requested 30 August 2005; Revisions received 1 November 2005; Accepted 2 November 2005

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Yu, H., Ryan, W., Yu, H. et al. Characterization of a Bifunctional Cytidine 5′-Monophosphate N-acetylneuraminic acid Synthetase Cloned from Streptococcus Agalactiae . Biotechnol Lett 28, 107–113 (2006). https://doi.org/10.1007/s10529-005-4955-z

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  • DOI: https://doi.org/10.1007/s10529-005-4955-z

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