Document Detail


Characterization of a bifunctional cytidine 5'-monophosphate N-acetylneuraminic acid synthetase cloned from Streptococcus agalactiae.
MedLine Citation:
PMID:  16369694     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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+).
Authors:
Hui Yu; Wesley Ryan; Hai Yu; Xi Chen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biotechnology letters     Volume:  28     ISSN:  0141-5492     ISO Abbreviation:  Biotechnol. Lett.     Publication Date:  2006 Jan 
Date Detail:
Created Date:  2005-12-21     Completed Date:  2006-06-22     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8008051     Medline TA:  Biotechnol Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  107-13     Citation Subset:  IM    
Affiliation:
Department of Chemistry, University of California, Davis, 95616, USA.
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MeSH Terms
Descriptor/Qualifier:
Catalysis
Cloning, Molecular
Coenzymes / chemistry
Hydrogen-Ion Concentration
Magnesium / chemistry
Manganese / chemistry
N-Acylneuraminate Cytidylyltransferase / chemistry*,  genetics
Streptococcus agalactiae / enzymology*,  genetics
Chemical
Reg. No./Substance:
0/Coenzymes; 7439-95-4/Magnesium; 7439-96-5/Manganese; EC 2.7.7.43/N-Acylneuraminate Cytidylyltransferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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