Document Detail

Cloning, expression, and characterization of sialic acid synthases.
MedLine Citation:
PMID:  16274664     Owner:  NLM     Status:  MEDLINE    
The most commonly occurring sialic acid, N-acetylneuraminic acid, is the repeating unit in polysialic acid chain of human neuronal cell adhesion molecule as well as in capsular polysialic acid of neuroinvasive bacteria, Escherichia coli K1 and Neisseria meningitidis. Sialic acid synthesis and polymerization occur in slightly different pathways in animals and bacteria. N-Acetylneuraminic acid (NeuNAc) is synthesized by the condensation of phosphoenolpyruvate and N-acetylmannosamine by NeuNAc synthase in bacteria. The mammalian homologue N-acetylneuraminic acid-9-phosphate (NeuNAc-9-P) synthase uses N-acetylmannosamine-6-phosphate in the condensation reaction to produce NeuNAc-9-P. Both subfamilies of sialic acid synthases possess N-terminal triosephosphate isomerase barrel domain and C-terminal antifreeze protein domain. We report cloning of the genes, expression, purification, and characterization of human NeuNAc-9-P synthase and N. meningitidis NeuNAc synthase. Stability of the purified enzymes and effects of pH and temperature on their activities were evaluated. Enzyme kinetics and preliminary mutagenesis experiments reveal the importance of C-terminal antifreeze protein domain and a conserved cysteine residue for the enzyme activities.
Jijun Hao; Pichumani Balagurumoorthy; Suryakala Sarilla; Munirathinam Sundaramoorthy
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2005-10-27
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  338     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2005 Dec 
Date Detail:
Created Date:  2005-11-18     Completed Date:  2006-01-06     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1507-14     Citation Subset:  IM    
Division of Nephrology, Department of Medicine, Center for Matrix Biology, Nashville, TN 37232-2372, USA.
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MeSH Terms
Cloning, Molecular
Enzyme Stability
Gene Expression / genetics*
Hydrogen-Ion Concentration
Metals, Heavy / pharmacology
Molecular Weight
Mutagenesis, Site-Directed
Neisseria meningitidis / enzymology,  genetics
Oxo-Acid-Lyases / chemistry,  genetics*,  isolation & purification,  metabolism*
Protein Binding
Grant Support
Reg. No./Substance:
0/Metals, Heavy; EC synthase; EC 4.1.3.-/Oxo-Acid-Lyases

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

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