Abstract：
:The glucose 1-phosphate uridylyltransferase (GalU) is absolutely required for the biosynthesis of capsular polysaccharide, the sine qua non virulence factor of Streptococcus pneumoniae. The pneumococcal GalU protein was overexpressed in Escherichia coli, and purified. GalU showed a pI of 4.23, and catalyzed the reversible formation of UDP-glucose and pyrophosphate from UTP and glucose 1-phosphate with K(m) values of 0.4 mM: for UDP-glucose, 0.26 mM: for pyrophosphate, 0.19 mM: for glucose 1-phosphate, and 0.24 mM: for UTP. GalU has an optimum pH of 8-8.5, and requires Mg(2+) for activity. Neither ADP-glucose nor TDP-glucose is utilized as substrates in vitro. The purification of GalU represents a fundamental step to provide insights on drug design to control the biosynthesis of the main pneumococcal virulence factor.
journal_name
Curr Microbioljournal_title
Current microbiologyauthors
Bonofiglio L,García E,Mollerach Mdoi
10.1007/s00284-005-4466-0keywords:
subject
Has Abstractpub_date
2005-10-01 00:00:00pages
217-21issue
4eissn
0343-8651issn
1432-0991journal_volume
51pub_type
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