Structural and functional evidence for two separate oligosaccharide binding sites of Pasteurella multocida hyaluronan synthase
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چکیده
منابع مشابه
Structural and functional evidence for two separate oligosaccharide binding sites of Pasteurella multocida hyaluronan synthase
Pasteurella multocida hyaluronan synthase (PmHAS) is a bi-functional glycosyltransferase, containing a β1,3-glucuronyltransferase and β1,4-N-acetylglucosaminetransferase domain. PmHAS catalyzes the elongation of hyaluronan (HA) through the sequential addition of single monosaccharides to the non-reducing end of the hyaluronan chain. Research is focused on the relation between the length of the ...
متن کاملCritical elements of oligosaccharide acceptor substrates for the Pasteurella multocida hyaluronan synthase.
Three-dimensional structures are not available for polysaccharide synthases and only minimal information on the molecular basis for catalysis is known. The Pasteurella multocida hyaluronan synthase (PmHAS) catalyzes the polymerization of the alternating beta1,3-N-acetylglucosamine-beta1,4-glucuronic acid sugar chain by the sequential addition of single monosaccharides to the non-reducing termin...
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The first complete genome sequence of the P. multocida avian isolate Pm70 was reported in 2001. Analysis of the genome identified many predicted virulence genes, including two encoding homologues of the Bordetella pertussis filamentous haemagluttinins, and genes involved in iron transport and metabolism. Availability of the genome sequence allowed for a range of whole-genome trans...
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The Pasteurella multocida adenylate cyclase gene has been cloned and expressed in Escherichia coli. The primary structure of the protein (838 amino acids) deduced from the corresponding nucleotide sequence was compared with that of E. coli. The two enzymes have similar molecular sizes and, based on sequence conservation at the protein level, are likely to be organized in two functional domains:...
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ژورنال
عنوان ژورنال: Advances in Enzyme Research
سال: 2013
ISSN: 2328-4846,2328-4854
DOI: 10.4236/aer.2013.14011