Abstract
An N-terminal and C-terminal truncated recombinant α2-6-sialyltransferase cloned from Photobacterium sp. JH-ISH-224, Psp2,6ST(15-501)-His(6), was shown to be an efficient catalyst for one-pot three-enzyme synthesis of sialyl Tn (STn) antigens and derivatives containing natural and non-natural sialic acid forms.
This journal is © The Royal Society of Chemistry 2011
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Antigens, Tumor-Associated, Carbohydrate / biosynthesis*
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Antigens, Tumor-Associated, Carbohydrate / chemistry
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Antigens, Tumor-Associated, Carbohydrate / immunology
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Biocatalysis
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Histidine / genetics
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Histidine / metabolism
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Kinetics
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N-Acylneuraminate Cytidylyltransferase / metabolism
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Oligopeptides / genetics
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Oligopeptides / metabolism
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Oxo-Acid-Lyases / metabolism
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Photobacterium / enzymology
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sialyltransferases / genetics
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Sialyltransferases / metabolism
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beta-D-Galactoside alpha 2-6-Sialyltransferase
Substances
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Antigens, Tumor-Associated, Carbohydrate
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His-His-His-His-His-His
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Oligopeptides
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Recombinant Proteins
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sialosyl-Tn antigen
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Histidine
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Sialyltransferases
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N-Acylneuraminate Cytidylyltransferase
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Oxo-Acid-Lyases
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N-acetylneuraminate lyase
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beta-D-Galactoside alpha 2-6-Sialyltransferase