Literature summary for 3.2.1.18 extracted from

Connaris, H.; Crocker, P.R.; Taylor, G.L.
Enhancing the receptor affinity of the sialic acid-binding domain of Vibrio cholerae sialidase through multivalency (2009), J. Biol. Chem., 284, 7339-7351.

Search for more literature for 3.2.1.18

Application

Application	Comment	Organism
analysis	subcloning of carbohydrate-binding module CBM40 of sialidase, showing high affinity for sialic acid and specificity to alpha(2,3), alpha(2,6), and alpha(2,8)-linked sialosides. Creation of polypeptides containing up to four CBM40 modules in tandem show increased affinities compared with the single module molecule. Variation in linker length has little effect on affinity	Vibrio cholerae serotype O1

Cloned(Commentary)

Cloned (Comment)	Organism
subcloning of the carbohydrate-binding module CBM40	Vibrio cholerae serotype O1

Crystallization (Commentary)

Crystallization (Comment)	Organism
carbohydrate-binding module CBM40 of sialidase, showing high affinity for sialic acid and specificity to alpha(2,3), alpha(2,6), and alpha(2,8)-linked sialosides	Vibrio cholerae serotype O1

Protein Variants

Protein Variants	Comment	Organism
additional information	subcloning of carbohydrate-binding module CBM40 of sialidase, showing high affinity for sialic acid and specificity to alpha(2,3), alpha(2,6), and alpha(2,8)-linked sialosides. Creation of polypeptides containing up to four CBM40 modules in tandem show increased affinities compared with the single module molecule. Variation in linker length has little effect on affinity	Vibrio cholerae serotype O1

Organism

Organism	UniProt	Comment	Textmining
Vibrio cholerae	P0C6E9	-	-

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Release 2023.1 (January 2023)