Literature summary for 2.4.3.1 extracted from

Kakuta, Y.; Okino, N.; Kajiwara, H.; Ichikawa, M.; Takakura, Y.; Ito, M.; Yamamoto, T.
Crystal structure of Vibrionaceae Photobacterium sp. JT-ISH-224 alpha2,6-sialyltransferase in a ternary complex with donor product CMP and acceptor substrate lactose: catalytic mechanism and substrate recognition (2008), Glycobiology, 18, 66-73.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
single crystals are grown by the hanging-drop vapor diffusion method at 20°C. Crystal structure of DELTA16psp26ST, the N-terminal truncated form of alpha2,6-sialyltransferase from Photobacterium sp. JT-ISH-224, complexed with a donor productCMPand an acceptor substrate lactose	Photobacterium sp.

Organism

Organism	UniProt	Comment	Textmining
Photobacterium sp.	A8QYL1	JT-ISH-224	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
CMP-N-acetylneuraminate + lactose	Asp232 might act as a catalytic base for deprotonation of the acceptor substrate, and His405 might act as a catalytic acid for protonation of the donor substrate	Photobacterium sp.	CMP + 6'-sialyllactose	-	?

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Release 2023.1 (January 2023)