Literature summary 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.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.4.3.1 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.4.3.1 |
Photobacterium sp. |
A8QYL1 |
JT-ISH-224 |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.4.3.1 |
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 |
- |
? |
|