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Literature summary for 2.4.3.1 extracted from

  • Yamamoto, T.; Hamada, Y.; Ichikawa, M.; Kajiwara, H.; Mine, T.; Tsukamoto, H.; Takakura, Y.
    A beta-galactoside alpha2,6-sialyltransferase produced by a marine bacterium, Photobacterium leiognathi JT-SHIZ-145, is active at pH 8 (2007), Glycobiology, 17, 1167-1174.
    View publication on PubMed

Application

Application Comment Organism
synthesis because this enzyme is most active at basic pH, sialyltransferase obtained from Photobacterium leiognathi JT-SHIZ-145 is a promising tool for the efficient production of sialosides and the modification of glycoconjugates Photobacterium leiognathi

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Photobacterium leiognathi

Organism

Organism UniProt Comment Textmining
Photobacterium leiognathi
-
JT-SHIZ-145
-
Photobacterium leiognathi JT-SHIZ-145
-
JT-SHIZ-145
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CMP-N-acetylneuraminate + lactose
-
Photobacterium leiognathi CMP + 6'-sialyllactose
-
?
CMP-N-acetylneuraminate + lactose
-
Photobacterium leiognathi JT-SHIZ-145 CMP + 6'-sialyllactose
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Photobacterium leiognathi