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Literature summary 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

EC Number Application Comment Organism
2.4.3.1 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)

EC Number Cloned (Comment) Organism
2.4.3.1 expressed in Escherichia coli Photobacterium leiognathi

Organism

EC Number Organism UniProt Comment Textmining
2.4.3.1 Photobacterium leiognathi
-
 JT-SHIZ-145
-
2.4.3.1 Photobacterium leiognathi JT-SHIZ-145
-
 JT-SHIZ-145
-

Substrates and Products (Substrate)

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.3.1 8
-
-
 Photobacterium leiognathi