Functional Diversity of Mammalian Sialyltransferases

  • Takashima Shou
    The Noguchi institute, 1-8-1 Kaga, Itabashi, Tokyo 173-0003, Japan
  • Tsuji Shuichi
    Institute of Glycoscience, Tokai University, 4-1-1 Kitakaname, Hiratsuka, Kanagawa 259-1292, Japan

Bibliographic Information

Other Title
  • 哺乳類シアル酸転移酵素の機能多様性
  • ホニュウルイ シアルサン テンイ コウソ ノ キノウ タヨウセイ

Search this article

Description

Sialic acids are negatively charged acidic sugars. Sialyltransferases are enzymes that catalyze the synthesis of sialylglycoconjugates, which play important roles in various biological processes. Twenty members of the mammalian sialyltransferase superfamily have been identified to date. These enzymes are grouped into 4 families according to the type of carbohydrate linkage they synthesize: β-galactoside α2,3-sialyltransferases (ST3Gal-I-VI), β-galactoside α2,6-sialyltransferases (ST6Gal-I and -II), GalNAc α2,6-sialyltransferases (ST6GalNAc-I-VI), and α2,8-sialyltransferases (ST8Sia-I-VI). Each sialyltransferase has its specific function in the complicated mammalian body system. In this review, we describe the functional diversity of mammalian sialyltransferases on the basis of recent studies and discuss the necessity for 20 different sialyltransferases.

Journal

Citations (6)*help

See more

References(255)*help

See more

Details 詳細情報について

Report a problem

Back to top