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Functional Diversity of Mammalian Sialyltransferases
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- Takashima Shou
- The Noguchi institute, 1-8-1 Kaga, Itabashi, Tokyo 173-0003, Japan
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- Tsuji Shuichi
- Institute of Glycoscience, Tokai University, 4-1-1 Kitakaname, Hiratsuka, Kanagawa 259-1292, Japan
Bibliographic Information
- Other Title
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- 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
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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
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- Trends in Glycoscience and Glycotechnology
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Trends in Glycoscience and Glycotechnology 23 (132), 178-193, 2011
FCCA(Forum: Carbohydrates Coming of Age)
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Details 詳細情報について
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- CRID
- 1390282679346494464
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- NII Article ID
- 10030388791
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- NII Book ID
- AA10995236
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- ISSN
- 18832113
- 09157352
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- NDL BIB ID
- 023456150
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL Search
- Crossref
- CiNii Articles
- OpenAIRE
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- Abstract License Flag
- Disallowed