Abstract
Lewis x (Lex) and sialyl Lewis x (SLex)-containing glycans play important roles in numerous physiological and pathological processes. The key enzyme for the final step formation of these Lewis antigens is α1-3-fucosyltransferase. Here we report molecular cloning and functional expression of a novel Helicobacter hepaticus α1-3- fucosyltransferase (HhFT1) which shows activity towards both non-sialylated and sialylated Type II oligosaccharide acceptor substrates. It is a promising catalyst for enzymatic and chemoenzymatic synthesis of Lex, sialyl Lex and their derivatives. Unlike all other α1-3/4- fucosyltransferases characterized so far which belong to Carbohydrate Active Enzyme (CAZy, http://www.cazy.org/) glycosyltransferase family GT10, the HhFT1 shares protein sequence homology with α1-2-fucosyltransferases and belongs to CAZy glycosyltransferase family GT11. The HhFT1 is thus the first α1-3-fucosyltransferase identified in the GT11 family.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1077-1088 |
| Number of pages | 12 |
| Journal | Glycobiology |
| Volume | 20 |
| Issue number | 9 |
| DOIs | |
| State | Published - Sep 2010 |
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Keywords
- cloning
- fucosyltransferase
- Helicobacter hepaticus
- Lewis x
- sialyl Lewis x
ASJC Scopus subject areas
- Biochemistry
Cite this
Helicobacter hepaticus Hh0072 gene encodes a novel α1-3- fucosyltransferase belonging to CAZy GT11 family. / Zhang, Lei; Lau, Kam; Cheng, Jiansong; Yu, Hai; Li, Yanhong; Sugiarto, Go; Huang, Shengshu; Ding, Li; Thon, Vireak; Wang, Peng G.; Chen, Xi.
In: Glycobiology, Vol. 20, No. 9, 09.2010, p. 1077-1088.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Helicobacter hepaticus Hh0072 gene encodes a novel α1-3- fucosyltransferase belonging to CAZy GT11 family
AU - Zhang, Lei
AU - Lau, Kam
AU - Cheng, Jiansong
AU - Yu, Hai
AU - Li, Yanhong
AU - Sugiarto, Go
AU - Huang, Shengshu
AU - Ding, Li
AU - Thon, Vireak
AU - Wang, Peng G.
AU - Chen, Xi
PY - 2010/9
Y1 - 2010/9
N2 - Lewis x (Lex) and sialyl Lewis x (SLex)-containing glycans play important roles in numerous physiological and pathological processes. The key enzyme for the final step formation of these Lewis antigens is α1-3-fucosyltransferase. Here we report molecular cloning and functional expression of a novel Helicobacter hepaticus α1-3- fucosyltransferase (HhFT1) which shows activity towards both non-sialylated and sialylated Type II oligosaccharide acceptor substrates. It is a promising catalyst for enzymatic and chemoenzymatic synthesis of Lex, sialyl Lex and their derivatives. Unlike all other α1-3/4- fucosyltransferases characterized so far which belong to Carbohydrate Active Enzyme (CAZy, http://www.cazy.org/) glycosyltransferase family GT10, the HhFT1 shares protein sequence homology with α1-2-fucosyltransferases and belongs to CAZy glycosyltransferase family GT11. The HhFT1 is thus the first α1-3-fucosyltransferase identified in the GT11 family.
AB - Lewis x (Lex) and sialyl Lewis x (SLex)-containing glycans play important roles in numerous physiological and pathological processes. The key enzyme for the final step formation of these Lewis antigens is α1-3-fucosyltransferase. Here we report molecular cloning and functional expression of a novel Helicobacter hepaticus α1-3- fucosyltransferase (HhFT1) which shows activity towards both non-sialylated and sialylated Type II oligosaccharide acceptor substrates. It is a promising catalyst for enzymatic and chemoenzymatic synthesis of Lex, sialyl Lex and their derivatives. Unlike all other α1-3/4- fucosyltransferases characterized so far which belong to Carbohydrate Active Enzyme (CAZy, http://www.cazy.org/) glycosyltransferase family GT10, the HhFT1 shares protein sequence homology with α1-2-fucosyltransferases and belongs to CAZy glycosyltransferase family GT11. The HhFT1 is thus the first α1-3-fucosyltransferase identified in the GT11 family.
KW - cloning
KW - fucosyltransferase
KW - Helicobacter hepaticus
KW - Lewis x
KW - sialyl Lewis x
UR - http://www.scopus.com/inward/record.url?scp=77955459001&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77955459001&partnerID=8YFLogxK
U2 - 10.1093/glycob/cwq068
DO - 10.1093/glycob/cwq068
M3 - Article
C2 - 20466652
AN - SCOPUS:77955459001
VL - 20
SP - 1077
EP - 1088
JO - Glycobiology
JF - Glycobiology
SN - 0959-6658
IS - 9
ER -