Characterization and synthetic application of a novel β1,3-galactosyltransferase from Escherichia coli O55:H7

被引：52

作者：

Liu, Xian-wei ^{[1
,2
,3
,4
]}

Xia, Chengfeng ^{[3
,4
,5
]}

Li, Lei ^{[1
,2
,3
,4
]}

Guan, Wan-yi ^{[1
,2
,3
,4
]}

Pettit, Nicholas ^{[3
,4
]}

Zhang, Hou-cheng ^{[1
,2
]}

Chen, Min ^{[1
,2
]}

Wang, Peng George ^{[3
,4
]}

机构：

[1] Shandong Univ, Natl Glycoengn Res Ctr, Jinan 250100, Shandong, Peoples R China

[2] Shandong Univ, State Key Lab Microbial Technol, Jinan 250100, Shandong, Peoples R China

[3] Ohio State Univ, Dept Chem, Columbus, OH 43202 USA

[4] Ohio State Univ, Dept Biochem, Columbus, OH 43202 USA

[5] Chinese Acad Sci, Kunming Inst Bot, State Key Lab Phytochem & Plant Resources W China, Kunming 650204, Peoples R China

来源：

BIOORGANIC & MEDICINAL CHEMISTRY | 2009年 / 17卷 / 14期

关键词：

O-Antigen; Galactosyltransferase; Type; 1; chain; Lacto-N-tetraose; MURINE UDP-GALACTOSE; N-BIOSE-I; POLYSACCHARIDE SYNTHESIS; PSEUDOMONAS-AERUGINOSA; TYPE-1; CHAIN; HUMAN-MILK; EXPRESSION; ANTIGENS; CELLS; GAL-BETA-1-3GLCNAC;

D O I：

10.1016/j.bmc.2009.06.005

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A beta 1,3-galactosyltransferase (WbgO) was identified in Escherichia coli O55:H7. Its function was confirmed by radioactive activity assay and structure analysis of the disaccharide synthesized with the recombinant enzyme. WbgO requires a divalent metal ion, either Mn2+ or Mg2+, for its activity and is active between pH 6.0-8.0 with a pH optimum of 7.0. N-acetylglucosamine (GlcNAc) and oligosaccharides with GlcNAc at the non-reducing end were shown to be its preferred substrates and it can be used for the synthesis of type 1 glycan chains from these substrates. Together with a recombinant bacterial GlcNAc-transferase, benzyl beta-lacto-N-tetraoside was synthesized with the purified WbgO to demonstrate the synthetic utility of WbgO. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：4910 / 4915

页数：6

共 33 条

[1] Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].

Altschul, SF ;

Madden, TL ;

Schaffer, AA ;

Zhang, JH ;

Zhang, Z ;

Miller, W ;

Lipman, DJ .

NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402

[2] On the preparative use of recombinant β(1-3)galactosyl-transferase [J].

Baisch, G ;

Öhrlein, R ;

Streiff, M ;

Kolbinger, F .

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 1998, 8 (07) :751-754

[3] Functional characterization of GumK, a membrane-associated β-glucuronosyltransferase from Xanthomonas campestris required for xanthan polysaccharide synthesis [J].

Barreras, M ;

Abdian, PL ;

Ielpi, L .

GLYCOBIOLOGY, 2004, 14 (03) :233-241

[4] High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcβ1→3Gal and GalNAcβ1-3Gal linkages [J].

Blixt, O ;

van Die, I ;

Norberg, T ;

van den Eijnden, DH .

GLYCOBIOLOGY, 1999, 9 (10) :1061-1071

[5] Structures and mechanisms of glycosyltransferases [J].

Breton, C ;

Snajdrová, L ;

Jeanneau, C ;

Koca, J ;

Imberty, A .

GLYCOBIOLOGY, 2006, 16 (02) :29R-37R

[6] The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics [J].

Cantarel, Brandi L. ;

Coutinho, Pedro M. ;

Rancurel, Corinne ;

Bernard, Thomas ;

Lombard, Vincent ;

Henrissat, Bernard .

NUCLEIC ACIDS RESEARCH, 2009, 37 :D233-D238

[7] Interactions between enteropathogenic Escherichia coli and host epithelial cells [J].

Donnenberg, MS ;

Kaper, JB ;

Finlay, BB .

TRENDS IN MICROBIOLOGY, 1997, 5 (03) :109-114

[8] Screening for galectin-3 inhibitors from synthetic lacto-N-biose libraries using microscale affinity chromatography coupled to mass spectrometry [J].

Fort, Sebastien ;

Kim, Hyo-Sun ;

Hindsgaul, Ole .

JOURNAL OF ORGANIC CHEMISTRY, 2006, 71 (19) :7146-7154

[9]

German JB, 2008, NESTLE NUTR WORKS SE, V62, P205, DOI 10.1159/000146322

[10]

Hakomori S, 2001, ADV EXP MED BIOL, V491, P369

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