Structural and mechanistic basis of bacterial sugar nucleotide-modifying enzymes

被引:28
作者
Field, RA
Naismith, JH [1 ]
机构
[1] Univ St Andrews, Ctr Biomol Sci, St Andrews KY16 9ST, Fife, Scotland
[2] Univ E Anglia, Sch Chem Sci & Pharm, Ctr Carbohydrate Chem, Norwich NR4 7TJ, Norfolk, England
基金
英国生物技术与生命科学研究理事会;
关键词
D O I
10.1021/bi0345079
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
Recently, carbohydrates have come to the fore because of their central role in many biological processes. One area of current interest concerns the enzymatic modification of sugar nucleotides, in relation to both secondary metabolite glycosylation and the formation of complex cell surface-associated glycoconjugates. Bacteria, in particular, have proven to be a rich field in which to study these transformations, because they are often unique to specific classes of organisms. This has led to the realization that such microbial biosynthetic pathways might be exploited in the generation of novel antibiotics, or indeed serve as targets for such compounds. This work illustrates the interplay between protein structure determination, chemistry, and molecular biology in providing insight into the mechanism of such biochemical transformations.
引用
收藏
页码:7637 / 7647
页数:11
相关论文
共 95 条
[91]   Crystal structures of the oxidized and reduced forms of UDP-galactose 4-epimerase isolated from Escherichia coli [J].
Thoden, JB ;
Frey, PA ;
Holden, HM .
BIOCHEMISTRY, 1996, 35 (08) :2557-2566
[92]   Molecular structure of the NADH/UDP-glucose abortive complex of UDP-galactose 4-epimerase from Escherichia coli: Implications for the catalytic mechanism [J].
Thoden, JB ;
Frey, PA ;
Holden, HM .
BIOCHEMISTRY, 1996, 35 (16) :5137-5144
[93]   Nature's carbohydrate chemists: The enzymatic glycosylation of bioactive bacterial metabolites [J].
Thorson, JS ;
Hosted, TJ ;
Jiang, JQ ;
Biggins, JB ;
Ahlert, J .
CURRENT ORGANIC CHEMISTRY, 2001, 5 (02) :139-167
[94]  
WEE TG, 1973, J BIOL CHEM, V248, P33
[95]   Studies of UDP-galactopyranose mutase from Escherichia coli:: An unusual role of reduced FAD in its catalysis [J].
Zhang, QB ;
Liu, HW .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2000, 122 (38) :9065-9070