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Chemoenzymatic synthesis of ADP-d-glycero-?-d-manno-heptose and study of the substrate specificity of HldE.

ABSTRACT: An efficient one-pot three enzymes strategy for chemoenzymatic synthesis of ADP-d-glycero-?-d-manno-heptose (ADP-d, d-heptose) was reported using chemically synthesized d, d-heptose-7-phosphate and the ADP-d, d-heptose biosynthetic enzymes HldE and GmhB. Moreover, the result of investigating substrate specificity of the kinase action of HldE revealed that HldE had highly restricted substrate specificity towards structurally modified heptose-7-phosphate analogs.

SUBMITTER: Li T 

PROVIDER: S-EPMC3976583 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature

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Chemoenzymatic synthesis of ADP-d-glycero-β-d-manno-heptose and study of the substrate specificity of HldE.

Li Tiehai T   Wen Liuqing L   Williams Adriel A   Wu Baolin B   Li Lei L   Qu Jingyao J   Meisner Jeffrey J   Xiao Zhongying Z   Fang Junqiang J   Wang Peng George PG  

Bioorganic & medicinal chemistry 20131219 3

An efficient one-pot three enzymes strategy for chemoenzymatic synthesis of ADP-d-glycero-β-d-manno-heptose (ADP-d, d-heptose) was reported using chemically synthesized d, d-heptose-7-phosphate and the ADP-d, d-heptose biosynthetic enzymes HldE and GmhB. Moreover, the result of investigating substrate specificity of the kinase action of HldE revealed that HldE had highly restricted substrate specificity towards structurally modified heptose-7-phosphate analogs. ...[more]

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