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

Bioorg Med Chem

Department of Chemistry, Center for Therapeutics and Diagnostics, Georgia State University, Atlanta, GA 30303, USA; National Glycoengineering Research Center, Shandong University, Jinan, Shandong 250100, People's Republic of China. Electronic address:

Published: February 2014

AI Article Synopsis

  • Researchers developed a one-pot method using three enzymes to efficiently produce ADP-d-glycero-β-d-manno-heptose (ADP-d, d-heptose).
  • The process involves chemically synthesized d, d-heptose-7-phosphate and the biosynthetic enzymes HldE and GmhB.
  • Additionally, it was found that the enzyme HldE has very limited substrate specificity, only acting on certain modified heptose-7-phosphate analogs.

Article Abstract

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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3976583PMC
http://dx.doi.org/10.1016/j.bmc.2013.12.019DOI Listing

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