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

Bioorg Med Chem. 2014 Feb 1;22(3):1139-47. doi: 10.1016/j.bmc.2013.12.019. Epub 2013 Dec 19.

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.

Keywords: Analogs; Chemoenzymatic; Specificity; Synthesis.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate Sugars / chemical synthesis*
  • Adenosine Diphosphate Sugars / metabolism
  • Chemistry Techniques, Synthetic
  • Multienzyme Complexes / metabolism*
  • Nucleotidyltransferases / metabolism*
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism*
  • Substrate Specificity
  • Sugar Phosphates / chemistry

Substances

  • Adenosine Diphosphate Sugars
  • Multienzyme Complexes
  • Sugar Phosphates
  • Phosphotransferases (Alcohol Group Acceptor)
  • Nucleotidyltransferases
  • D,D heptose 7-phosphate kinase-D,D-heptose 1-phosphate adenylyltransferase, E coli