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J Lehmann1, E Pfeiffer

  • 1Chemisches Laboratorium der Universität i. Br., Freiburg, Germany

FEBS Letters
|May 1, 1970
PubMed
Summary
This summary is machine-generated.

Researchers identified TDP-4-keto-D-glucose as a key intermediate in the enzymatic conversion of TDP-D-glucose to TDP-L-rhamnose. This intermediate is enzyme-bound, explaining the stereospecificity observed during the reaction.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Microbial Metabolism

Background:

  • TDP-D-glucose is a precursor in various metabolic pathways.
  • E. coli B possesses enzymes involved in sugar nucleotide transformations.
  • Understanding enzymatic intermediates is crucial for metabolic pathway elucidation.

Purpose of the Study:

  • To investigate the intermediate in the enzymatic conversion of TDP-D-glucose to TDP-L-rhamnose.
  • To determine the stereochemical properties of the reaction mechanism.

Main Methods:

  • Incubation of TDP-D-glucose with E. coli B enzyme extract.
  • Treatment with sodium borohydride (NaB(3)H(4)) for reduction.
  • Hydrolysis of sugar nucleotide fractions and analysis of labeled products.

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Main Results:

  • D-galactose-4-(3H) was produced, but no 3H-labeled D-glucose.
  • The stereospecificity of NaB(3)H(4) reduction was observed.
  • TDP-4-keto-D-glucose was identified as an intermediate.

Conclusions:

  • TDP-4-keto-D-glucose is an intermediate in TDP-D-glucose to TDP-L-rhamnose conversion.
  • The intermediate is likely enzyme-bound to explain stereospecificity.
  • This finding provides insight into the mechanism of TDP-L-rhamnose biosynthesis.