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Restructuring catalysis in the mandelate pathway.

D C Neidhart1, P L Howell, G A Petsko

  • 1Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.

Biochemical Society Symposium
|January 1, 1990
PubMed
Summary
This summary is machine-generated.

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Mandelate racemase (MR) is a TIM-barrel enzyme crucial for bacterial mandelic acid metabolism. Its structure reveals remarkable similarity to muconate lactonizing enzyme (MLE), suggesting evolutionary links and potential for enzyme engineering.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Mandelate racemase (MR) initiates the bacterial conversion of mandelic acid to benzoic acid.
  • The mandelate pathway's ability to process both mandelate enantiomers relies on MR's interconversion activity.

Purpose of the Study:

  • To determine the three-dimensional structure of mandelate racemase (MR).
  • To explore the evolutionary relationship between MR and other enzymes.

Main Methods:

  • X-ray crystallography was used to solve the structure of MR at 2.5 A resolution.

Main Results:

  • The determined structure of MR shows a conformation nearly identical to muconate lactonizing enzyme (MLE).
  • Both MR and MLE belong to the TIM-barrel protein superfamily.

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Conclusions:

  • The structural similarity between MR and MLE provides significant insights into enzyme evolution and the origin of metabolic pathways.
  • This finding suggests that MR could potentially be engineered into MLE through site-directed mutagenesis.