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Related Experiment Videos

Plant glycerol-3-phosphate-1-acyltransferase (GPAT): structure selectivity studies.

A R Slabas1, W R Simon, T Schierer

  • 1Department of Biological Sciences, University of Durham, Science Laboratories, South Road, Durham DH1 3LE, UK. A.R.Slabas@Durham.ac.uk

Biochemical Society Transactions
|February 15, 2001
PubMed
Summary

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Squash glycerol-3-phosphate-1-acyltransferase structure was determined, revealing substrate selectivity differences. Site-directed mutagenesis and structural analysis will clarify enzyme mechanisms.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzyme kinetics

Background:

  • Glycerol-3-phosphate-1-acyltransferase (GPAT) is crucial for lipid biosynthesis.
  • Understanding GPAT substrate selectivity is key to metabolic pathway regulation.

Purpose of the Study:

  • To determine the crystal structure of squash GPAT.
  • To investigate the enzyme's substrate selectivity using in vitro assays and mutagenesis.

Main Methods:

  • X-ray crystallography at 1.9-A resolution.
  • Multiple isomorphous replacement with wild-type and mutant enzymes.
  • Competitive in vitro substrate selectivity assays at near-physiological concentrations.

Main Results:

  • The crystal structure of squash GPAT was determined.

Related Experiment Videos

  • Substrate selectivity was demonstrated with acyl-acyl carrier protein but not acyl-CoA.
  • Assays differentiated between selective and non-selective enzyme forms.

    • Conclusions:

    • Structural determination provides a basis for understanding GPAT function.
    • Site-directed mutagenesis coupled with structural data can elucidate substrate selectivity determinants.