Chemical Function of Substituted Amino Acids in Glyceraldehyde-3-Phosphate Dehydrogenase

Abstract

An investigation of the amino acids responsible for the thermostability of the T. aquaticus glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was initiated. The gene encoding this enzyme was isolated from a genomic library and sequenced. The gene encoded a functional GAPDH by virtue of its ability to rescue a mutant bacterial strain whose own GAPDH gene was deleted. The heat-stability of the isolated enzyme is impressive, i.e., it retains 100% of its activity after 2 hours at 90 C while requiring 100 C to lose 50% of its activity. Defining the conditions for crystallization as well as the physicochemical properties of the purified GAPDH are currently ongoing.

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Document Details

Document Type
Technical Report
Publication Date
Nov 12, 1991
Accession Number
ADA244388

Entities

People

  • Ralph M. Hecht

Organizations

  • University of Houston

Tags

Communities of Interest

  • Human Systems

DTIC Thesaurus Topics

  • Acids
  • Aldehydes
  • Amino Acids
  • Classification
  • Coding
  • Crystallization
  • Genetic Structures
  • Heat Energy
  • Military Research
  • Nucleic Acids
  • Scientists
  • Security
  • Structural Analysis
  • Thermostability
  • Three Dimensional

Readers

  • Molecular Genetics
  • Molecular and Cellular Biochemistry