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Structure-function relationships in enzymes from psychrophilic (cold-loving) bacteria

Dutch title: Structuur-funktie relaties bij enzymen uit psychrofiele (koudeminnende) bacterien
Funder identifier: P101/1943210070; P101/1953210450 (Other contract id)
Period: 1994 till December 1996
Status: Completed
 Institutes 

Institutes (2)  Top 
  • Vrije Universiteit Brussel; Vakgroep Toegepaste Biologische Wetenschappen; Laboratorium voor Microbiologie (VUB), more
  • Vrije Universiteit Brussel; Vakgroep Toegepaste Biologische Wetenschappen; Laboratorium voor Microbiologie (VUB), more, sponsor

Abstract
The relationships between temperature, catalytic activity, regulatory properties and stability will be investigated in a group of three enzymes chosen as model systems for the study of psychrophilic (cold-loving) bacteria isolated from the Antarctic Ocean by H. RĂ¼ger and N. Glansdorff. The enzymes are the carbamoyltransferases of aspartate (one of the three or four best known allosteric enzymes), of ornithine and carbamoylphosphate synthetase. In order to investigate the relationships between structure and function in these enzymes we shall determine their kinetic, allosteric and thermal profiles, clone the corresponding genes, sequence them and proceed to a thorough comparison with the mesophilic and thermophilic homologs. Experiments of in vitro mutagenesis will be performed to test the hypothesis formulated on the basis of these investigations.

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