Evolution of enzyme structure

Proceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character
B S Hartley

Abstract

Three-dimensional structures of enzymes offer evidence about their evolution. There are clear examples of divergent families (e.g. mammalian serine proteases) and convergence (e.g. chymotrypsin and subtilisin). Topological similarities in dehydrogenases may reflect an ancient divergence or merely chemical constraints on protein architectures. Further experimental evidence is desirable to back up arguments based on molecular morphology. By growing microorganisms on novel foodstuffs in a chemostat, one can focus selective pressure on a specific enzyme activity. Experiments will be described in which such pressure is focused on pentitol metabolism. Examination of the fine structure of the genes responsible for this pentitol metabolism has given clues about the volution of metabolic pathways.

References

Jul 15, 1986·Experientia·E J Barrington
Jan 1, 1983·CRC Critical Reviews in Biochemistry·W V Shaw
Nov 20, 1986·Journal of Molecular Biology·D M Burns, I R Beacham
Apr 5, 1988·Journal of Molecular Biology·R J Read, M N James
Jan 1, 1981·Annals of the New York Academy of Sciences·D Hewett-EmmettM Goodman
Mar 31, 1995·The Journal of Biological Chemistry·S S SidhuT J Borgford

Related Concepts

Microorganism
Alkalescens-Dispar Group
Genes
Enzymes, antithrombotic
Science of Morphology
Peptide Hydrolases
Subtilisins
Enzyme structure
Serine Endopeptidases
Metabolic Syndrome Pathway

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