Understanding the Importance of Protein Structure to Nature's Routes for Divergent Evolution in TIM Barrel Enzymes
- 20 February 2004
- journal article
- Published by American Chemical Society (ACS) in Accounts of Chemical Research
- Vol. 37 (3) , 149-158
- https://doi.org/10.1021/ar030250v
Abstract
It is widely agreed that new enzymes evolve from existing ones through the duplication of genes encoding existing enzymes followed by sequence divergence. While evolution is an inherently random process, studies of divergently related enzymes have shown that the evolution of new enzymes follows one of three general routes in which the substrate specificity, reaction mechanism, or active site architecture of the progenitor enzyme is reused in the new enzyme. Recent developments in structural biology relating to divergently related (beta/alpha)8 enzymes have brought new insight into these processes and have revealed that conserved structural elements play an important role in divergent evolution. These studies have shown that, although evolution occurs as a series of random mutations, stable folds such as the (beta/alpha)8 barrel and structural features of the active sites of enzymes are frequently reused in evolution and adapted for new catalytic purposes.Keywords
This publication has 34 references indexed in Scilit:
- Catalysing New Reactions during Evolution: Economy of Residues and MechanismJournal of Molecular Biology, 2003
- Evolution of function in (β/α)8-barrel enzymesCurrent Opinion in Chemical Biology, 2003
- Two (βα)8-Barrel Enzymes of Histidine and Tryptophan Biosynthesis Have Similar Reaction Mechanisms and Common Strategies for Protecting Their Labile Substrates,Biochemistry, 2002
- One Fold with Many Functions: The Evolutionary Relationships between TIM Barrel Families Based on their Sequences, Structures and FunctionsJournal of Molecular Biology, 2002
- Homologous (β/α)8-Barrel Enzymes That Catalyze Unrelated Reactions: Orotidine 5‘-Monophosphate Decarboxylase and 3-Keto-l-Gulonate 6-Phosphate Decarboxylase,Biochemistry, 2002
- Divergent Evolution of Enzymatic Function: Mechanistically Diverse Superfamilies and Functionally Distinct SuprafamiliesAnnual Review of Biochemistry, 2001
- Catalytic promiscuity and the evolution of new enzymatic activitiesChemistry & Biology, 1999
- The Enolase Superfamily: A General Strategy for Enzyme-Catalyzed Abstraction of the α-Protons of Carboxylic Acids†Biochemistry, 1996
- ENZYME RECRUITMENT IN EVOLUTION OF NEW FUNCTIONAnnual Review of Microbiology, 1976
- On the Evolution of Biochemical SynthesesProceedings of the National Academy of Sciences, 1945