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Related Experiment Video

Updated: May 27, 2026

Following the Dynamics of Structural Variants in Experimentally Evolved Populations

Following the Dynamics of Structural Variants in Experimentally Evolved Populations

Published on: February 3, 2023

Divergence and convergence in enzyme evolution.

Michael Y Galperin¹, Eugene V Koonin¹

¹National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894.

The Journal of Biological Chemistry

|November 10, 2011

Summary

This summary is machine-generated.

Enzyme superfamilies show conserved active sites but diverse functions. Sequence analysis aids in predicting protein functions, guiding experimental studies for uncharacterized enzymes.

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Area of Science:

Biochemistry
Bioinformatics
Structural Biology

Background:

Enzymes exhibit functional convergence and divergence across species.
Structurally distinct enzymes can perform similar reactions, while similar enzymes may act on different substrates.

Purpose of the Study:

To analyze sequence and structural patterns in enzyme superfamilies.
To investigate conserved and diverse features within ATP-grasp, alkaline phosphatase, cupin, HD hydrolase, and N-terminal nucleophile (Ntn) hydrolase superfamilies.

Main Methods:

Comparative sequence analysis of enzymes from prokaryotic and eukaryotic genomes.
Examination of sequence motifs, active site residues, and predicted reaction mechanisms.

Main Results:

Enzymes within superfamilies share conserved sequence motifs and active site residues.
The strained active site conformation (entatic state) is often conserved, facilitating substrate binding and transition complex formation.
Reaction outcomes can vary due to enzyme and substrate structural specifics.

Conclusions:

Enzyme superfamilies display conserved active site properties but diverse functional outcomes.
Sequence-based functional predictions, while imprecise, are valuable for annotating uncharacterized proteins and directing experimental research.