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Sequence and structural differences between enzyme and nonenzyme homologs.

Annabel E Todd¹, Christine A Orengo, Janet M Thornton

¹Biochemistry and Molecular Biology Department, University College London, United Kingdom.

Structure (London, England : 1993)

|October 16, 2002

Summary

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This study reveals that nonenzymes often evolve from ancestral enzymes, with disrupted active sites hindering function. This evolutionary path, rather than enzyme gain, is common for novel function development.

Area of Science:

Biochemistry
Evolutionary Biology
Structural Biology

Background:

Understanding the evolution of novel biological functions is crucial.
Homologous enzymes and nonenzymes with known structures provide insights into evolutionary pathways.

Purpose of the Study:

To analyze the sequence, structure, and function of homologous enzymes and nonenzymes.
To elucidate the evolutionary mechanisms leading to novel functions.

Main Methods:

Sequence analysis of homologous proteins.
Structural analysis of enzymes and nonenzymes.
Functional characterization of protein pairs.

Main Results:

Nonenzymes predominantly originate from ancestral catalytic precursors.

Related Experiment Videos

Active site disruption, through residue substitution or steric hindrance, is a key feature in nonenzyme evolution.

Low sequence identity and functional divergence are common between enzyme-nonenzyme pairs.

Conclusions:

The evolution of novel functions often involves the loss of catalytic activity from ancestral enzymes.
Structural modifications of active sites play a critical role in the transition from enzyme to nonenzyme.
The study discusses complex evolutionary scenarios including heterooligomeric enzymes and duplicated domains.