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Related Experiment Video

Updated: Sep 8, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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Evolutionary origin and functional diversification of aminotransferases.

Kaan Koper¹, Sang-Woo Han², Delia Casas Pastor³

¹Department of Botany, University of Wisconsin-Madison, Madison, Wisconsin, USA.

The Journal of Biological Chemistry

|June 13, 2022

Summary

Aminotransferases (ATs) are crucial enzymes in nitrogen metabolism. This review explores their evolution, diverse roles, and emphasizes their substrate promiscuity and multifunctionality in various organisms.

Keywords:

PLP-dependent enzymes amino acids aminotransferases enzyme evolution nitrogen metabolism transaminases

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Area of Science:

Biochemistry
Enzymology
Metabolic Engineering

Background:

Aminotransferases (ATs) are pyridoxal 5'-phosphate-dependent enzymes central to nitrogen metabolism.
They catalyze essential transamination reactions, generating numerous primary and secondary metabolites.
ATs represent approximately 2% of all classified enzymatic activities.

Purpose of the Study:

To review the evolutionary history of AT enzymes.
To summarize their diverse metabolic roles, reaction mechanisms, and structure-function relationships.
To highlight the substrate promiscuity and multifunctionality within the AT enzyme family.

Main Methods:

Literature review and synthesis of existing research on aminotransferases.
Analysis of evolutionary divergence and functional specialization of AT classes.
Examination of structural and mechanistic constraints influencing AT substrate specificity.

Main Results:

AT enzymes likely diverged into four classes before the last universal common ancestor.
Despite functional specialization, many ATs retain significant substrate promiscuity and multifunctionality.
The review consolidates current knowledge on ATs' evolutionary trajectory and metabolic significance.

Conclusions:

Aminotransferases play a vital and diverse role in organismal metabolism.
Understanding AT substrate specificity is key to fully elucidating their function in nitrogen metabolic networks.
Further comprehensive characterization is needed to reveal the full metabolic scope of these enzymes.