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Evolutionary origin and functional diversification of aminotransferases

Aminotransferases (ATs) are pyridoxal 5′-phosphate–dependent enzymes that catalyze the transamination reactions between amino acid donor and keto acid acceptor substrates. Modern AT enzymes constitute ∼2% of all classified enzymatic activities, play central roles in nitrogen metabolism, and generate...

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Autores principales: Koper, Kaan, Han, Sang-Woo, Pastor, Delia Casas, Yoshikuni, Yasuo, Maeda, Hiroshi A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9309667/
https://www.ncbi.nlm.nih.gov/pubmed/35697072
http://dx.doi.org/10.1016/j.jbc.2022.102122
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author Koper, Kaan
Han, Sang-Woo
Pastor, Delia Casas
Yoshikuni, Yasuo
Maeda, Hiroshi A.
author_facet Koper, Kaan
Han, Sang-Woo
Pastor, Delia Casas
Yoshikuni, Yasuo
Maeda, Hiroshi A.
author_sort Koper, Kaan
collection PubMed
description Aminotransferases (ATs) are pyridoxal 5′-phosphate–dependent enzymes that catalyze the transamination reactions between amino acid donor and keto acid acceptor substrates. Modern AT enzymes constitute ∼2% of all classified enzymatic activities, play central roles in nitrogen metabolism, and generate multitude of primary and secondary metabolites. ATs likely diverged into four distinct AT classes before the appearance of the last universal common ancestor and further expanded to a large and diverse enzyme family. Although the AT family underwent an extensive functional specialization, many AT enzymes retained considerable substrate promiscuity and multifunctionality because of their inherent mechanistic, structural, and functional constraints. This review summarizes the evolutionary history, diverse metabolic roles, reaction mechanisms, and structure–function relationships of the AT family enzymes, with a special emphasis on their substrate promiscuity and multifunctionality. Comprehensive characterization of AT substrate specificity is still needed to reveal their true metabolic functions in interconnecting various branches of the nitrogen metabolic network in different organisms.
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spelling pubmed-93096672022-07-26 Evolutionary origin and functional diversification of aminotransferases Koper, Kaan Han, Sang-Woo Pastor, Delia Casas Yoshikuni, Yasuo Maeda, Hiroshi A. J Biol Chem JBC Reviews Aminotransferases (ATs) are pyridoxal 5′-phosphate–dependent enzymes that catalyze the transamination reactions between amino acid donor and keto acid acceptor substrates. Modern AT enzymes constitute ∼2% of all classified enzymatic activities, play central roles in nitrogen metabolism, and generate multitude of primary and secondary metabolites. ATs likely diverged into four distinct AT classes before the appearance of the last universal common ancestor and further expanded to a large and diverse enzyme family. Although the AT family underwent an extensive functional specialization, many AT enzymes retained considerable substrate promiscuity and multifunctionality because of their inherent mechanistic, structural, and functional constraints. This review summarizes the evolutionary history, diverse metabolic roles, reaction mechanisms, and structure–function relationships of the AT family enzymes, with a special emphasis on their substrate promiscuity and multifunctionality. Comprehensive characterization of AT substrate specificity is still needed to reveal their true metabolic functions in interconnecting various branches of the nitrogen metabolic network in different organisms. American Society for Biochemistry and Molecular Biology 2022-06-11 /pmc/articles/PMC9309667/ /pubmed/35697072 http://dx.doi.org/10.1016/j.jbc.2022.102122 Text en © 2022 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle JBC Reviews
Koper, Kaan
Han, Sang-Woo
Pastor, Delia Casas
Yoshikuni, Yasuo
Maeda, Hiroshi A.
Evolutionary origin and functional diversification of aminotransferases
title Evolutionary origin and functional diversification of aminotransferases
title_full Evolutionary origin and functional diversification of aminotransferases
title_fullStr Evolutionary origin and functional diversification of aminotransferases
title_full_unstemmed Evolutionary origin and functional diversification of aminotransferases
title_short Evolutionary origin and functional diversification of aminotransferases
title_sort evolutionary origin and functional diversification of aminotransferases
topic JBC Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9309667/
https://www.ncbi.nlm.nih.gov/pubmed/35697072
http://dx.doi.org/10.1016/j.jbc.2022.102122
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