Biochemical characterization of plant aromatic aminotransferases.

Autor:	Koper K; Department of Botany, University of Wisconsin-Madison, Madison, WI, United States. Electronic address: koper@wisc.edu., Hataya S; Research Faculty of Agriculture, Hokkaido University, Sapporo, Japan., Hall AG; Department of Botany, University of Wisconsin-Madison, Madison, WI, United States., Takasuka TE; Research Faculty of Agriculture, Hokkaido University, Sapporo, Japan., Maeda HA; Department of Botany, University of Wisconsin-Madison, Madison, WI, United States. Electronic address: maeda2@wisc.edu.
Jazyk:	angličtina
Zdroj:	Methods in enzymology [Methods Enzymol] 2023; Vol. 680, pp. 35-83. Date of Electronic Publication: 2022 Sep 07.
DOI:	10.1016/bs.mie.2022.07.034
Abstrakt:	Aromatic aminotransferases (Aro ATs) are pyridoxal-5-phosphate (PLP)-dependent enzymes that catalyze the transamination reactions of an aromatic amino acid (AAA) or a keto acid. Aro ATs are involved in biosynthesis or degradation of AAAs and play important functions in controlling the production of plant hormones and secondary metabolites, such as auxin, tocopherols, flavonoids, and lignin. Most Aro ATs show substrate promiscuity and can accept multiple aromatic and non-aromatic amino and keto acid substrates, which complicates and limits our understanding of their in planta functions. Considering the critical roles Aro ATs play in plant primary and secondary metabolism, it is important to accurately determine substrate specificity and kinetic properties of Aro ATs. This chapter describes various methodologies of protein expression, purification and enzymatic assays, which can be used for biochemical characterization of Aro ATs. (Copyright © 2023 Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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