Multifaceted Regulations of Gateway Enzyme Phenylalanine Ammonia-Lyase in the Biosynthesis of Phenylpropanoids

• Published in: Molecular plant Vol. 8; no. 1; pp. 17 - 27
• Main Authors: Zhang, Xuebin, Liu, Chang-Jun
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 05.01.2015; Elsevier
• Subjects: BASIC BIOLOGICAL SCIENCES; biosynthesis; carbon; economic valuation; enzyme activity; metabolic regulation; metabolites; phenylalanine ammonia-lyase; Phenylalanine Ammonia-Lyase - metabolism; Phenylpropanoids; Plants - enzymology; Plants - metabolism; post-translational modification; Propanols - metabolism; Protein Processing, Post-Translational; phenylalanine ammonia-lyase; phenylpropanoids; metabolic regulation
• ISSN: 1674-2052; 1752-9867; 1752-9867
• DOI: 10.1016/j.molp.2014.11.001

Phenylpropanoid biosynthesis in plants engenders a vast variety of aromatic metabolites critically important for their growth, development, and environmental adaptation. Some of these aromatic compounds have high economic value. Phenylalanine ammonia-lyase (PAL) is the first committed enzyme in the pathway; it diverts the central flux of carbon from the primary metabolism to the synthesis of myriad phenolics. Over the decades, many studies have shown that exquisite regulatory mechanisms at multiple levels control the transcription and the enzymatic activity of PALs. In this review, a current overview of our understanding of the complicated regulatory mechanisms governing the activity of PAL is presented; recent progress in unraveling its post-translational modifications, its metabolite feedback regulation, and its enzyme organization is highlighted. Phenylalanine ammonia-lyase (PAL) is the first committed enzyme in phenylpropanoid biosynthesis pathway. It is controlled under a multitude of regulatory mechanisms. In this review, a current overview on our understanding of the complicated regulatory mechanisms governing the activity of PAL is presented.