skip to main content

This content will become publicly available on December 11, 2015

Title: Multifaceted regulations of gateway enzyme phenylalanine ammonia-lyase in the biosynthesis of phenylpropanoids

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 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, we present a current overview on our understanding of the complicated regulatory mechanisms governing PAL's activity; we particularly highlight recent progresses in unraveling its post-translational modifications, its metabolite feedback regulation, and its enzyme organization.
 [1] ;  [1]
  1. Brookhaven National Lab. (BNL), Upton, NY (United States)
Publication Date:
OSTI Identifier:
Report Number(s):
Journal ID: ISSN 1674-2052; R&D Project: BO-169; KC0304000
Grant/Contract Number:
Accepted Manuscript
Journal Name:
Molecular Plant
Additional Journal Information:
Journal Volume: 8; Journal Issue: 1; Journal ID: ISSN 1674-2052
Research Org:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
59 BASIC BIOLOGICAL SCIENCES; Phenylpropanoids; phenylalanine ammonia-lyase; metabolic regulation