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HERO ID
2995790
Reference Type
Journal Article
Title
Fungal and Plant Phenylalanine Ammonia-lyase
Author(s)
Hyun, MW; Yun, YH; Kim, JY; Kim, SH
Year
2011
Volume
39
Issue
4
Page Numbers
257-265
Language
English
PMID
22783113
DOI
10.5941/MYCO.2011.39.4.257
Abstract
L-Phenylalanine is one of the essential amino acids that cannot be synthesized in mammals in adequate amounts to meet the requirements for protein synthesis. Fungi and plants are able to synthesize phenylalanine via the shikimic acid pathway. L-Phenylalanine, derived from the shikimic acid pathway, is used directly for protein synthesis in plants or metabolized through the phenylpropanoid pathway. This phenylpropanoid metabolism leads to the biosynthesis of a wide array of phenylpropanoid secondary products. The first step in this metabolic sequence involves the action of phenylalanine ammonia-lyase (PAL). The discovery of PAL enzyme in fungi and the detection of (14)CO(2) production from (14)C-ring-labeled phenylalanine and cinnamic acid demonstrated that certain fungi can degrade phenylalanine by a pathway involving an initial deamination to cinnamic acid, as happens in plants. In this review, we provide background information on PAL and a recent update on the presence of PAL genes in fungi.
Tags
IRIS
•
Ammonia
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