Bifunctional Phenylalanine/Tyrosine Ammonia-Lyase (PTAL) Enhances Lignin Biosynthesis: Implications in Carbon Fixation in Plants by Genetic Engineering.
Arabidopsis
PTAL
bioengineering
carbon fixation
lignin biosynthesis
phenylalanine
tyrosine
weedy rice
Journal
Biology
ISSN: 2079-7737
Titre abrégé: Biology (Basel)
Pays: Switzerland
ID NLM: 101587988
Informations de publication
Date de publication:
22 Sep 2024
22 Sep 2024
Historique:
received:
02
09
2024
revised:
18
09
2024
accepted:
19
09
2024
medline:
28
9
2024
pubmed:
28
9
2024
entrez:
28
9
2024
Statut:
epublish
Résumé
Lignin is a key metabolite for terrestrial plants. Two types of aromatic amino acids, phenylalanine (Phe) and tyrosine (Tyr), serve as the precursors for lignin biosynthesis. In most plant species, Phe is deaminated by Phe ammonia-lyase (PAL) to initiate lignin biosynthesis, but in grass species, Phe and Tyr are deaminated by Phe/Tyr ammonia-lyase (PTAL). To understand the efficiency of PAL and PTAL, we used transgenic and non-transgenic Arabidopsis with PAL and crop-weedy rice hybrids (CWRH) with PTAL to analyze lignin-biosynthesis-associated metabolites. The transgenic plants overexpressed the exogenous 5-enolpyruvylshikimate-3-phosphate synthase (
Identifiants
pubmed: 39336169
pii: biology13090742
doi: 10.3390/biology13090742
pii:
doi:
Types de publication
Journal Article
Langues
eng
Subventions
Organisme : National Natural Science Foundation of China
ID : 32070245
Organisme : National Natural Science Foundation of China
ID : 31770409