ArticleMolecular biology reports2012
Characterization, and expression profile of a phenylalanine ammonia lyase gene from Jatropha curcas L.
Article in Molecular biology reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Phenylalanine Ammonia-Lyase: A Core Regulator of Plant Carbon Metabolic Flux Redistribution-From Molecular Mechanisms and Growth Modulation to Stress Adaptability.Plants (Basel, Switzerland) · 2025Review
- Enzymatic Characterization ofPlants (Basel, Switzerland) · 2024Article
- Expression profiling of the phenylalanine ammonia-lyase (Plant signaling & behavior · 2023Article
- Identification and Characterization of an Efficient Phenylalanine Ammonia-Lyase from Photorhabdus luminescens.Applied biochemistry and biotechnology · 2021Article
- A comprehensive in silico characterization of bacterial signal peptides for the excretory production of3 Biotech · 2018Article
- Article
- Isolation and Functional Characterization of a Phenylalanine Ammonia-Lyase Gene (SsPAL1) from Coleus (Solenostemon scutellarioides (L.) Codd).Molecules (Basel, Switzerland) · 2015Article
- JcCBF2 gene from Jatropha curcas improves freezing tolerance of Arabidopsis thaliana during the early stage of stress.Molecular biology reports · 2015Article
- Molecular evolution and functional characterisation of an ancient phenylalanine ammonia-lyase gene (NnPAL1) from Nelumbo nucifera: novel insight into the evolution of the PAL family in angiosperms.BMC evolutionary biology · 2014Article
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Authors and funding
11 authors.
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Abstract
A PAL gene designated as JcPAL1 was cloned from J. curcas L. The full-length is 2336 bp in size with one intron and two exons, encoding a polypeptide of 713 amino acids. Its 5'-upstream region is rich in putative cis-elements including not only PAL typical TATA box, L-box and transcriptional initiation site (TIS) but also light responding motifs. Expression pattern analysis indicated that JcPAL1 were expressed in all tissues, most highly in flowers. When Treated with ABA, GA3, high and low temperature, expression of JcPAL1 were induced. Recombinant JcPAL1 has a pH optimum at 8.7 and a temperature optimum at 60°C in 100 mM Tris-HCl buffer. The Km and Kcat values are 0.125 mM and 1.73 S(-1) for L: -phenylalanine, and 1.312 mM and 0.109 S(-1) for L: -tyrosine, respectively. These findings suggested that JcPAL1 might involve in the J. curcas responding to various stresses and L: -Phe should be its true physiological substrate. This study is essential prior to uncover whether and how the PAL initiated phenylpropanoid metabolic networks functioning in the defense responses of J. curcas.
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