Evidence map›Paper›PMID 20354908›Full record

ArticleMolecular biology reports2011

Molecular characterization of a phenylalanine ammonia-lyase gene (BoPAL1) from Bambusa oldhamii.

Lu-Sheng Hsieh, Yi-Lin Hsieh, Chuan-Shan Yeh, Chieh-Yang Cheng, Chien-Chih Yang, Ping-Du Lee

Abstract read
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Article in Molecular biology reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.8field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 55 citations in OpenAlex.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Lu-Sheng HsiehInstitute of Microbiology and Biochemistry, Department of Biochemical Science and Technology, College of Life Science, National Taiwan University, 1 Roosevelt Road Section 4, Taipei, 106, Taiwan, ROC.
Yi-Lin Hsieh
Chuan-Shan Yeh
Chieh-Yang Cheng
Chien-Chih Yang
Ping-Du Lee
National Taiwan University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phenylalanine ammonia-lyase is the first enzyme of general phenylpropanoid pathway. A PAL gene, designated as BoPAL1, was cloned from a Bambusa oldhamii cDNA library. The open reading frame of BoPAL1 was 2,139 bp in size and predicted to encode a 712-amino acid polypeptide. BoPAL1 was the first intronless PAL gene found in angiosperm plant. Several putative cis-acting elements such as P box, GT-1motif, and SOLIPs involved in light responsiveness were found in the 5'-flanking sequence of BoPAL1 which was obtained by TAIL-PCR method. Recombinant BoPAL1 protein expressed in Pichia pastoris was active. The optimum temperature and pH for BoPAL1 activity was 50°C and 9.0, respectively. The molecular mass of recombinant BoPAL1 was estimated as 323 kDa using gel filtration chromatography and the molecular mass of full-length BoPAL was about 80 kDa, indicating that BoPAL1 presents as a homotetramer. The Km and kcat values of BoPAL1 for L-Phe were 1.01 mM and 10.11 s(-1), respectively. The recombinant protein had similar biochemical properties with PALs reported in other plants.

Indexed as

5' Flanking RegionBambusaBase SequenceChromatography, AffinityCloning, MolecularGenes, PlantKineticsModels, MolecularMolecular Sequence DataPhenylalanine Ammonia-LyasePichiaPlant ProteinsRecombinant ProteinsRegulatory Sequences, Nucleic AcidSpecies SpecificityPhenylalanine Ammonia-LyasePlant ProteinsRecombinant Proteins

Identifiers

PMID20354908
OpenAlexW1973455979

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.