Evidence map›Paper›PMID 33411135›Full record

ArticleApplied biochemistry and biotechnology2021

Identification and Characterization of an Efficient Phenylalanine Ammonia-Lyase from Photorhabdus luminescens.

Fang Zhang, Jie Ren, Jixun Zhan

Abstract read
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In one paragraph

Article in Applied biochemistry and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.8field-weighted citation impact, top 30% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Frontiers in microbiology · 2022
    Review
  8. Plants (Basel, Switzerland) · 2021
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 2 countries.

Fang ZhangDepartment of Biological Engineering, Utah State University, 4105 Old Main Hill, Logan, UT, 84322, USA.
Jie RenDepartment of Biological Engineering, Utah State University, 4105 Old Main Hill, Logan, UT, 84322, USA.
Jixun ZhanDepartment of Biological Engineering, Utah State University, 4105 Old Main Hill, Logan, UT, 84322, USA. jixun.zhan@usu.edu.ORCID http://orcid.org/0000-0003-0200-9183
Utah State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A putative aromatic amino acid ammonia-lyase gene (named Pl-pal) was discovered in Photorhabdus luminescens DSM 3368. BLAST and phylogenetic analyses predicted that this enzyme is a histidine ammonia-lyase, whereas sequence alignment suggested that it is more likely a phenylalanine ammonia-lyase (PAL). This gene was amplified from P. luminescens and expressed in Escherichia coli BL21(DE3). The function of Pl-PAL (58 kDa) was characterized by in vitro enzymatic reactions with L-phenylalanine (L-Phe), L-tyrosine (L-Tyr), L-histidine (L-His), and L-tryptophan (L-Trp). Pl-PAL can convert L-Phe and L-Tyr to trans-cinnamic acid and p-coumaric acid, respectively, but had no function on L-His and L-Trp. The optimum temperature and pH were determined to be 40 °C and 11.0, respectively. Under the optimal conditions, Pl-PAL had a k

Indexed as

Bacterial ProteinsPhenylalanine Ammonia-LyasePhotorhabdusRecombinant ProteinsBacterial ProteinsPhenylalanine Ammonia-LyaseRecombinant ProteinsHeterologous expressionIn vitro enzymatic reactionsPhenylalanine ammonia-lyasePhotorhabdus luminescensWhole-cell transformation

Identifiers

PMID33411135
OpenAlexW3119040357

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.