Evidence map›Paper›PMID 36908174›Full record

ReviewProceedings of the Japan Academy. Series B, Physical and biological sciences2023

Research overview of L-DOPA production using a bacterial enzyme, tyrosine phenol-lyase.

Hidehiko Kumagai, Takane Katayama, Takashi Koyanagi, Hideyuki Suzuki

Open access · diamondAbstract readReview
In one paragraph

Review in Proceedings of the Japan Academy. Series B, Physical and biological sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

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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

4 authors at 3 institutions in 1 country.

Hidehiko KumagaiIshikawa Prefectural University.ORCID http://orcid.org/0000-0003-2464-3249
Takane KatayamaGraduate School of Biostudies, Kyoto University.ORCID http://orcid.org/0000-0003-4009-7874
Takashi KoyanagiIshikawa Prefectural University.ORCID http://orcid.org/0000-0003-3688-0022
Hideyuki SuzukiDivision of Applied Biology, Kyoto Institute of Technology.ORCID http://orcid.org/0000-0003-0323-7196
Ishikawa Prefectural University · JPKyoto Institute of Technology · JPKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

L-DOPA is an amino acid that is used as a treatment for Parkinson's disease. A simple enzymatic synthesis method of L-DOPA had been developed using bacterial L-tyrosine phenol-lyase (Tpl). This review describes research on screening of bacterial strains, culture conditions, properties of the enzyme, reaction mechanism of the enzyme, and the reaction conditions for the production of L-DOPA. Furthermore, molecular bleeding of constitutively Tpl-overproducing strains is described, which were developed based on mutations in a DNA binding protein, TyrR, which controls the induction of tpl gene expression.

Indexed as

Tyrosine Phenol-LyaseBacteriaLevodopaLevodopaTyrosine Phenol-LyaseErwinia herbicolaEscherichia intermediaL-DOPAParkinson’s diseasetyrosine phenol-lyaseTyrR

Identifiers

PMID36908174
PMCPMC10170061
OpenAlexW4323655665

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.