Evidence map›Paper›PMID 32042199›Full record

ArticleNature chemical biology2020

A suicide enzyme catalyzes multiple reactions for biotin biosynthesis in cyanobacteria.

Kei Sakaki, Keita Ohishi, Tetsu Shimizu, Ikki Kobayashi, Naoki Mori, Kenichi Matsuda, Takeo Tomita, Hidenori Watanabe, Kan Tanaka, Tomohisa Kuzuyama and 1 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. A ferritin-like diiron oxygenase BioE initiates bacterial biotin synthesis, a promising antivirulence target.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Oxidative Dearomatization of PLP in Thiamin Pyrimidine Biosynthesis inJournal of the American Chemical Society · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. An Unusual Route forJournal of bacteriology · 2020
    Article
  13. 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

11 authors at 1 institution in 1 country.

Kei Sakaki *Biotechnology Research Center, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.ORCID http://orcid.org/0000-0003-3226-1013
Keita Ohishi *Biotechnology Research Center, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Tetsu ShimizuBiotechnology Research Center, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Ikki KobayashiLaboratory for Chemistry and Life Science Institute of Innovative Research, Tokyo Institute of Technology, Midori-ku, Yokohama, Japan.
Naoki MoriDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Kenichi MatsudaBiotechnology Research Center, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Takeo TomitaBiotechnology Research Center, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Hidenori WatanabeDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Kan TanakaLaboratory for Chemistry and Life Science Institute of Innovative Research, Tokyo Institute of Technology, Midori-ku, Yokohama, Japan.
Tomohisa KuzuyamaBiotechnology Research Center, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.ORCID http://orcid.org/0000-0002-7221-5858
Makoto NishiyamaBiotechnology Research Center, The University of Tokyo, Bunkyo-ku, Tokyo, Japan. umanis@mail.ecc.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0001-8143-8052
The University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In biotin biosynthesis, the conversion of pimeloyl intermediates to biotin is catalyzed by a universal set of four enzymes: BioF, BioA, BioD and BioB. We found that the gene homologous to bioA, the product of which is involved in the conversion of 8-amino-7-oxononanoate (AON) to 7,8-diaminononanoate (DAN), is missing in the genome of the cyanobacterium Synechocystis sp. PCC 6803. We provide structural and biochemical evidence showing that a novel dehydrogenase, BioU, is involved in biotin biosynthesis and functionally replaces BioA. This enzyme catalyzes three reactions: formation of covalent linkage with AON to yield a BioU-DAN conjugate at the ε-amino group of Lys124 of BioU using NAD(P)H, carboxylation of the conjugate to form BioU-DAN-carbamic acid, and release of DAN-carbamic acid using NAD(P)

Indexed as

Amino AcidsAmino Acids, DiaminoAmino Acid SequenceBacterial ProteinsBiosynthetic PathwaysBiotinCatalysisCloning, MolecularCyanobacteriaDNA, BacterialEscherichia coliGenes, BacterialOxidoreductasesSynechocystisTransaminases7,8-diaminopelargonic acid8-amino-7-oxooctanoic acidAmino AcidsAmino Acids, DiaminoBacterial ProteinsBioA protein, bacteriaBiotinDNA, BacterialOxidoreductasesTransaminases

Identifiers

PMID32042199
OpenAlexW3004570048

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.