Evidence map›Paper›PMID 20304931›Full record

ArticleThe Journal of biological chemistry2010

Hidden function of catalytic domain in 6-methylsalicylic acid synthase for product release.

Tomomi Moriguchi, Yuichiro Kezuka, Takamasa Nonaka, Yutaka Ebizuka, Isao Fujii

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.0field-weighted citation impact, top 7% 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

17 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. The enzyme kinetics of branched-chain fatty acid synthesis of metazoan fatty acid synthase.Protein science : a publication of the Protein Society · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Insights into 6-Methylsalicylic Acid Bio-assembly by Using Chemical Probes.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2016
    Article
  8. Insights into 6-Methylsalicylic Acid Bio-assembly by Using Chemical Probes.Angewandte Chemie (International ed. in English) · 2016
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Construction and engineering of large biochemical pathways via DNA assembler.Methods in molecular biology (Clifton, N.J.) · 2013
    Article
  14. Article
  15. Dehydratase-specific probes for fatty acid and polyketide synthases.Journal of the American Chemical Society · 2012
    Article
  16. Article
  17. Article
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

5 authors at 2 institutions in 1 country.

Tomomi MoriguchiGraduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033.
Yuichiro KezukaSchool of Pharmacy, Iwate Medical University, 2-1-1 Nishitokuta, Yahaba, Iwate 028-3694, Japan.
Takamasa NonakaSchool of Pharmacy, Iwate Medical University, 2-1-1 Nishitokuta, Yahaba, Iwate 028-3694, Japan.
Yutaka EbizukaGraduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033.
Isao FujiiSchool of Pharmacy, Iwate Medical University, 2-1-1 Nishitokuta, Yahaba, Iwate 028-3694, Japan. Electronic address: ifujii@iwate-med.ac.jp.
Iwate Medical University · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Functional investigation of the proposed dehydratase domain of ATX, a 6-methylsalicylic acid synthase from Aspergillus terreus, revealed that the domain is not involved in dehydration of the beta-hydroxytriketide intermediate tethered on the acyl carrier protein but catalyzes thioester hydrolysis to release the product from the acyl carrier protein. Thus, we renamed this domain the thioester hydrolase (TH) domain. The intermediate bound to the TH domain of mutant H972A formed in the presence of NADPH was released as 6-methylsalicylic acid by both the intact ATX and by THID (a 541-amino acid region containing TH domain and its downstream) protein, in trans. Furthermore, THID showed a catalytic activity to hydrolyze a model substrate, 6-methylsalicylic acid-N-acetylcysteamine. The TH domain is the first example of a product-releasing domain that is located in the middle of a multidomain iterative type I polyketide synthase. Moreover, it is functionally different from serine protease-type thioesterase domains of iterative type I polyketide synthases.

Indexed as

AcyltransferasesAmino Acid SequenceAspergillusAutoradiographyCatalytic DomainElectrophoresis, Polyacrylamide GelEscherichia coliHydrolysisLigasesMultienzyme ComplexesOxidoreductasesPlasmids6-methylsalicylic acid synthetaseAcyltransferasesLigasesMultienzyme ComplexesOxidoreductases

Identifiers

PMID20304931
PMCPMC2865267
OpenAlexW1977520648

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.