Evidence map›Paper›PMID 25815148›Full record

ArticleACS medicinal chemistry letters2015

α-Carbonic Anhydrases Possess Thioesterase Activity.

Muhammet Tanc, Fabrizio Carta, Andrea Scozzafava, Claudiu T Supuran

Abstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Coumarin carbonic anhydrase inhibitors from natural sources.Journal of enzyme inhibition and medicinal chemistry · 2020
    Review
  10. Investigation of pesticides on honey bee carbonic anhydrase inhibition.Journal of enzyme inhibition and medicinal chemistry · 2020
    Article
  11. Phosphorylation increases the catalytic activity of rainbow trout gill cytosolic carbonic anhydrase.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2016
    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

4 authors.

Muhammet TancLaboratorio di Chimica Bioinorganica, Università degli Studi di Firenze, Polo Scientifico , Room 188, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy ; NEUROFARBA Department, Sezione di Scienze Farmaceutiche e Nutraceutiche, Università degli Studi di Firenze , Via Ugo Schiff 6, 50019 Sesto Fiorentino, Florence, Italy.
Fabrizio CartaNEUROFARBA Department, Sezione di Scienze Farmaceutiche e Nutraceutiche, Università degli Studi di Firenze , Via Ugo Schiff 6, 50019 Sesto Fiorentino, Florence, Italy.
Andrea ScozzafavaNEUROFARBA Department, Sezione di Scienze Farmaceutiche e Nutraceutiche, Università degli Studi di Firenze , Via Ugo Schiff 6, 50019 Sesto Fiorentino, Florence, Italy.
Claudiu T SupuranLaboratorio di Chimica Bioinorganica, Università degli Studi di Firenze, Polo Scientifico , Room 188, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy ; NEUROFARBA Department, Sezione di Scienze Farmaceutiche e Nutraceutiche, Università degli Studi di Firenze , Via Ugo Schiff 6, 50019 Sesto Fiorentino, Florence, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The α-carbonic anhydrases (CAs, EC 4.2.1.1) show catalytic versatility acting as esterases with carboxylic, sulfonic, and phosphate esters. Here we prove by kinetic, spectroscopic, and MS studies that they also possess thioesterase activity with a dithiocarbamate ester as a substrate (PhSO2NHCSSMe). Its CA-mediated hydrolysis leads to benzenesulfonamide, methyl mercaptan, and COS. The CA thioesterase activity may be useful for designing prodrug enzyme inhibitors, whereas some CA isoforms may use this activity for modulating physiologic/pathologic processes, which are possibly amenable to drug discovery of agents with multiple mechanisms of action.

Indexed as

Carbonic anhydraseinhibitorsprodrugsthioesterase

Identifiers

PMID25815148
PMCPMC4360143

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.