Evidence map›Paper›PMID 28229634›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2017

Biochemical characterization of the native α-carbonic anhydrase purified from the mantle of the Mediterranean mussel, Mytilus galloprovincialis.

Rosa Perfetto, Sonia Del Prete, Daniela Vullo, Giovanni Sansone, Carmela Barone, Mosè Rossi, Claudiu T Supuran, Clemente Capasso

Open access · goldAbstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2017. 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
2.1field-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

13 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Introduction to Carbonic Anhydrase.Sub-cellular biochemistry · 2026
    Review
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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

8 authors at 3 institutions in 1 country.

Rosa Perfettoa Istituto di Bioscienze e Biorisorse, CNR , Napoli , Italy.
Sonia Del Pretea Istituto di Bioscienze e Biorisorse, CNR , Napoli , Italy.
Daniela Vullob Dipartimento Neurofarba , Università degli Studi di Firenze, Sezione di Scienze Farmaceutiche, and Laboratorio di Chimica Bioinorganica, Polo Scientifico , Sesto Fiorentino , Florence , Italy.
Giovanni Sansonec Dipartimento di Biologia , Università degli Studi di Napoli, Federico II , Napoli , Italy.
Carmela Baroned Dipartimento di Agraria , Università degli Studi di Napoli, Federico II , Portici (Napoli) , Italy.
Mosè Rossia Istituto di Bioscienze e Biorisorse, CNR , Napoli , Italy.
Claudiu T Supuranb Dipartimento Neurofarba , Università degli Studi di Firenze, Sezione di Scienze Farmaceutiche, and Laboratorio di Chimica Bioinorganica, Polo Scientifico , Sesto Fiorentino , Florence , Italy.
Clemente Capassoa Istituto di Bioscienze e Biorisorse, CNR , Napoli , Italy.
Institute of Biosciences and Bioresources · ITUniversity of Florence · ITUniversity of Naples Federico II · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A α-carbonic anhydrase (CA, EC 4.2.1.1) has been purified and characterized biochemically from the mollusk Mytilus galloprovincialis. As in most mollusks, this α-CA is involved in the biomineralization processes leading to the precipitation of calcium carbonate in the mussel shell. The new enzyme had a molecular weight of 50 kDa, which is roughly two times higher than that of a monomeric α-class enzyme. Thus, Mytilus galloprovincialis α-CA is either a dimer, or similar to the Tridacna gigas CA described earlier, may have two different CA domains in its polypeptide chain. The Mytilus galloprovincialis α-CA sequence contained the three His residues acting as zinc ligands and the gate-keeper residues present in all α-CAs (Glu106-Thr199), but had a Lys in position 64 and not a His as proton shuttling residue, being thus similar to the human isoform hCA III. This probably explains the relatively low catalytic activity of Mytilus galloprovincialis α-CA, with the following kinetic parameters for the CO

Indexed as

AnimalsCarbonic Anhydrase InhibitorsCarbonic AnhydrasesMytilusCarbonic Anhydrase InhibitorsCarbonic AnhydrasesbivalveCarbonic anhydrasehydratase activitymetalloenzymesmusselprotonographyα-class enzyme

Identifiers

PMID28229634
PMCPMC6010126
OpenAlexW2591225413

What OpenQuestion holds

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LicenceCC BY
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.