<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>15(9)</volume><submitter>Perfetto R</submitter><pubmed_abstract>The carbonic anhydrase (CA, EC 4.2.1.1) superfamily of metalloenzymes catalyzes the hydration of carbon dioxide to bicarbonate and protons. The catalytically active form of these enzymes incorporates a metal hydroxide derivative, the formation of which is the rate-determining step of catalytic reaction, being affected by the transfer of a proton from a metal-coordinated water molecule to the environment. Here, we report the cloning, expression, and purification of a particular CA, i.e., nacrein-like protein encoded in the genome of the Pacific oyster Magallana gigas (previously known as Crassostrea gigas). Furthermore, the amino acid sequence, kinetic constants, and anion inhibition profile of the recombinant enzyme were investigated for the first time. The new protein, CgiNAP2X1, is highl</pubmed_abstract><journal>Marine drugs</journal><pagination>E270</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5618409</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Sequence Analysis, Kinetic Constants, and Anion Inhibition Profile of the Nacrein-Like Protein (CgiNAP2X1) from the Pacific Oyster Magallana gigas (Ex-Crassostrea gigas).</pubmed_title><pmcid>PMC5618409</pmcid><pubmed_authors>Barone CMA</pubmed_authors><pubmed_authors>Perfetto R</pubmed_authors><pubmed_authors>Sansone G</pubmed_authors><pubmed_authors>Capasso C</pubmed_authors><pubmed_authors>Vullo D</pubmed_authors><pubmed_authors>Rossi M</pubmed_authors><pubmed_authors>Del Prete S</pubmed_authors><pubmed_authors>Supuran CT</pubmed_authors></additional><is_claimable>false</is_claimable><name>Sequence Analysis, Kinetic Constants, and Anion Inhibition Profile of the Nacrein-Like Protein (CgiNAP2X1) from the Pacific Oyster Magallana gigas (Ex-Crassostrea gigas).</name><description>The carbonic anhydrase (CA, EC 4.2.1.1) superfamily of metalloenzymes catalyzes the hydration of carbon dioxide to bicarbonate and protons. The catalytically active form of these enzymes incorporates a metal hydroxide derivative, the formation of which is the rate-determining step of catalytic reaction, being affected by the transfer of a proton from a metal-coordinated water molecule to the environment. Here, we report the cloning, expression, and purification of a particular CA, i.e., nacrein-like protein encoded in the genome of the Pacific oyster Magallana gigas (previously known as Crassostrea gigas). Furthermore, the amino acid sequence, kinetic constants, and anion inhibition profile of the recombinant enzyme were investigated for the first time. The new protein, CgiNAP2X1, is highl</description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Aug</publication><modification>2025-04-19T09:27:23.516Z</modification><creation>2019-03-27T02:57:36Z</creation></dates><accession>S-EPMC5618409</accession><cross_references><pubmed>28846630</pubmed><doi>10.3390/md15090270</doi></cross_references></HashMap>