{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Grigorian E"],"funding":["Agence Nationale de la Recherche","Centre National de la Recherche Scientifique"],"pagination":["e4540"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9794022"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(1)"],"pubmed_abstract":["Haloacid dehalogenases are potentially involved in bioremediation of contaminated environments and few have been biochemically characterized from marine organisms. The l-2-haloacid dehalogenase (l-2-HAD) from the marine Bacteroidetes Zobellia galactanivorans Dsij<sup>T</sup> (ZgHAD) has been shown to catalyze the dehalogenation of C2 and C3 short-chain l-2-haloalkanoic acids. To better understand its catalytic properties, its enzymatic stability, active site, and 3D structure were analyzed. ZgHAD demonstrates high stability to solvents and a conserved catalytic activity when heated up to 60°C, its melting temperature being at 65°C. The X-ray structure of the recombinant enzyme was solved by molecular replacement. The enzyme folds as a homodimer and its active site is very similar to DehRhb"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["X-ray structure and mechanism of ZgHAD, a l-2-haloacid dehalogenase from the marine Flavobacterium Zobellia galactanivorans."],"pmcid":["PMC9794022"],"funding_grant_id":["ANR‐10‐BTBR‐04"],"pubmed_authors":["Grigorian E","Czjzek M","Leblanc C","Roret T","Delage L"],"additional_accession":[]},"is_claimable":false,"name":"X-ray structure and mechanism of ZgHAD, a l-2-haloacid dehalogenase from the marine Flavobacterium Zobellia galactanivorans.","description":"Haloacid dehalogenases are potentially involved in bioremediation of contaminated environments and few have been biochemically characterized from marine organisms. The l-2-haloacid dehalogenase (l-2-HAD) from the marine Bacteroidetes Zobellia galactanivorans Dsij<sup>T</sup> (ZgHAD) has been shown to catalyze the dehalogenation of C2 and C3 short-chain l-2-haloalkanoic acids. To better understand its catalytic properties, its enzymatic stability, active site, and 3D structure were analyzed. ZgHAD demonstrates high stability to solvents and a conserved catalytic activity when heated up to 60°C, its melting temperature being at 65°C. The X-ray structure of the recombinant enzyme was solved by molecular replacement. The enzyme folds as a homodimer and its active site is very similar to DehRhb","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2026-05-27T21:03:54.013Z","creation":"2025-02-18T22:34:28.514Z"},"accession":"S-EPMC9794022","cross_references":{"pubmed":["36502283"],"doi":["10.1002/pro.4540"]}}