دورية أكاديمية
Defluorination Capability of l-2-Haloacid Dehalogenases in the HAD-Like Hydrolase Superfamily Correlates with Active Site Compactness
| العنوان: | Defluorination Capability of l-2-Haloacid Dehalogenases in the HAD-Like Hydrolase Superfamily Correlates with Active Site Compactness |
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| المؤلفون: | Chan, Peter W. Y., Chakrabarti, Nilmadhab, Ing, Chris, Halgas, Ondrej, To, Terence K. W., Wälti, Marielle, Petit, Alain-Pierre, Tran, Christopher, Savchenko, Alexei, Yakunin, Alexander F., Edwards, Elizabeth A., Pomès, Régis, Pai, Emil F. |
| المصدر: | Chan , P W Y , Chakrabarti , N , Ing , C , Halgas , O , To , T K W , Wälti , M , Petit , A-P , Tran , C , Savchenko , A , Yakunin , A F , Edwards , E A , Pomès , R & Pai , E F 2022 , ' Defluorination Capability of l-2-Haloacid Dehalogenases in the HAD-Like Hydrolase Superfamily Correlates with Active Site Compactness ' , ChemBioChem , vol. 23 , no. 1 , e202100414 . https://doi.org/10.1002/cbic.202100414Test |
| سنة النشر: | 2022 |
| المجموعة: | Discovery - University of Dundee Online Publications |
| مصطلحات موضوعية: | enzyme catalysis, enzymic defluorination, L-2-haloacid dehalogenases, molecular dynamics, protein structures, /dk/atira/pure/subjectarea/asjc/1300/1303, name=Biochemistry, /dk/atira/pure/subjectarea/asjc/1300/1313, name=Molecular Medicine, /dk/atira/pure/subjectarea/asjc/1300/1312, name=Molecular Biology, /dk/atira/pure/subjectarea/asjc/1600/1605, name=Organic Chemistry |
| الوصف: | l-2-Haloacid dehalogenases, industrially and environmentally important enzymes that catalyse cleavage of the carbon-halogen bond in S-2-halocarboxylic acids, were known to hydrolyse chlorinated, brominated and iodinated substrates but no activity towards fluorinated compounds had been reported. A screen for novel dehalogenase activities revealed four l-2-haloacid dehalogenases capable of defluorination. We now report crystal structures for two of these enzymes, Bpro0530 and Rha0230, as well as for the related proteins PA0810 and RSc1362, which hydrolyse chloroacetate but not fluoroacetate, all at ∼2.2 Å resolution. Overall structure and active sites of these enzymes are highly similar. In molecular dynamics (MD) calculations, only the defluorinating enzymes sample more compact conformations, which in turn allow more effective interactions with the small fluorine atom. Structural constraints, based on X-ray structures and MD calculations, correctly predict the defluorination activity of the homologous enzyme ST2570. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | https://discovery.dundee.ac.uk/en/publications/34c2e792-c3a2-4bcf-8f36-0f28f3f3329cTest |
| DOI: | 10.1002/cbic.202100414 |
| الإتاحة: | https://doi.org/10.1002/cbic.202100414Test https://discovery.dundee.ac.uk/en/publications/34c2e792-c3a2-4bcf-8f36-0f28f3f3329cTest http://www.scopus.com/inward/record.url?scp=85117465831&partnerID=8YFLogxKTest |
| حقوق: | info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsbas.4B68B45B |
| قاعدة البيانات: | BASE |
| DOI: | 10.1002/cbic.202100414 |
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