Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases?
Candida Antarctica lipase B (CALB) is a well-known enzyme, especially because of its promiscuous activity. Due to its properties, CALB was widely used as a benchmark for designing new catalysts for important organic reactions. The active site of CALB is very similar to that of soluble epoxide hydrol...
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| Format: | Article |
| Language: | English |
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MDPI AG
2015-09-01
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| Series: | Molecules |
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| Online Access: | http://www.mdpi.com/1420-3049/20/10/17789 |
| _version_ | 1811232500504068096 |
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| author | Isabel Bordes José Recatalá Katarzyna Świderek Vicent Moliner |
| author_facet | Isabel Bordes José Recatalá Katarzyna Świderek Vicent Moliner |
| author_sort | Isabel Bordes |
| collection | DOAJ |
| description | Candida Antarctica lipase B (CALB) is a well-known enzyme, especially because of its promiscuous activity. Due to its properties, CALB was widely used as a benchmark for designing new catalysts for important organic reactions. The active site of CALB is very similar to that of soluble epoxide hydrolase (sEH) formed by a nucleophile-histidine-acid catalytic triad and an oxyanion hole typical for molecular structures derived from processes of α/β hydrolases. In this work we are exploring these similarities and proposing a Ser105Asp variant of CALB as a new catalyst for epoxide hydrolysis. In particular, the hydrolysis of the trans-diphenylpropene oxide (t-DPPO) is studied by means of quantum cluster models mimicking the active site of both enzymes. Our results, based on semi-empirical and DFT calculations, suggest that mutant Ser105Asp CALB is a good protein scaffold to be used for the bio-synthesis of chiral compounds. |
| first_indexed | 2024-04-12T11:03:53Z |
| format | Article |
| id | doaj.art-cf4b12b9443d46a2a4c0cb885267d58f |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-04-12T11:03:53Z |
| publishDate | 2015-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-cf4b12b9443d46a2a4c0cb885267d58f2022-12-22T03:35:52ZengMDPI AGMolecules1420-30492015-09-012010177891780610.3390/molecules201017789molecules201017789Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases?Isabel Bordes0José Recatalá1Katarzyna Świderek2Vicent Moliner3Departament de Química Física i Analítica, Universitat Jaume I, Castellón 12071, SpainDepartament de Química Física i Analítica, Universitat Jaume I, Castellón 12071, SpainDepartament de Química Física i Analítica, Universitat Jaume I, Castellón 12071, SpainDepartament de Química Física i Analítica, Universitat Jaume I, Castellón 12071, SpainCandida Antarctica lipase B (CALB) is a well-known enzyme, especially because of its promiscuous activity. Due to its properties, CALB was widely used as a benchmark for designing new catalysts for important organic reactions. The active site of CALB is very similar to that of soluble epoxide hydrolase (sEH) formed by a nucleophile-histidine-acid catalytic triad and an oxyanion hole typical for molecular structures derived from processes of α/β hydrolases. In this work we are exploring these similarities and proposing a Ser105Asp variant of CALB as a new catalyst for epoxide hydrolysis. In particular, the hydrolysis of the trans-diphenylpropene oxide (t-DPPO) is studied by means of quantum cluster models mimicking the active site of both enzymes. Our results, based on semi-empirical and DFT calculations, suggest that mutant Ser105Asp CALB is a good protein scaffold to be used for the bio-synthesis of chiral compounds.http://www.mdpi.com/1420-3049/20/10/17789Candida antarctica lipase BCALBepoxide hydrolasesEHreaction mechanismtrans-diphenylpropene oxideenzyme promiscuitycatalysisquantum cluster models |
| spellingShingle | Isabel Bordes José Recatalá Katarzyna Świderek Vicent Moliner Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? Molecules Candida antarctica lipase B CALB epoxide hydrolase sEH reaction mechanism trans-diphenylpropene oxide enzyme promiscuity catalysis quantum cluster models |
| title | Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
| title_full | Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
| title_fullStr | Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
| title_full_unstemmed | Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
| title_short | Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
| title_sort | is promiscuous calb a good scaffold for designing new epoxidases |
| topic | Candida antarctica lipase B CALB epoxide hydrolase sEH reaction mechanism trans-diphenylpropene oxide enzyme promiscuity catalysis quantum cluster models |
| url | http://www.mdpi.com/1420-3049/20/10/17789 |
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