Enhanced Thermostability of Lipoxygenase from Anabaena sp. PCC 7120 by Site-Directed Mutagenesis Based on Computer-Aided Rational Design
Lipoxygenase from Anabaena sp. PCC 7120 (Ana-LOX) was thermally unstable. So, improving the thermostability of the enzyme was quite essential. The target site of Ana-LOX selected for site-directed mutagenesis was based on computer-aided rational design. The thermostability and specific activity of A...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Diao, Hanwen [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016 |
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| Rechteinformationen: |
Nutzungsrecht: © Springer Science+Business Media New York 2016 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Applied biochemistry and biotechnology / A - New York, NY : Springer, 1994, 178(2016), 7, Seite 1339-1350 |
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| Übergeordnetes Werk: |
volume:178 ; year:2016 ; number:7 ; pages:1339-1350 |
| Links: |
|---|
| DOI / URN: |
10.1007/s12010-015-1950-2 |
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OLC1975144333 |
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| 520 | |a Lipoxygenase from Anabaena sp. PCC 7120 (Ana-LOX) was thermally unstable. So, improving the thermostability of the enzyme was quite essential. The target site of Ana-LOX selected for site-directed mutagenesis was based on computer-aided rational design. The thermostability and specific activity of Ana-LOX were improved with replacing valine with alanine at the target site 421 and the site 40. Compared to the wild-type enzyme which has a half-life (T 1/2) of inactivation of 3.8 min at 50 °C, the T 1/2 of mutant enzymes with V421A and V40A substitution increased to 4.4 and 7.0 min, respectively. The double mutant V421A/V40A showed a synergistic effect with a T 1/2 value of 8.3 min, resulting in a 1.18-fold improvement compared to the original Ana-LOX. V421A, V40A, and V421A/V40A also obtained 4.83, 41.58, and 80.07 % increase in specific activity, respectively. This study provides useful theoretical reference for enzyme molecular modification and computer-aided rational design. | ||
| 540 | |a Nutzungsrecht: © Springer Science+Business Media New York 2016 | ||
| 650 | 4 | |a Site-directed mutagenesis | |
| 650 | 4 | |a Biochemistry, general | |
| 650 | 4 | |a Chemistry | |
| 650 | 4 | |a Computer-aided rational design | |
| 650 | 4 | |a Thermostability | |
| 650 | 4 | |a Lipoxygenase | |
| 650 | 4 | |a Biotechnology | |
| 700 | 1 | |a Zhang, Chong |4 oth | |
| 700 | 1 | |a Wang, Shuicheng |4 oth | |
| 700 | 1 | |a Lu, Fengxia |4 oth | |
| 700 | 1 | |a Lu, Zhaoxin |4 oth | |
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10.1007/s12010-015-1950-2 doi PQ20160610 (DE-627)OLC1975144333 (DE-599)GBVOLC1975144333 (PRQ)p1420-a740b4ac53531622c94cb6d3b9762919d5b2a31de5e4b5dc8ea1a0a7876389590 (KEY)0068751020160000178000701339enhancedthermostabilityoflipoxygenasefromanabaenas DE-627 ger DE-627 rakwb eng 570 540 660 DNB 42.00 bkl Diao, Hanwen verfasserin aut Enhanced Thermostability of Lipoxygenase from Anabaena sp. PCC 7120 by Site-Directed Mutagenesis Based on Computer-Aided Rational Design 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Lipoxygenase from Anabaena sp. PCC 7120 (Ana-LOX) was thermally unstable. So, improving the thermostability of the enzyme was quite essential. The target site of Ana-LOX selected for site-directed mutagenesis was based on computer-aided rational design. The thermostability and specific activity of Ana-LOX were improved with replacing valine with alanine at the target site 421 and the site 40. Compared to the wild-type enzyme which has a half-life (T 1/2) of inactivation of 3.8 min at 50 °C, the T 1/2 of mutant enzymes with V421A and V40A substitution increased to 4.4 and 7.0 min, respectively. The double mutant V421A/V40A showed a synergistic effect with a T 1/2 value of 8.3 min, resulting in a 1.18-fold improvement compared to the original Ana-LOX. V421A, V40A, and V421A/V40A also obtained 4.83, 41.58, and 80.07 % increase in specific activity, respectively. This study provides useful theoretical reference for enzyme molecular modification and computer-aided rational design. Nutzungsrecht: © Springer Science+Business Media New York 2016 Site-directed mutagenesis Biochemistry, general Chemistry Computer-aided rational design Thermostability Lipoxygenase Biotechnology Zhang, Chong oth Wang, Shuicheng oth Lu, Fengxia oth Lu, Zhaoxin oth Enthalten in Applied biochemistry and biotechnology / A New York, NY : Springer, 1994 178(2016), 7, Seite 1339-1350 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:178 year:2016 number:7 pages:1339-1350 http://dx.doi.org/10.1007/s12010-015-1950-2 Volltext http://www.ncbi.nlm.nih.gov/pubmed/26686337 http://search.proquest.com/docview/1787036237 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_4012 42.00 AVZ AR 178 2016 7 1339-1350 |
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10.1007/s12010-015-1950-2 doi PQ20160610 (DE-627)OLC1975144333 (DE-599)GBVOLC1975144333 (PRQ)p1420-a740b4ac53531622c94cb6d3b9762919d5b2a31de5e4b5dc8ea1a0a7876389590 (KEY)0068751020160000178000701339enhancedthermostabilityoflipoxygenasefromanabaenas DE-627 ger DE-627 rakwb eng 570 540 660 DNB 42.00 bkl Diao, Hanwen verfasserin aut Enhanced Thermostability of Lipoxygenase from Anabaena sp. PCC 7120 by Site-Directed Mutagenesis Based on Computer-Aided Rational Design 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Lipoxygenase from Anabaena sp. PCC 7120 (Ana-LOX) was thermally unstable. So, improving the thermostability of the enzyme was quite essential. The target site of Ana-LOX selected for site-directed mutagenesis was based on computer-aided rational design. The thermostability and specific activity of Ana-LOX were improved with replacing valine with alanine at the target site 421 and the site 40. Compared to the wild-type enzyme which has a half-life (T 1/2) of inactivation of 3.8 min at 50 °C, the T 1/2 of mutant enzymes with V421A and V40A substitution increased to 4.4 and 7.0 min, respectively. The double mutant V421A/V40A showed a synergistic effect with a T 1/2 value of 8.3 min, resulting in a 1.18-fold improvement compared to the original Ana-LOX. V421A, V40A, and V421A/V40A also obtained 4.83, 41.58, and 80.07 % increase in specific activity, respectively. This study provides useful theoretical reference for enzyme molecular modification and computer-aided rational design. Nutzungsrecht: © Springer Science+Business Media New York 2016 Site-directed mutagenesis Biochemistry, general Chemistry Computer-aided rational design Thermostability Lipoxygenase Biotechnology Zhang, Chong oth Wang, Shuicheng oth Lu, Fengxia oth Lu, Zhaoxin oth Enthalten in Applied biochemistry and biotechnology / A New York, NY : Springer, 1994 178(2016), 7, Seite 1339-1350 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:178 year:2016 number:7 pages:1339-1350 http://dx.doi.org/10.1007/s12010-015-1950-2 Volltext http://www.ncbi.nlm.nih.gov/pubmed/26686337 http://search.proquest.com/docview/1787036237 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_4012 42.00 AVZ AR 178 2016 7 1339-1350 |
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10.1007/s12010-015-1950-2 doi PQ20160610 (DE-627)OLC1975144333 (DE-599)GBVOLC1975144333 (PRQ)p1420-a740b4ac53531622c94cb6d3b9762919d5b2a31de5e4b5dc8ea1a0a7876389590 (KEY)0068751020160000178000701339enhancedthermostabilityoflipoxygenasefromanabaenas DE-627 ger DE-627 rakwb eng 570 540 660 DNB 42.00 bkl Diao, Hanwen verfasserin aut Enhanced Thermostability of Lipoxygenase from Anabaena sp. PCC 7120 by Site-Directed Mutagenesis Based on Computer-Aided Rational Design 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Lipoxygenase from Anabaena sp. PCC 7120 (Ana-LOX) was thermally unstable. So, improving the thermostability of the enzyme was quite essential. The target site of Ana-LOX selected for site-directed mutagenesis was based on computer-aided rational design. The thermostability and specific activity of Ana-LOX were improved with replacing valine with alanine at the target site 421 and the site 40. Compared to the wild-type enzyme which has a half-life (T 1/2) of inactivation of 3.8 min at 50 °C, the T 1/2 of mutant enzymes with V421A and V40A substitution increased to 4.4 and 7.0 min, respectively. The double mutant V421A/V40A showed a synergistic effect with a T 1/2 value of 8.3 min, resulting in a 1.18-fold improvement compared to the original Ana-LOX. V421A, V40A, and V421A/V40A also obtained 4.83, 41.58, and 80.07 % increase in specific activity, respectively. This study provides useful theoretical reference for enzyme molecular modification and computer-aided rational design. Nutzungsrecht: © Springer Science+Business Media New York 2016 Site-directed mutagenesis Biochemistry, general Chemistry Computer-aided rational design Thermostability Lipoxygenase Biotechnology Zhang, Chong oth Wang, Shuicheng oth Lu, Fengxia oth Lu, Zhaoxin oth Enthalten in Applied biochemistry and biotechnology / A New York, NY : Springer, 1994 178(2016), 7, Seite 1339-1350 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:178 year:2016 number:7 pages:1339-1350 http://dx.doi.org/10.1007/s12010-015-1950-2 Volltext http://www.ncbi.nlm.nih.gov/pubmed/26686337 http://search.proquest.com/docview/1787036237 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_4012 42.00 AVZ AR 178 2016 7 1339-1350 |
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10.1007/s12010-015-1950-2 doi PQ20160610 (DE-627)OLC1975144333 (DE-599)GBVOLC1975144333 (PRQ)p1420-a740b4ac53531622c94cb6d3b9762919d5b2a31de5e4b5dc8ea1a0a7876389590 (KEY)0068751020160000178000701339enhancedthermostabilityoflipoxygenasefromanabaenas DE-627 ger DE-627 rakwb eng 570 540 660 DNB 42.00 bkl Diao, Hanwen verfasserin aut Enhanced Thermostability of Lipoxygenase from Anabaena sp. PCC 7120 by Site-Directed Mutagenesis Based on Computer-Aided Rational Design 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Lipoxygenase from Anabaena sp. PCC 7120 (Ana-LOX) was thermally unstable. So, improving the thermostability of the enzyme was quite essential. The target site of Ana-LOX selected for site-directed mutagenesis was based on computer-aided rational design. The thermostability and specific activity of Ana-LOX were improved with replacing valine with alanine at the target site 421 and the site 40. Compared to the wild-type enzyme which has a half-life (T 1/2) of inactivation of 3.8 min at 50 °C, the T 1/2 of mutant enzymes with V421A and V40A substitution increased to 4.4 and 7.0 min, respectively. The double mutant V421A/V40A showed a synergistic effect with a T 1/2 value of 8.3 min, resulting in a 1.18-fold improvement compared to the original Ana-LOX. V421A, V40A, and V421A/V40A also obtained 4.83, 41.58, and 80.07 % increase in specific activity, respectively. This study provides useful theoretical reference for enzyme molecular modification and computer-aided rational design. Nutzungsrecht: © Springer Science+Business Media New York 2016 Site-directed mutagenesis Biochemistry, general Chemistry Computer-aided rational design Thermostability Lipoxygenase Biotechnology Zhang, Chong oth Wang, Shuicheng oth Lu, Fengxia oth Lu, Zhaoxin oth Enthalten in Applied biochemistry and biotechnology / A New York, NY : Springer, 1994 178(2016), 7, Seite 1339-1350 (DE-627)182278573 (DE-600)1193054-8 (DE-576)043085105 0273-2289 nnns volume:178 year:2016 number:7 pages:1339-1350 http://dx.doi.org/10.1007/s12010-015-1950-2 Volltext http://www.ncbi.nlm.nih.gov/pubmed/26686337 http://search.proquest.com/docview/1787036237 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 GBV_ILN_4012 42.00 AVZ AR 178 2016 7 1339-1350 |
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PCC 7120 by Site-Directed Mutagenesis Based on Computer-Aided Rational Design</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2016</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Lipoxygenase from Anabaena sp. PCC 7120 (Ana-LOX) was thermally unstable. So, improving the thermostability of the enzyme was quite essential. The target site of Ana-LOX selected for site-directed mutagenesis was based on computer-aided rational design. The thermostability and specific activity of Ana-LOX were improved with replacing valine with alanine at the target site 421 and the site 40. Compared to the wild-type enzyme which has a half-life (T 1/2) of inactivation of 3.8 min at 50 °C, the T 1/2 of mutant enzymes with V421A and V40A substitution increased to 4.4 and 7.0 min, respectively. The double mutant V421A/V40A showed a synergistic effect with a T 1/2 value of 8.3 min, resulting in a 1.18-fold improvement compared to the original Ana-LOX. V421A, V40A, and V421A/V40A also obtained 4.83, 41.58, and 80.07 % increase in specific activity, respectively. 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enhanced thermostability of lipoxygenase from anabaena sp. pcc 7120 by site-directed mutagenesis based on computer-aided rational design |
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Enhanced Thermostability of Lipoxygenase from Anabaena sp. PCC 7120 by Site-Directed Mutagenesis Based on Computer-Aided Rational Design |
| abstract |
Lipoxygenase from Anabaena sp. PCC 7120 (Ana-LOX) was thermally unstable. So, improving the thermostability of the enzyme was quite essential. The target site of Ana-LOX selected for site-directed mutagenesis was based on computer-aided rational design. The thermostability and specific activity of Ana-LOX were improved with replacing valine with alanine at the target site 421 and the site 40. Compared to the wild-type enzyme which has a half-life (T 1/2) of inactivation of 3.8 min at 50 °C, the T 1/2 of mutant enzymes with V421A and V40A substitution increased to 4.4 and 7.0 min, respectively. The double mutant V421A/V40A showed a synergistic effect with a T 1/2 value of 8.3 min, resulting in a 1.18-fold improvement compared to the original Ana-LOX. V421A, V40A, and V421A/V40A also obtained 4.83, 41.58, and 80.07 % increase in specific activity, respectively. This study provides useful theoretical reference for enzyme molecular modification and computer-aided rational design. |
| abstractGer |
Lipoxygenase from Anabaena sp. PCC 7120 (Ana-LOX) was thermally unstable. So, improving the thermostability of the enzyme was quite essential. The target site of Ana-LOX selected for site-directed mutagenesis was based on computer-aided rational design. The thermostability and specific activity of Ana-LOX were improved with replacing valine with alanine at the target site 421 and the site 40. Compared to the wild-type enzyme which has a half-life (T 1/2) of inactivation of 3.8 min at 50 °C, the T 1/2 of mutant enzymes with V421A and V40A substitution increased to 4.4 and 7.0 min, respectively. The double mutant V421A/V40A showed a synergistic effect with a T 1/2 value of 8.3 min, resulting in a 1.18-fold improvement compared to the original Ana-LOX. V421A, V40A, and V421A/V40A also obtained 4.83, 41.58, and 80.07 % increase in specific activity, respectively. This study provides useful theoretical reference for enzyme molecular modification and computer-aided rational design. |
| abstract_unstemmed |
Lipoxygenase from Anabaena sp. PCC 7120 (Ana-LOX) was thermally unstable. So, improving the thermostability of the enzyme was quite essential. The target site of Ana-LOX selected for site-directed mutagenesis was based on computer-aided rational design. The thermostability and specific activity of Ana-LOX were improved with replacing valine with alanine at the target site 421 and the site 40. Compared to the wild-type enzyme which has a half-life (T 1/2) of inactivation of 3.8 min at 50 °C, the T 1/2 of mutant enzymes with V421A and V40A substitution increased to 4.4 and 7.0 min, respectively. The double mutant V421A/V40A showed a synergistic effect with a T 1/2 value of 8.3 min, resulting in a 1.18-fold improvement compared to the original Ana-LOX. V421A, V40A, and V421A/V40A also obtained 4.83, 41.58, and 80.07 % increase in specific activity, respectively. This study provides useful theoretical reference for enzyme molecular modification and computer-aided rational design. |
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Enhanced Thermostability of Lipoxygenase from Anabaena sp. PCC 7120 by Site-Directed Mutagenesis Based on Computer-Aided Rational Design |
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