Old yellow enzymes: structures and structure-guided engineering for stereocomplementary bioreduction
Abstract Since the first discovery of old yellow enzyme 1 (OYE1) from Saccharomyces pastorianus in 1932, biocatalytic asymmetric reduction of activated alkenes by OYEs has become a valuable reaction in organic synthesis. To access stereocomplementary C=C-bond bioreduction, the mining of novel OYEs a...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Shi, Qinghua [verfasserIn] Wang, Huibin [verfasserIn] Liu, Junling [verfasserIn] Li, Shang [verfasserIn] Guo, Jiyang [verfasserIn] Li, Hengyu [verfasserIn] Jia, Xian [verfasserIn] Huo, Hua [verfasserIn] Zheng, Zhendong [verfasserIn] You, Song [verfasserIn] Qin, Bin [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2020 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Berlin : Springer, 1975, 104(2020), 19 vom: 24. Aug., Seite 8155-8170 |
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| Übergeordnetes Werk: |
volume:104 ; year:2020 ; number:19 ; day:24 ; month:08 ; pages:8155-8170 |
| Links: |
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| DOI / URN: |
10.1007/s00253-020-10845-z |
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| Katalog-ID: |
SPR040857816 |
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| 520 | |a Abstract Since the first discovery of old yellow enzyme 1 (OYE1) from Saccharomyces pastorianus in 1932, biocatalytic asymmetric reduction of activated alkenes by OYEs has become a valuable reaction in organic synthesis. To access stereocomplementary C=C-bond bioreduction, the mining of novel OYEs and especially the protein engineering of existing OYEs have been performed, which successfully achieved the stereocomplementary reduction in several cases and further raise the potential of applications. In this review, we analyzed the structures, active sites, and substrate recognition of OYEs, which are the bases for their substrate specificity and stereospecificity. Sequence similarity network of OYEs superfamily was also constructed to investigate the scope of characterized OYEs. The structure-guided engineering to switch the stereoselectivity of OYEs and thus access stereocomplementary bioreduction over the last decade (2009–2020) was then reviewed and discussed, which might give new insights into the mining and engineering of related biocatalysts. Key points • The sequence similarity network of OYEs superfamily was constructed and annotated. • The structures and active sites of OYEs from different classes were compared. • “Left/right” binding mode was used to explain the stereopreferences of OYEs. • Structure-guided engineering of OYEs to switch their stereoselectivity was reviewed. | ||
| 650 | 4 | |a Biocatalysis |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Old yellow enzymes |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Protein engineering |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Biocatalytic reduction |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Stereopreference switch |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Wang, Huibin |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Junling |e verfasserin |4 aut | |
| 700 | 1 | |a Li, Shang |e verfasserin |4 aut | |
| 700 | 1 | |a Guo, Jiyang |e verfasserin |4 aut | |
| 700 | 1 | |a Li, Hengyu |e verfasserin |4 aut | |
| 700 | 1 | |a Jia, Xian |e verfasserin |4 aut | |
| 700 | 1 | |a Huo, Hua |e verfasserin |4 aut | |
| 700 | 1 | |a Zheng, Zhendong |e verfasserin |4 aut | |
| 700 | 1 | |a You, Song |e verfasserin |4 aut | |
| 700 | 1 | |a Qin, Bin |e verfasserin |4 aut | |
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10.1007/s00253-020-10845-z doi (DE-627)SPR040857816 (SPR)s00253-020-10845-z-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Shi, Qinghua verfasserin aut Old yellow enzymes: structures and structure-guided engineering for stereocomplementary bioreduction 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Since the first discovery of old yellow enzyme 1 (OYE1) from Saccharomyces pastorianus in 1932, biocatalytic asymmetric reduction of activated alkenes by OYEs has become a valuable reaction in organic synthesis. To access stereocomplementary C=C-bond bioreduction, the mining of novel OYEs and especially the protein engineering of existing OYEs have been performed, which successfully achieved the stereocomplementary reduction in several cases and further raise the potential of applications. In this review, we analyzed the structures, active sites, and substrate recognition of OYEs, which are the bases for their substrate specificity and stereospecificity. Sequence similarity network of OYEs superfamily was also constructed to investigate the scope of characterized OYEs. The structure-guided engineering to switch the stereoselectivity of OYEs and thus access stereocomplementary bioreduction over the last decade (2009–2020) was then reviewed and discussed, which might give new insights into the mining and engineering of related biocatalysts. Key points • The sequence similarity network of OYEs superfamily was constructed and annotated. • The structures and active sites of OYEs from different classes were compared. • “Left/right” binding mode was used to explain the stereopreferences of OYEs. • Structure-guided engineering of OYEs to switch their stereoselectivity was reviewed. Biocatalysis (dpeaa)DE-He213 Old yellow enzymes (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Biocatalytic reduction (dpeaa)DE-He213 Stereopreference switch (dpeaa)DE-He213 Wang, Huibin verfasserin aut Liu, Junling verfasserin aut Li, Shang verfasserin aut Guo, Jiyang verfasserin aut Li, Hengyu verfasserin aut Jia, Xian verfasserin aut Huo, Hua verfasserin aut Zheng, Zhendong verfasserin aut You, Song verfasserin aut Qin, Bin verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 104(2020), 19 vom: 24. Aug., Seite 8155-8170 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:104 year:2020 number:19 day:24 month:08 pages:8155-8170 https://dx.doi.org/10.1007/s00253-020-10845-z lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 104 2020 19 24 08 8155-8170 |
| spelling |
10.1007/s00253-020-10845-z doi (DE-627)SPR040857816 (SPR)s00253-020-10845-z-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Shi, Qinghua verfasserin aut Old yellow enzymes: structures and structure-guided engineering for stereocomplementary bioreduction 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Since the first discovery of old yellow enzyme 1 (OYE1) from Saccharomyces pastorianus in 1932, biocatalytic asymmetric reduction of activated alkenes by OYEs has become a valuable reaction in organic synthesis. To access stereocomplementary C=C-bond bioreduction, the mining of novel OYEs and especially the protein engineering of existing OYEs have been performed, which successfully achieved the stereocomplementary reduction in several cases and further raise the potential of applications. In this review, we analyzed the structures, active sites, and substrate recognition of OYEs, which are the bases for their substrate specificity and stereospecificity. Sequence similarity network of OYEs superfamily was also constructed to investigate the scope of characterized OYEs. The structure-guided engineering to switch the stereoselectivity of OYEs and thus access stereocomplementary bioreduction over the last decade (2009–2020) was then reviewed and discussed, which might give new insights into the mining and engineering of related biocatalysts. Key points • The sequence similarity network of OYEs superfamily was constructed and annotated. • The structures and active sites of OYEs from different classes were compared. • “Left/right” binding mode was used to explain the stereopreferences of OYEs. • Structure-guided engineering of OYEs to switch their stereoselectivity was reviewed. Biocatalysis (dpeaa)DE-He213 Old yellow enzymes (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Biocatalytic reduction (dpeaa)DE-He213 Stereopreference switch (dpeaa)DE-He213 Wang, Huibin verfasserin aut Liu, Junling verfasserin aut Li, Shang verfasserin aut Guo, Jiyang verfasserin aut Li, Hengyu verfasserin aut Jia, Xian verfasserin aut Huo, Hua verfasserin aut Zheng, Zhendong verfasserin aut You, Song verfasserin aut Qin, Bin verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 104(2020), 19 vom: 24. Aug., Seite 8155-8170 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:104 year:2020 number:19 day:24 month:08 pages:8155-8170 https://dx.doi.org/10.1007/s00253-020-10845-z lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 104 2020 19 24 08 8155-8170 |
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10.1007/s00253-020-10845-z doi (DE-627)SPR040857816 (SPR)s00253-020-10845-z-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Shi, Qinghua verfasserin aut Old yellow enzymes: structures and structure-guided engineering for stereocomplementary bioreduction 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Since the first discovery of old yellow enzyme 1 (OYE1) from Saccharomyces pastorianus in 1932, biocatalytic asymmetric reduction of activated alkenes by OYEs has become a valuable reaction in organic synthesis. To access stereocomplementary C=C-bond bioreduction, the mining of novel OYEs and especially the protein engineering of existing OYEs have been performed, which successfully achieved the stereocomplementary reduction in several cases and further raise the potential of applications. In this review, we analyzed the structures, active sites, and substrate recognition of OYEs, which are the bases for their substrate specificity and stereospecificity. Sequence similarity network of OYEs superfamily was also constructed to investigate the scope of characterized OYEs. The structure-guided engineering to switch the stereoselectivity of OYEs and thus access stereocomplementary bioreduction over the last decade (2009–2020) was then reviewed and discussed, which might give new insights into the mining and engineering of related biocatalysts. Key points • The sequence similarity network of OYEs superfamily was constructed and annotated. • The structures and active sites of OYEs from different classes were compared. • “Left/right” binding mode was used to explain the stereopreferences of OYEs. • Structure-guided engineering of OYEs to switch their stereoselectivity was reviewed. Biocatalysis (dpeaa)DE-He213 Old yellow enzymes (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Biocatalytic reduction (dpeaa)DE-He213 Stereopreference switch (dpeaa)DE-He213 Wang, Huibin verfasserin aut Liu, Junling verfasserin aut Li, Shang verfasserin aut Guo, Jiyang verfasserin aut Li, Hengyu verfasserin aut Jia, Xian verfasserin aut Huo, Hua verfasserin aut Zheng, Zhendong verfasserin aut You, Song verfasserin aut Qin, Bin verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 104(2020), 19 vom: 24. Aug., Seite 8155-8170 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:104 year:2020 number:19 day:24 month:08 pages:8155-8170 https://dx.doi.org/10.1007/s00253-020-10845-z lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 104 2020 19 24 08 8155-8170 |
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10.1007/s00253-020-10845-z doi (DE-627)SPR040857816 (SPR)s00253-020-10845-z-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Shi, Qinghua verfasserin aut Old yellow enzymes: structures and structure-guided engineering for stereocomplementary bioreduction 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Since the first discovery of old yellow enzyme 1 (OYE1) from Saccharomyces pastorianus in 1932, biocatalytic asymmetric reduction of activated alkenes by OYEs has become a valuable reaction in organic synthesis. To access stereocomplementary C=C-bond bioreduction, the mining of novel OYEs and especially the protein engineering of existing OYEs have been performed, which successfully achieved the stereocomplementary reduction in several cases and further raise the potential of applications. In this review, we analyzed the structures, active sites, and substrate recognition of OYEs, which are the bases for their substrate specificity and stereospecificity. Sequence similarity network of OYEs superfamily was also constructed to investigate the scope of characterized OYEs. The structure-guided engineering to switch the stereoselectivity of OYEs and thus access stereocomplementary bioreduction over the last decade (2009–2020) was then reviewed and discussed, which might give new insights into the mining and engineering of related biocatalysts. Key points • The sequence similarity network of OYEs superfamily was constructed and annotated. • The structures and active sites of OYEs from different classes were compared. • “Left/right” binding mode was used to explain the stereopreferences of OYEs. • Structure-guided engineering of OYEs to switch their stereoselectivity was reviewed. Biocatalysis (dpeaa)DE-He213 Old yellow enzymes (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Biocatalytic reduction (dpeaa)DE-He213 Stereopreference switch (dpeaa)DE-He213 Wang, Huibin verfasserin aut Liu, Junling verfasserin aut Li, Shang verfasserin aut Guo, Jiyang verfasserin aut Li, Hengyu verfasserin aut Jia, Xian verfasserin aut Huo, Hua verfasserin aut Zheng, Zhendong verfasserin aut You, Song verfasserin aut Qin, Bin verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 104(2020), 19 vom: 24. Aug., Seite 8155-8170 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:104 year:2020 number:19 day:24 month:08 pages:8155-8170 https://dx.doi.org/10.1007/s00253-020-10845-z lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 104 2020 19 24 08 8155-8170 |
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10.1007/s00253-020-10845-z doi (DE-627)SPR040857816 (SPR)s00253-020-10845-z-e DE-627 ger DE-627 rakwb eng 570 ASE 58.30 bkl 42.30 bkl Shi, Qinghua verfasserin aut Old yellow enzymes: structures and structure-guided engineering for stereocomplementary bioreduction 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Since the first discovery of old yellow enzyme 1 (OYE1) from Saccharomyces pastorianus in 1932, biocatalytic asymmetric reduction of activated alkenes by OYEs has become a valuable reaction in organic synthesis. To access stereocomplementary C=C-bond bioreduction, the mining of novel OYEs and especially the protein engineering of existing OYEs have been performed, which successfully achieved the stereocomplementary reduction in several cases and further raise the potential of applications. In this review, we analyzed the structures, active sites, and substrate recognition of OYEs, which are the bases for their substrate specificity and stereospecificity. Sequence similarity network of OYEs superfamily was also constructed to investigate the scope of characterized OYEs. The structure-guided engineering to switch the stereoselectivity of OYEs and thus access stereocomplementary bioreduction over the last decade (2009–2020) was then reviewed and discussed, which might give new insights into the mining and engineering of related biocatalysts. Key points • The sequence similarity network of OYEs superfamily was constructed and annotated. • The structures and active sites of OYEs from different classes were compared. • “Left/right” binding mode was used to explain the stereopreferences of OYEs. • Structure-guided engineering of OYEs to switch their stereoselectivity was reviewed. Biocatalysis (dpeaa)DE-He213 Old yellow enzymes (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Biocatalytic reduction (dpeaa)DE-He213 Stereopreference switch (dpeaa)DE-He213 Wang, Huibin verfasserin aut Liu, Junling verfasserin aut Li, Shang verfasserin aut Guo, Jiyang verfasserin aut Li, Hengyu verfasserin aut Jia, Xian verfasserin aut Huo, Hua verfasserin aut Zheng, Zhendong verfasserin aut You, Song verfasserin aut Qin, Bin verfasserin aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 104(2020), 19 vom: 24. Aug., Seite 8155-8170 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:104 year:2020 number:19 day:24 month:08 pages:8155-8170 https://dx.doi.org/10.1007/s00253-020-10845-z lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2360 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.30 ASE 42.30 ASE AR 104 2020 19 24 08 8155-8170 |
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Enthalten in Applied microbiology and biotechnology 104(2020), 19 vom: 24. Aug., Seite 8155-8170 volume:104 year:2020 number:19 day:24 month:08 pages:8155-8170 |
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Enthalten in Applied microbiology and biotechnology 104(2020), 19 vom: 24. Aug., Seite 8155-8170 volume:104 year:2020 number:19 day:24 month:08 pages:8155-8170 |
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Biocatalysis Old yellow enzymes Protein engineering Biocatalytic reduction Stereopreference switch |
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Shi, Qinghua @@aut@@ Wang, Huibin @@aut@@ Liu, Junling @@aut@@ Li, Shang @@aut@@ Guo, Jiyang @@aut@@ Li, Hengyu @@aut@@ Jia, Xian @@aut@@ Huo, Hua @@aut@@ Zheng, Zhendong @@aut@@ You, Song @@aut@@ Qin, Bin @@aut@@ |
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To access stereocomplementary C=C-bond bioreduction, the mining of novel OYEs and especially the protein engineering of existing OYEs have been performed, which successfully achieved the stereocomplementary reduction in several cases and further raise the potential of applications. In this review, we analyzed the structures, active sites, and substrate recognition of OYEs, which are the bases for their substrate specificity and stereospecificity. Sequence similarity network of OYEs superfamily was also constructed to investigate the scope of characterized OYEs. The structure-guided engineering to switch the stereoselectivity of OYEs and thus access stereocomplementary bioreduction over the last decade (2009–2020) was then reviewed and discussed, which might give new insights into the mining and engineering of related biocatalysts. Key points • The sequence similarity network of OYEs superfamily was constructed and annotated. • The structures and active sites of OYEs from different classes were compared. • “Left/right” binding mode was used to explain the stereopreferences of OYEs. • Structure-guided engineering of OYEs to switch their stereoselectivity was reviewed.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Biocatalysis</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Old yellow enzymes</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein engineering</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Biocatalytic reduction</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Stereopreference switch</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wang, Huibin</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Liu, Junling</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Li, Shang</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Guo, Jiyang</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Li, Hengyu</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Jia, Xian</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Huo, Hua</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zheng, Zhendong</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">You, Song</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Qin, Bin</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Applied microbiology and biotechnology</subfield><subfield code="d">Berlin : Springer, 1975</subfield><subfield code="g">104(2020), 19 vom: 24. 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Shi, Qinghua |
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Shi, Qinghua ddc 570 bkl 58.30 bkl 42.30 misc Biocatalysis misc Old yellow enzymes misc Protein engineering misc Biocatalytic reduction misc Stereopreference switch Old yellow enzymes: structures and structure-guided engineering for stereocomplementary bioreduction |
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570 ASE 58.30 bkl 42.30 bkl Old yellow enzymes: structures and structure-guided engineering for stereocomplementary bioreduction Biocatalysis (dpeaa)DE-He213 Old yellow enzymes (dpeaa)DE-He213 Protein engineering (dpeaa)DE-He213 Biocatalytic reduction (dpeaa)DE-He213 Stereopreference switch (dpeaa)DE-He213 |
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ddc 570 bkl 58.30 bkl 42.30 misc Biocatalysis misc Old yellow enzymes misc Protein engineering misc Biocatalytic reduction misc Stereopreference switch |
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Old yellow enzymes: structures and structure-guided engineering for stereocomplementary bioreduction |
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Shi, Qinghua Wang, Huibin Liu, Junling Li, Shang Guo, Jiyang Li, Hengyu Jia, Xian Huo, Hua Zheng, Zhendong You, Song Qin, Bin |
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old yellow enzymes: structures and structure-guided engineering for stereocomplementary bioreduction |
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Old yellow enzymes: structures and structure-guided engineering for stereocomplementary bioreduction |
| abstract |
Abstract Since the first discovery of old yellow enzyme 1 (OYE1) from Saccharomyces pastorianus in 1932, biocatalytic asymmetric reduction of activated alkenes by OYEs has become a valuable reaction in organic synthesis. To access stereocomplementary C=C-bond bioreduction, the mining of novel OYEs and especially the protein engineering of existing OYEs have been performed, which successfully achieved the stereocomplementary reduction in several cases and further raise the potential of applications. In this review, we analyzed the structures, active sites, and substrate recognition of OYEs, which are the bases for their substrate specificity and stereospecificity. Sequence similarity network of OYEs superfamily was also constructed to investigate the scope of characterized OYEs. The structure-guided engineering to switch the stereoselectivity of OYEs and thus access stereocomplementary bioreduction over the last decade (2009–2020) was then reviewed and discussed, which might give new insights into the mining and engineering of related biocatalysts. Key points • The sequence similarity network of OYEs superfamily was constructed and annotated. • The structures and active sites of OYEs from different classes were compared. • “Left/right” binding mode was used to explain the stereopreferences of OYEs. • Structure-guided engineering of OYEs to switch their stereoselectivity was reviewed. |
| abstractGer |
Abstract Since the first discovery of old yellow enzyme 1 (OYE1) from Saccharomyces pastorianus in 1932, biocatalytic asymmetric reduction of activated alkenes by OYEs has become a valuable reaction in organic synthesis. To access stereocomplementary C=C-bond bioreduction, the mining of novel OYEs and especially the protein engineering of existing OYEs have been performed, which successfully achieved the stereocomplementary reduction in several cases and further raise the potential of applications. In this review, we analyzed the structures, active sites, and substrate recognition of OYEs, which are the bases for their substrate specificity and stereospecificity. Sequence similarity network of OYEs superfamily was also constructed to investigate the scope of characterized OYEs. The structure-guided engineering to switch the stereoselectivity of OYEs and thus access stereocomplementary bioreduction over the last decade (2009–2020) was then reviewed and discussed, which might give new insights into the mining and engineering of related biocatalysts. Key points • The sequence similarity network of OYEs superfamily was constructed and annotated. • The structures and active sites of OYEs from different classes were compared. • “Left/right” binding mode was used to explain the stereopreferences of OYEs. • Structure-guided engineering of OYEs to switch their stereoselectivity was reviewed. |
| abstract_unstemmed |
Abstract Since the first discovery of old yellow enzyme 1 (OYE1) from Saccharomyces pastorianus in 1932, biocatalytic asymmetric reduction of activated alkenes by OYEs has become a valuable reaction in organic synthesis. To access stereocomplementary C=C-bond bioreduction, the mining of novel OYEs and especially the protein engineering of existing OYEs have been performed, which successfully achieved the stereocomplementary reduction in several cases and further raise the potential of applications. In this review, we analyzed the structures, active sites, and substrate recognition of OYEs, which are the bases for their substrate specificity and stereospecificity. Sequence similarity network of OYEs superfamily was also constructed to investigate the scope of characterized OYEs. The structure-guided engineering to switch the stereoselectivity of OYEs and thus access stereocomplementary bioreduction over the last decade (2009–2020) was then reviewed and discussed, which might give new insights into the mining and engineering of related biocatalysts. Key points • The sequence similarity network of OYEs superfamily was constructed and annotated. • The structures and active sites of OYEs from different classes were compared. • “Left/right” binding mode was used to explain the stereopreferences of OYEs. • Structure-guided engineering of OYEs to switch their stereoselectivity was reviewed. |
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Old yellow enzymes: structures and structure-guided engineering for stereocomplementary bioreduction |
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Wang, Huibin Liu, Junling Li, Shang Guo, Jiyang Li, Hengyu Jia, Xian Huo, Hua Zheng, Zhendong You, Song Qin, Bin |
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| score |
7.401232 |