Structural and Functional Analysis of the Only Two Pyridoxal 5′-Phosphate-Dependent Fold Type IV Transaminases in <i>Bacillus altitudinis</i> W3
Aminotransferases are employed as industrial biocatalysts to produce chiral amines with high enantioselectivity and yield. BpTA-1 and BpTA-2 are the only two pyridoxal 5′-phosphate-dependent fold type IV transaminase enzymes in <i>Bacillus altitudinis</i> W3. Herein, we compared the stru...
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MDPI AG
2020-11-01
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| Series: | Catalysts |
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| author | Lixin Zhai Zihao Xie Qiaopeng Tian Zhengbing Guan Yujie Cai Xiangru Liao |
| author_facet | Lixin Zhai Zihao Xie Qiaopeng Tian Zhengbing Guan Yujie Cai Xiangru Liao |
| author_sort | Lixin Zhai |
| collection | DOAJ |
| description | Aminotransferases are employed as industrial biocatalysts to produce chiral amines with high enantioselectivity and yield. BpTA-1 and BpTA-2 are the only two pyridoxal 5′-phosphate-dependent fold type IV transaminase enzymes in <i>Bacillus altitudinis</i> W3. Herein, we compared the structures and biochemical characteristics of BpTA-1 and BpTA-2 using bioinformatic analysis, circular dichroism spectroscopy, atomic force microscopy and other approaches. BpTA-1 and BpTA-2 are similar overall; both form homodimers and utilize a catalytic lysine. However, there are distinct differences in the substrate cofactor-binding pocket, molecular weight and the proportion of the secondary structure. Both enzymes have the same stereoselectivity but different enzymatic properties. BpTA-2 is more active under partial alkaline and ambient temperature conditions and BpTA-1 is more sensitive to pH and temperature. BpTA-2 as novel enzyme not only fills the building blocks of transaminase but also has broader industrial application potential for (<i>R</i>)-α-phenethylamines than BpTA-1. Structure-function relationships were explored to assess similarities and differences. The findings lay the foundation for modifying these enzymes via protein engineering to enhance their industrial application potential. |
| first_indexed | 2024-03-10T14:54:28Z |
| format | Article |
| id | doaj.art-069324815f8f44b596cb54a83f41797c |
| institution | Directory Open Access Journal |
| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-10T14:54:28Z |
| publishDate | 2020-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Catalysts |
| spelling | doaj.art-069324815f8f44b596cb54a83f41797c2023-11-20T20:42:19ZengMDPI AGCatalysts2073-43442020-11-011011130810.3390/catal10111308Structural and Functional Analysis of the Only Two Pyridoxal 5′-Phosphate-Dependent Fold Type IV Transaminases in <i>Bacillus altitudinis</i> W3Lixin Zhai0Zihao Xie1Qiaopeng Tian2Zhengbing Guan3Yujie Cai4Xiangru Liao5Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, ChinaKey Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, ChinaKey Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, ChinaKey Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, ChinaKey Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, ChinaKey Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, ChinaAminotransferases are employed as industrial biocatalysts to produce chiral amines with high enantioselectivity and yield. BpTA-1 and BpTA-2 are the only two pyridoxal 5′-phosphate-dependent fold type IV transaminase enzymes in <i>Bacillus altitudinis</i> W3. Herein, we compared the structures and biochemical characteristics of BpTA-1 and BpTA-2 using bioinformatic analysis, circular dichroism spectroscopy, atomic force microscopy and other approaches. BpTA-1 and BpTA-2 are similar overall; both form homodimers and utilize a catalytic lysine. However, there are distinct differences in the substrate cofactor-binding pocket, molecular weight and the proportion of the secondary structure. Both enzymes have the same stereoselectivity but different enzymatic properties. BpTA-2 is more active under partial alkaline and ambient temperature conditions and BpTA-1 is more sensitive to pH and temperature. BpTA-2 as novel enzyme not only fills the building blocks of transaminase but also has broader industrial application potential for (<i>R</i>)-α-phenethylamines than BpTA-1. Structure-function relationships were explored to assess similarities and differences. The findings lay the foundation for modifying these enzymes via protein engineering to enhance their industrial application potential.https://www.mdpi.com/2073-4344/10/11/1308aminotransferasepyridoxal 5′-phosphatesecondary structureconserved domainAFMcatalytic activity |
| spellingShingle | Lixin Zhai Zihao Xie Qiaopeng Tian Zhengbing Guan Yujie Cai Xiangru Liao Structural and Functional Analysis of the Only Two Pyridoxal 5′-Phosphate-Dependent Fold Type IV Transaminases in <i>Bacillus altitudinis</i> W3 Catalysts aminotransferase pyridoxal 5′-phosphate secondary structure conserved domain AFM catalytic activity |
| title | Structural and Functional Analysis of the Only Two Pyridoxal 5′-Phosphate-Dependent Fold Type IV Transaminases in <i>Bacillus altitudinis</i> W3 |
| title_full | Structural and Functional Analysis of the Only Two Pyridoxal 5′-Phosphate-Dependent Fold Type IV Transaminases in <i>Bacillus altitudinis</i> W3 |
| title_fullStr | Structural and Functional Analysis of the Only Two Pyridoxal 5′-Phosphate-Dependent Fold Type IV Transaminases in <i>Bacillus altitudinis</i> W3 |
| title_full_unstemmed | Structural and Functional Analysis of the Only Two Pyridoxal 5′-Phosphate-Dependent Fold Type IV Transaminases in <i>Bacillus altitudinis</i> W3 |
| title_short | Structural and Functional Analysis of the Only Two Pyridoxal 5′-Phosphate-Dependent Fold Type IV Transaminases in <i>Bacillus altitudinis</i> W3 |
| title_sort | structural and functional analysis of the only two pyridoxal 5 phosphate dependent fold type iv transaminases in i bacillus altitudinis i w3 |
| topic | aminotransferase pyridoxal 5′-phosphate secondary structure conserved domain AFM catalytic activity |
| url | https://www.mdpi.com/2073-4344/10/11/1308 |
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