Substrate profiling of cyclohexylamine oxidase and its mutants reveals new biocatalytic potential in deracemization of racemic amines
文献类型：期刊论文
| 作者 | Li, Guangyue1; Ren, Jie1; Iwaki, Hiroaki5; Zhang, Dalong1; Hasegawa, Yoshie5; Wu, Qiaqing1; Feng, Jinhui1; Lau, Peter C. K.2,3,4; Zhu, Dunming1 |
| 刊名 | APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
 |
| 出版日期 | 2014-02-01 |
| 卷号 | 98期号:4页码:1681-1689 |
| 关键词 | Biocatalysis Monoamine oxidase Site mutagenesis Chiral amines Deracemization Norsertraline |
| 英文摘要 | A cyclohexylamine oxidase (CHAO) of bacterial origin was previously shown to be a potentially useful catalyst in the deracemization of racemic primary amines. To further explore the properties and application of this enzyme, five single-amino acid substitution mutants (L199A, M226A, Y321A, Y321F, and L353M) were created based on superimposition of the tertiary structure of CHAO and the monoamine oxidase (MAO) B homolog. The substrate specificity of the purified wild-type and five mutant enzymes were examined towards 38 structurally diverse amines. All the enzymes exhibited better activity for primary amines than secondary and tertiary amines and in general exhibited high stereoselectivity. Among the mutant enzymes, M226A displayed an enhanced activity (5-400 %) towards most substrates, and L353M showed 7-445 % higher activity towards primary aliphatic amines with cycloalkane or aromatic moieties. Kinetic parameters revealed that both Y321 mutants showed higher catalytic efficiency towards cyclooctanamine, whereas the wild-type CHAO (wt CHAO) was most efficient towards cyclohexylamine. The wt CHAO or variant L353M in combination with a borane-ammonia complex as reducing agent was applied to the deracemization of 1-aminotetraline to give the (R)-enantiomer, a precursor of an antidepressant drug Norsertrali ne, in good yield (73-76 %), demonstrating their application potential in chiral amine synthesis. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biotechnology & Applied Microbiology |
| 研究领域[WOS] | Biotechnology & Applied Microbiology |
| 关键词[WOS] | MONOAMINE-OXIDASE ; KINETIC RESOLUTION ; CHIRAL AMINES ; DESYMMETRIZATION ; MANUFACTURE ; EFFICIENT ; ACID |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000332106000020 |
| 源URL | [http://124.16.173.210/handle/834782/1415]  |
| 专题 | 天津工业生物技术研究所_生物催化与绿色化工 朱敦明_期刊论文 |
| 作者单位 | 1.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Natl Engn Lab Ind Enzymes, Tianjin Airport Econ Area, Tianjin 300308, Peoples R China 2.Natl Res Council Canada, Montreal, PQ H4P 2R2, Canada 3.McGill Univ, Dept Chem & Microbiol Immunol, Montreal, PQ, Canada 4.FQRNT Ctr Green Chem & Catalysis, Montreal, PQ, Canada 5.Kansai Univ, Dept Life Sci Biotechnol & ORDIST, Suita, Osaka 5648680, Japan |
| 推荐引用方式 GB/T 7714 | Li, Guangyue,Ren, Jie,Iwaki, Hiroaki,et al. Substrate profiling of cyclohexylamine oxidase and its mutants reveals new biocatalytic potential in deracemization of racemic amines[J]. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY,2014,98(4):1681-1689. |
| APA | Li, Guangyue.,Ren, Jie.,Iwaki, Hiroaki.,Zhang, Dalong.,Hasegawa, Yoshie.,...&Zhu, Dunming.(2014).Substrate profiling of cyclohexylamine oxidase and its mutants reveals new biocatalytic potential in deracemization of racemic amines.APPLIED MICROBIOLOGY AND BIOTECHNOLOGY,98(4),1681-1689. |
| MLA | Li, Guangyue,et al."Substrate profiling of cyclohexylamine oxidase and its mutants reveals new biocatalytic potential in deracemization of racemic amines".APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 98.4(2014):1681-1689. |
入库方式： OAI收割
来源：天津工业生物技术研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。