Substrate profile of an omega-transaminase from Burkholderia vietnamiensis and its potential for the production of optically pure amines and unnatural amino acids
文献类型：期刊论文
| 作者 | Jiang, Jinju1,2,3; Chen, Xi1,2; Feng, Jinhui1,2; Wu, Qiaqing1,2; Zhu, Dunming1,2 |
| 刊名 | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
 |
| 出版日期 | 2014-02-01 |
| 卷号 | 100页码:32-39 |
| 关键词 | Biocatalysis omega-Transaminase Chiral amine Unnatural amino acid beta-Keto ester |
| 英文摘要 | A new (S)-enantioselective omega-transaminase (omega-TA) gene from Burkholderia vietnamiensis G4 was functionally expressed in Escherichia coli BL21 (DE3), and the purified recombinant N-terminal His-tagged (omega-TA (HBV-omega-TA) had a dimeric structure with optimum pH and temperature of 8.4 and 40 degrees C, respectively. The enzyme showed higher activities toward aromatic amines than aliphatic amines and (S)-1-methylbenzylamine ((S)-alpha-MBA) was the most active amino donor. For amino acceptor, keto acids, keto esters and aldehydes were more reactive than ketones with pyruvate ethyl ester being most active. Several chiral amines and unnatural amino acids or esters were synthesized using HBV-w-TA as the catalyst and isopropylamine or (S)-alpha-MBA as amino donor. Notably, HBV-omega-TA catalyzed the amino transfer to beta-keto esters to give optically pure beta-amino acid esters. In addition, glyoxylate was used as amino acceptor for the first time in the kinetic resolution of racemic amines and optically pure amines, such as (R)-1-methylbenzylamine, (R)-1-phenylpropylamine, (R)-2-amino-4-phenylbutane and (R)-1-aminotetraline, were obtained. (C) 2013 Elsevier B.V. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences |
| 类目[WOS] | Biochemistry & Molecular Biology ; Chemistry, Physical |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Chemistry |
| 关键词[WOS] | ASYMMETRIC-SYNTHESIS ; PYRUVATE TRANSAMINASE ; KINETIC RESOLUTION ; ENZYME CONTROLS ; CHIRAL AMINES ; AMINOTRANSFERASE ; PEPTIDOMIMETICS ; SPECIFICITY ; CLONING ; DESIGN |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000331027900005 |
| 源URL | [http://124.16.173.210/handle/834782/1377]  |
| 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 300308, Peoples R China 2.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Tianjin Engn Ctr Biocatalyt Technol, Tianjin 300308, Peoples R China 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Jiang, Jinju,Chen, Xi,Feng, Jinhui,et al. Substrate profile of an omega-transaminase from Burkholderia vietnamiensis and its potential for the production of optically pure amines and unnatural amino acids[J]. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,2014,100:32-39. |
| APA | Jiang, Jinju,Chen, Xi,Feng, Jinhui,Wu, Qiaqing,&Zhu, Dunming.(2014).Substrate profile of an omega-transaminase from Burkholderia vietnamiensis and its potential for the production of optically pure amines and unnatural amino acids.JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,100,32-39. |
| MLA | Jiang, Jinju,et al."Substrate profile of an omega-transaminase from Burkholderia vietnamiensis and its potential for the production of optically pure amines and unnatural amino acids".JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 100(2014):32-39. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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