Rhodococcus rhodochrous PA‐34硝化酶基因的克隆与测序

T. Bhalla, M. Aoshima, S. Misawa, R. Muramatsu, K. Furuhashi
{"title":"Rhodococcus rhodochrous PA‐34硝化酶基因的克隆与测序","authors":"T. Bhalla, M. Aoshima, S. Misawa, R. Muramatsu, K. Furuhashi","doi":"10.1002/ABIO.370150308","DOIUrl":null,"url":null,"abstract":"The nitrilase of Rhodococcus rhodochrous PA-34 catalyzes the production of optically active amino acids from aminonitriles. The amino acid sequence of the NH 2 terminus of the purified nitrilase was determined for the preparation of a synthetic oligonucleotide as a southern hybridization probe. A 9.5-kbp Pst I-fragment, which hybridized with the oligonucleotide probe, was isolated from R. rhodochrous PA-34 genomic libraries constructed in pUC 19. Nucleotide sequence analysis revealed that the nitrilase gene codes for a putative polypeptide of 380 amino acids which correspond to a relative molecular weight of 41,723.","PeriodicalId":7037,"journal":{"name":"Acta Biotechnologica","volume":"7 1","pages":"297-306"},"PeriodicalIF":0.0000,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"17","resultStr":"{\"title\":\"The molecular cloning and sequencing of the nitrilase gene of Rhodococcus rhodochrous PA‐34\",\"authors\":\"T. Bhalla, M. Aoshima, S. Misawa, R. Muramatsu, K. Furuhashi\",\"doi\":\"10.1002/ABIO.370150308\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The nitrilase of Rhodococcus rhodochrous PA-34 catalyzes the production of optically active amino acids from aminonitriles. The amino acid sequence of the NH 2 terminus of the purified nitrilase was determined for the preparation of a synthetic oligonucleotide as a southern hybridization probe. A 9.5-kbp Pst I-fragment, which hybridized with the oligonucleotide probe, was isolated from R. rhodochrous PA-34 genomic libraries constructed in pUC 19. Nucleotide sequence analysis revealed that the nitrilase gene codes for a putative polypeptide of 380 amino acids which correspond to a relative molecular weight of 41,723.\",\"PeriodicalId\":7037,\"journal\":{\"name\":\"Acta Biotechnologica\",\"volume\":\"7 1\",\"pages\":\"297-306\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1900-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"17\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Acta Biotechnologica\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1002/ABIO.370150308\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta Biotechnologica","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1002/ABIO.370150308","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 17

摘要

Rhodococcus rhodochrous PA-34的腈酶催化氨基腈生成光学活性氨基酸。测定纯化的腈酶nh2末端的氨基酸序列,制备合成的寡核苷酸作为南杂交探针。从pUC 19构建的R. rhodochrous PA-34基因组文库中分离到一个9.5 kbp的Pst - 1片段,并与寡核苷酸探针杂交。核苷酸序列分析表明,该基因编码的推测多肽有380个氨基酸,相对分子量为41723。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
The molecular cloning and sequencing of the nitrilase gene of Rhodococcus rhodochrous PA‐34
The nitrilase of Rhodococcus rhodochrous PA-34 catalyzes the production of optically active amino acids from aminonitriles. The amino acid sequence of the NH 2 terminus of the purified nitrilase was determined for the preparation of a synthetic oligonucleotide as a southern hybridization probe. A 9.5-kbp Pst I-fragment, which hybridized with the oligonucleotide probe, was isolated from R. rhodochrous PA-34 genomic libraries constructed in pUC 19. Nucleotide sequence analysis revealed that the nitrilase gene codes for a putative polypeptide of 380 amino acids which correspond to a relative molecular weight of 41,723.
求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
The effect of rhizodeposition from helophytes on bacterial degradation of phenolic compounds Exposure to xenobiotics deeply affects the bacteriocenosis in the rhizosphere of helophytes Production of Indole Acetic Acid in Culture by a Rhizobium Species from the Root Nodules of a Monocotyledonous Tree, Roystonea regia Chemical sensors and biosensors for medical and biological applications. Chichester, New York, Weinheim, Brisbane, Singapore, Toronto: John Wiley & Sons XII + 413 pages, 82 figures, 41 tables; DM 198.00, ISBN 3-527-28855-4 Flow cytometric monitoring of Rhodococcus erythropolis and Ochrobactrum anthropi in a mixed culture
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1