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恶臭假单胞菌酰胺酶基因的克隆与核苷酸序列分析

Cloning and nucleotide sequence of amidase gene from Pseudomonas putida.

作者信息

Wu S, Fallon R D, Payne M S

机构信息

DuPont Central Research and Development, Glasgow Site, Newark, DE 19714-6101, USA.

出版信息

DNA Cell Biol. 1998 Oct;17(10):915-20. doi: 10.1089/dna.1998.17.915.

Abstract

Amidases are a class of enzymes which convert amides to acids and have potential value in the development of commercial bioprocesses for the production of useful chemicals. A gene encoding an amidase in Pseudomonas putida 5B has been cloned, sequenced, and overexpressed in Escherichia coli. An additional open reading frame (P38K) encoding a putative protein of 38 kDa was found immediately upstream of the amidase gene. This work continues our characterization of a P. putida operon, which now appears to include P38K, amidase, and a stereo-specific nitrile hydratase. This characterization underlies continuing efforts in biocatalyst development.

摘要

酰胺酶是一类将酰胺转化为酸的酶,在用于生产有用化学品的商业生物工艺开发中具有潜在价值。恶臭假单胞菌5B中编码酰胺酶的基因已被克隆、测序并在大肠杆菌中过表达。在酰胺酶基因的紧邻上游发现了一个额外的开放阅读框(P38K),其编码一个推定的38 kDa蛋白质。这项工作延续了我们对恶臭假单胞菌操纵子的表征,该操纵子现在似乎包括P38K、酰胺酶和一种立体特异性腈水合酶。这一表征是生物催化剂开发持续努力的基础。

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