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少动假单胞菌中参与β-芳基醚裂解的Cα-脱氢酶基因的表征

Characterization of the C alpha-dehydrogenase gene involved in the cleavage of beta-aryl ether by Pseudomonas paucimobilis.

作者信息

Masai E, Kubota S, Katayama Y, Kawai S, Yamasaki M, Morohoshi N

机构信息

Laboratory of Wood Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Japan.

出版信息

Biosci Biotechnol Biochem. 1993 Oct;57(10):1655-9. doi: 10.1271/bbb.57.1655.

Abstract

C alpha-dehydrogenase catalyzes the oxidation of arylglycerol-beta-aryl ether at the C alpha-position, and therefore this process produces the specific substrate for beta-etherase, which cleaves beta-ary ethers (C alpha carbonyl type). Here we isolated the C alpha-dehydrogenase gene (lig D) and sequenced its nucleotides. This gene contains an open reading frame of 915 bp and the deduced amino acid sequence had a homology with the ribitol dehydrogenase family. lig D is about 1 kbp upstream of the beta-etherase gene (lig E).

摘要

Cα-脱氢酶催化芳基甘油-β-芳基醚在Cα位的氧化反应,因此该过程产生β-醚酶的特定底物,β-醚酶可裂解β-芳基醚(Cα羰基类型)。在此,我们分离出Cα-脱氢酶基因(lig D)并对其核苷酸进行了测序。该基因包含一个915 bp的开放阅读框,推导的氨基酸序列与核糖醇脱氢酶家族具有同源性。lig D位于β-醚酶基因(lig E)上游约1 kbp处。

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