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从醋酸钙不动杆菌中克隆编码两种不同葡萄糖脱氢酶的基因。

Cloning of the genes encoding the two different glucose dehydrogenases from Acinetobacter calcoaceticus.

作者信息

Cleton-Jansen A M, Goosen N, Vink K, van de Putte P

机构信息

Laboratory of Molecular Genetics, University of Leiden, The Netherlands.

出版信息

Antonie Van Leeuwenhoek. 1989 May;56(1):73-9. doi: 10.1007/BF00822586.

Abstract

Glucose dehydrogenase (GDH) is a PQQ dependent bacterial enzyme which converts aldoses to their corresponding acids. A. calcoaceticus contains two different PQQ dependent glucose dehydrogenases designated GDH-A which is active in vivo and GDH-B of which only in vitro activity can be shown. We cloned the genes coding for the two GDH enzymes. The DNA sequences of both gdh genes were determined. There is no obvious homology between gdhA and gdhB. Both GDH enzymes oxidize D-glucose in vitro but disaccharides are specific GDH-B substrates and 2-deoxyglucose is specifically oxidized by GDH-A.

摘要

葡萄糖脱氢酶(GDH)是一种依赖吡咯喹啉醌(PQQ)的细菌酶,可将醛糖转化为相应的酸。醋酸钙不动杆菌含有两种不同的依赖PQQ的葡萄糖脱氢酶,分别命名为GDH-A(在体内具有活性)和GDH-B(仅能显示体外活性)。我们克隆了编码这两种GDH酶的基因。测定了两个gdh基因的DNA序列。gdhA和gdhB之间没有明显的同源性。两种GDH酶在体外均能氧化D-葡萄糖,但二糖是GDH-B的特异性底物,而2-脱氧葡萄糖则被GDH-A特异性氧化。

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