GLU742 SUBSTITUTION TO LYS ENHANCES THE EDTA TOLERANCE OF ESCHERICHIA-COLI PQQ GLUCOSE-DEHYDROGENASE

被引：34

作者：

SODE, K

SANO, H

机构：

[1] Department of Biotechnology, Faculty of Technology, Tokyo University of Agriculture and Technology, Koganei, Tokyo, 184

来源：

BIOTECHNOLOGY LETTERS | 1994年 / 16卷 / 05期

关键词：

PYRROLOQUINOLINE QUINONE(PQQ); QUINOPROTEIN GLUCOSE DEHYDROGENASE (GDH); PUTATIVE PQQ BINDING SITE; SITE DIRECTED MUTAGENESIS; ESCHERICHIA COLI; ACINETOBACTER CALCOACETICUS;

D O I：

10.1007/BF01023325

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Based on homology analysis of the PQQ (pyrroloquinoline quinone) glucose dehydrogenase (PQQGDH) gene from Esherichia coli and Acinetobacter calcoaceticus, Glu742 was substituted to Lys by site directed mutagenesis of the E. coli PQQGDH gene (gcd). The mutant enzyme, E742K showed higher tolerance towards EDTA inactivation than wild type PQQGDH. This is the first mutagenesis study of putative a PQQ binding site in PQQ enzyme.

引用

页码：455 / 460

页数：6

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