The membrane glucose dehydrogenase of Escherichia coli

2000 ◽  
pp. 49-54
Author(s):  
C. Anthony ◽  
R. A. Salleh ◽  
P. L. James ◽  
G. E. Cozier
Keyword(s):  
Escherichia Coli ◽  
Glucose Dehydrogenase

scholarly journals Topological analysis of quinoprotein glucose dehydrogenase in Escherichia coli and its ubiquinone-binding site

1993 ◽  
Vol 268 (17) ◽  
pp. 12812-12817
Author(s):  
M. Yamada ◽  
K. Sumi ◽  
K. Matsushita ◽  
O. Adachi ◽  
Y. Yamada
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Glucose Dehydrogenase ◽  
Topological Analysis ◽  
Ubiquinone Binding

scholarly journals Efficient production of (S)-1-phenyl-1, 2-ethanediol using xylan as co-substrate by a coupled multi-enzyme Escherichia coli system

2020 ◽  
Author(s):  
Junchao Rao ◽  
Rongzhen Zhang ◽  
Guanyu Xu ◽  
Lihong Li ◽  
Yan Xu
Keyword(s):  
Escherichia Coli ◽  
Glucose Dehydrogenase ◽  
Optical Purity ◽  
Carbonyl Reductase ◽  
Cofactor Regeneration ◽  
Efficient Production ◽  
Chiral Synthesis ◽  
E Coli ◽  
Concomitant Reduction ◽  
Different Strains

Abstract Background: ( S )-1-phenyl-1,2-ethanediol is an important chiral intermediate in the synthesis of liquid crystals and chiral biphosphines.(S)-carbonyl reductase II from Candida parapsilosis catalyzes the conversion of 2-hydroxyacetophenone to ( S )-1-phenyl-1,2-ethanediol with NADPH as a cofactor. Glucose dehydrogenase with a Ala258Phe mutation is able to catalyze the oxidation of xylose with concomitant reduction of NADP + to NADPH, while endo-β-1,4-xylanase 2 catalyzes the conversion of xylan to xylose. In the present work, the Ala258Phe glucose dehydrogenase mutant and endo-β-1,4-xylanase 2 were introduced into the ( S )-carbonyl reductase II-mediated chiral pathway to strengthen cofactor regeneration by using xylan as a naturally abundant co-substrate. Results: We constructed several coupled multi-enzyme systems by introducing ( S )-carbonyl reductase II, the A258F glucose dehydrogenase mutant and endo-β-1,4-xylanase 2 into Escherichia coli . Different strains were produced by altering the location of the encoding genes on the plasmid. Only recombinant E. coli /pET-G-S-2 expressed all three enzymes, and this strain produced ( S )-1-phenyl-1,2-ethanediol from 2-hydroxyacetophenone as a substrate and xylan as a co-substrate. The optical purity was 100% and the yield was 98.3% (6 g/L 2-HAP) under optimal conditions of 35°C, pH 6.5 and a 2:1 substrate-co-substrate ratio. The introduction of A258F glucose dehydrogenase and endo-β-1,4-xylanase 2 into the ( S )-carbonyl reductase II-mediated chiral pathway caused a 54.6% increase in yield, and simultaneously reduced the reaction time from 48 h to 28 h. Conclusions: This study demonstrates efficient chiral synthesis using a pentose as a co-substrate to enhance cofactor regeneration. This provides a new approach for enantiomeric catalysis through the inclusion of naturally abundant materials.

Effect of PQQ glucose dehydrogenase overexpression in Escherichia coli on sugar-dependent respiration

1995 ◽  
Vol 43 (1) ◽  
pp. 41-44 ◽  
Author(s):  
Koji Sode ◽  
Sayaka Sugimoto ◽  
Mika Watanabe ◽  
Wakako Tsugawa
Keyword(s):  
Escherichia Coli ◽  
Glucose Dehydrogenase ◽  
Pqq Glucose Dehydrogenase

scholarly journals Overexpression of UDP-glucose dehydrogenase in Escherichia coli results in decreased biosynthesis of K5 polysaccharide

2003 ◽  
Vol 374 (3) ◽  
pp. 767-772 ◽  
Author(s):  
Elisabet ROMAN ◽  
Ian ROBERTS ◽  
Kerstin LIDHOLT ◽  
Marion KUSCHE-GULLBERG
Keyword(s):  
Escherichia Coli ◽  
Capsular Polysaccharide ◽  
Glucose Dehydrogenase ◽  
Fold Increase ◽  
Extra Copy ◽  
Polysaccharide Biosynthesis ◽  
Polysaccharide Production ◽  
Significant Difference ◽  
K5 Polysaccharide

The Escherichia coli K5 capsular polysaccharide (glycosaminoglycan) chains are composed of the repeated disaccharide structure: -GlcAβ1,4-GlcNAcα1,4-(where GlcA is glucuronic acid and GlcNAc is N-acetyl-d-glucosamine). The GlcA, present in most glycosaminoglycans, is donated from UDP-GlcA, which, in turn, is generated from UDP-glucose by the enzyme UDP-glucose dehydrogenase (UDPGDH). The formation of UDP-GlcA is critical for the biosynthesis of glycosaminoglycans. To investigate the role of UDPGDH in glycosaminoglycan biosynthesis, we used K5 polysaccharide biosynthesis as a model. E. coli was transformed with the complete gene cluster for K5 polysaccharide production. Additional transformation with an extra copy of UDPGDH resulted in an approx. 15-fold increase in the in vitro UDPGDH enzyme activity compared with the strain lacking extra UDPGDH. UDP-GlcA levels were increased 3-fold in overexpressing strains. However, metabolic labelling with [14C]glucose showed, unexpectedly, that overexpression of UDPGDH lead to decreased formation of K5 polysaccharide. No significant difference in the K5 polysaccharide chain length was observed between control and overexpressing strains, indicating that the decrease in K5-polysaccharide production most probably was due to synthesis of fewer chains. Our results suggest that K5-polysaccharide biosynthesis is strictly regulated such that increasing the amount of available UDP-GlcA results in diminished K5-polysaccharide production.

scholarly journals Heterologous overexpression of Glomerella cingulata FAD-dependent glucose dehydrogenase in Escherichia coli and Pichia pastoris

2011 ◽  
Vol 10 (1) ◽  
pp. 106 ◽  
Author(s):  
Christoph Sygmund ◽  
Petra Staudigl ◽  
Miriam Klausberger ◽  
Nikos Pinotsis ◽  
Kristina Djinović-Carugo ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pichia Pastoris ◽  
Glucose Dehydrogenase ◽  
Glomerella Cingulata ◽  
Heterologous Overexpression

Highly Conserved Asp-204 and Gly-776 Are Important for Activity of the Quinoprotein Glucose Dehydrogenase of Escherichia coli and for Mineral Phosphate Solubilization

2010 ◽  
Vol 18 (2) ◽  
pp. 109-119 ◽  
Author(s):  
Burla Sashidhar ◽  
Krishna Kishore Inampudi ◽  
Lalitha Guruprasad ◽  
Anil Kondreddy ◽  
Kodetham Gopinath ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Phosphate Solubilization ◽  
Glucose Dehydrogenase ◽  
Mineral Phosphate Solubilization ◽  
Mineral Phosphate

scholarly journals Tyrosine Phosphorylation of the UDP-Glucose Dehydrogenase of Escherichia coli Is at the Crossroads of Colanic Acid Synthesis and Polymyxin Resistance

PLoS ONE ◽  
2008 ◽  
Vol 3 (8) ◽  
pp. e3053 ◽  
Author(s):  
Soline Lacour ◽  
Emmanuelle Bechet ◽  
Alain J. Cozzone ◽  
Ivan Mijakovic ◽  
Christophe Grangeasse
Keyword(s):  
Escherichia Coli ◽  
Tyrosine Phosphorylation ◽  
Glucose Dehydrogenase ◽  
Acid Synthesis ◽  
Colanic Acid

scholarly journals Topographical characterization of the ubiquinone reduction site of glucose dehydrogenase in Escherichia coli using depth-dependent fluorescent inhibitors

1999 ◽  
Vol 1412 (1) ◽  
pp. 29-36 ◽  
Author(s):  
Hideto Miyoshi ◽  
Yutaka Niitome ◽  
Kazunobu Matsushita ◽  
Mamoru Yamada ◽  
Hajime Iwamura
Keyword(s):  
Escherichia Coli ◽  
Glucose Dehydrogenase
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