Archaebacterial dehydrogenases with dual cofactor specificity: glucose dehydrogenase from Thermoplasma acidophilum

1988 ◽  
Vol 16 (5) ◽  
pp. 864-864 ◽  
Author(s):  
L. D. SMITH ◽  
S. J. BUNGARD ◽  
M. J. DANSON ◽  
D. W. HOUGH
Keyword(s):  
Glucose Dehydrogenase ◽  
Thermoplasma Acidophilum ◽  
Cofactor Specificity

scholarly journals Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum

1989 ◽  
Vol 261 (3) ◽  
pp. 973-977 ◽  
Author(s):  
L D Smith ◽  
N Budgen ◽  
S J Bungard ◽  
M J Danson ◽  
D W Hough
Keyword(s):  
Amino Acid ◽  
Polypeptide Chain ◽  
Glucose Dehydrogenase ◽  
Sulfolobus Solfataricus ◽  
Purification And Characterization ◽  
Terminal Amino Acid ◽  
Thermoplasma Acidophilum ◽  
Catalytically Active ◽  
Terminal Amino

Glucose dehydrogenase was purified to homogeneity from the thermoacidophilic archaebacterium Thermoplasma acidophilum. The enzyme is a tetramer of polypeptide chain Mr 38,000 +/- 3000, it is catalytically active with both NAD+ and NADP+ cofactors, and it is thermostable and remarkably resistant to a variety of organic solvents. The amino acid composition was determined and compared with those of the glucose dehydrogenases from the archaebacterium Sulfolobus solfataricus and the eubacteria Bacillus subtilis and Bacillus megaterium. The N-terminal amino acid sequence of the Thermoplasma acidophilum enzyme was determined to be: (S/T)-E-Q-K-A-I-V-T-D-A-P-K-G-G-V-K-Y-T-T-I-D-M-P-E.

scholarly journals The crystal structure of glucose dehydrogenase from Thermoplasma acidophilum

Structure ◽  
1994 ◽  
Vol 2 (5) ◽  
pp. 385-393 ◽  
Author(s):  
Jamie John ◽  
Susan J Crennell ◽  
David W Hough ◽  
Michael J Danson ◽  
Garry L Taylor
Keyword(s):  
Crystal Structure ◽  
Glucose Dehydrogenase ◽  
Thermoplasma Acidophilum

Crystallization and preliminary crystallographic study of glucose dehydrogenase from the archaebacterium Thermoplasma acidophilum

1991 ◽  
Vol 222 (2) ◽  
pp. 143-144 ◽  
Author(s):  
Jeremy R. Bright ◽  
Ruth Mackness ◽  
Michael J. Danson ◽  
David W. Hough ◽  
Garry L. Taylor ◽  
...  
Keyword(s):  
Glucose Dehydrogenase ◽  
Thermoplasma Acidophilum ◽  
Crystallographic Study

Probing the Substrate Promiscuity of Isopentenyl Phosphate Kinase as a Platform for Hemiterpene Analogue Production

2019 ◽  
Author(s):  
Sean Lund ◽  
Taylor Courtney ◽  
Gavin Williams
Keyword(s):  
Synthetic Biology ◽  
Building Blocks ◽  
Isoprenoid Biosynthesis ◽  
Thermoplasma Acidophilum ◽  
Substrate Promiscuity ◽  
Enzymatic Pathways ◽  
First Time ◽  
Rate Limiting ◽  
Alcohol Dependent ◽  
Isopentenyl Phosphate

Isoprenoids are a large class of natural products with wide-ranging applications. Synthetic biology approaches to the manufacture of isoprenoids and their new-to-nature derivatives are limited due to the provision in Nature of just two hemiterpene building blocks for isoprenoid biosynthesis. To address this limitation, artificial chemo-enzymatic pathways such as the alcohol-dependent hemiterpene pathway (ADH) serve to leverage consecutive kinases to convert exogenous alcohols to pyrophosphates that could be coupled to downstream isoprenoid biosynthesis. To be successful, each kinase in this pathway should be permissive of a broad range of substrates. For the first time, we have probed the promiscuity of the second enzyme in the ADH pathway, isopentenyl phosphate kinase from Thermoplasma acidophilum, towards a broad range of acceptor monophosphates. Subsequently, we evaluate the suitability of this enzyme to provide non-natural pyrophosphates and provide a critical first step in characterizing the rate limiting steps in the artificial ADH pathway.<br>

scholarly journals Exploration of the cofactor specificity of wild-type phosphite dehydrogenase and its mutant using molecular dynamics simulations

RSC Advances ◽  
2021 ◽  
Vol 11 (24) ◽  
pp. 14527-14533
Author(s):  
Kunlu Liu ◽  
Min Wang ◽  
Yubo Zhou ◽  
Hongxiang Wang ◽  
Yudong Liu ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Wild Type ◽  
Cofactor Specificity ◽  
Phosphite Dehydrogenase ◽  
Dynamics Simulations

Phosphite dehydrogenase (Pdh) catalyzes the NAD-dependent oxidation of phosphite to phosphate with the formation of NADH.

scholarly journals Towards a Novel Computer-Aided Optimization of Microreactors: Techno-Economic Evaluation of an Immobilized Enzyme System

Symmetry ◽  
2021 ◽  
Vol 13 (3) ◽  
pp. 524
Author(s):  
Philip Pietrek ◽  
Manfred Kraut ◽  
Roland Dittmeyer
Keyword(s):  
Magnetic Beads ◽  
Glucose Dehydrogenase ◽  
Packed Bed ◽  
Detailed Knowledge ◽  
Reaction Conditions ◽  
Flow Reactors ◽  
Continuous Flow Reactors ◽  
Enzyme Cascades ◽  
And Control ◽  
Physical And Chemical

Immobilized multi-enzyme cascades are increasingly used in microfluidic devices. In particular, their application in continuous flow reactors shows great potential, utilizing the benefits of reusability and control of the reaction conditions. However, capitalizing on this potential is challenging and requires detailed knowledge of the investigated system. Here, we show the application of computational methods for optimization with multi-level reactor design (MLRD) methodology based on the underlying physical and chemical processes. We optimize a stereoselective reduction of a diketone catalyzed by ketoreductase (Gre2) and Nicotinamidadenindinukleotidphosphat (NADPH) cofactor regeneration with glucose dehydrogenase (GDH). Both enzymes are separately immobilized on magnetic beads forming a packed bed within the microreactor. We derive optimal reactor feed concentrations and enzyme ratios for enhanced performance and a basic economic model in order to maximize the techno-economic performance (TEP) for the first reduction of 5-nitrononane-2,8-dione.

scholarly journals A Redox-Neutral, Two-Enzyme Cascade for the Production of Malate and Gluconate from Pyruvate and Glucose

2021 ◽  
Vol 11 (11) ◽  
pp. 4877
Author(s):  
Ravneet Mandair ◽  
Pinar Karagoz ◽  
Roslyn M. Bill
Keyword(s):  
Malate Dehydrogenase ◽  
Closed System ◽  
Glucose Dehydrogenase ◽  
Sulfolobus Solfataricus ◽  
Cofactor Regeneration ◽  
Triple Mutant ◽  
Thermococcus Kodakarensis ◽  
Platform Chemicals ◽  
Enzyme Cascade

A triple mutant of NADP(H)-dependent malate dehydrogenase from thermotolerant Thermococcus kodakarensis has an altered cofactor preference for NAD+, as well as improved malate production compared to wildtype malate dehydrogenase. By combining mutant malate dehydrogenase with glucose dehydrogenase from Sulfolobus solfataricus and NAD+/NADH in a closed reaction environment, gluconate and malate could be produced from pyruvate and glucose. After 3 h, the yield of malate was 15.96 mM. These data demonstrate the feasibility of a closed system capable of cofactor regeneration in the production of platform chemicals.

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