Results 131 to 140 of about 8,399 (179)

A prescription for engineering PFAS biodegradation. [PDF]

Biochem J
Wackett LP, Robinson SL.
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A Biosensor for Aromatic Aldehydes Comprising the Mediator Dependent PaoABC‐Aldehyde Oxidoreductase

Electroanalysis, 2012
AbstractA novel aldehyde oxidoreductase (PaoABC) from Escherichia coli was utilized for the development of an oxygen insensitive biosensor for benzaldehyde. The enzyme was immobilized in polyvinyl alcohol and currents were measured for aldehyde oxidation with different one and two electron mediators with the highest sensitivity for benzaldehyde in the ...
Badalyan, Artavazd, Neumann-Schaal, Meina, Leimkühler, Silke (Prof. Dr.), Wollenberger, Ursula (Prof. Dr.)   +3 more
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Aldehyde oxidoreductase as a biocatalyst: Reductions of vanillic acid

Enzyme and Microbial Technology, 2008
Aldehyde oxidoreductase (carboxylic acid reductase) catalyzes the Mg(2+), ATP and NADPH dependent reduction of carboxylic acids to their corresponding aldehydes. The identification of the gene from Nocardia sp. NRRL 5646 and its expression in E.
Lacy Daniels, Shuvendu Das, John P. N. Rosazza, Padmesh Venkitasubramanian, Andrew S. Lamm   +4 more
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Structure of a Hyperthermophilic Tungstopterin Enzyme, Aldehyde Ferredoxin Oxidoreductase

Science, 1995
The crystal structure of the tungsten-containing aldehyde ferredoxin oxidoreductase (AOR) from Pyrococcus furiosus , a hyperthermophilic archaeon (formerly archaebacterium) that grows optimally at 100°C, has been determined at 2.3 angstrom resolution by means of multiple isomorphous replacement and multiple crystal ...
Chan, Michael K., Mukund, Swarnalatha, Kletzin, Arnulf, Adams, Michael W. W., Rees, Douglas C.   +4 more
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Microbial Alcohol, Aldehyde and Formate Ester Oxidoreductases

1993
Formation of alcohols by natural processes takes place in the fermentative breakdown of sugars and the oxidative dissimilation of alkanes. In view of the wide-spreadness of these processes, it is understandable that many microbial species have the capacity to degrade these compounds.
Peter W. van Ophem, Johannis A. Duine
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Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 Å [PDF]

JBIC Journal of Biological Inorganic Chemistry, 2001
The sulfate-reducing bacterium aldehyde oxidoreductase from Desulfovibrio gigas (MOP) is a member of the xanthine oxidase family of enzymes. It has 907 residues on a single polypeptide chain, a molybdopterin cytosine dinucleotide (MCD) cofactor and two [2Fe-2S] iron-sulfur clusters.
Jorge Rebelo, Robert Huber, José J. G. Moura, Maria João Romão, João M. Dias   +4 more
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Nicotinoprotein Alcohol/Aldehyde Oxidoreductases

1996
Enzymes with tightly bound NAD(P), acting as cofactor, have been described in the past. Well known examples include UDP-galactose 4-epimerase from E. coli (Wilson and Hogness, 1964) and lactate-oxaloacetate transhydrogenase from V. alcalescens (Allen, 1966).
Johannis A. Duine, Simon de Vries, Sander R. Piersma   +2 more
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[4] Aldehyde oxidoreductases and other molybdenum-containing enzymes

1994
Publisher Summary This chapter describes aldehyde oxidoreductases and other molybdenum (Mo)-containing enzymes. Desulfovibrio gigas ( D. gigas ) Mo -containing protein is isolated on the basis of its optical absorption characteristics.Mo was first detected by electron paramagnetic resonance (EPR).
Belarmino A.S. Barata, José J. G. Moura
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Microbial Alcohol/Aldehyde Oxidoreductases in Enantioselective Conversions

1992
Microbes have an enormous diversity of alcohol and aldehyde oxidoreductases. A brief overview is given of the types known and of some novel ones discovered recently. Except from the classical, NAD-dependent, alcohol dehydrogenase (the long chain, zinc-containing type, EC 1.1.1.1), these enzymes are unexplored with respect to enantioselectivity.
Jaap A. Jongejan, J. B. A. Van Tol, Johannis A. Duine, Arie Geerlof   +3 more
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On a reversible molybdenum-containing aldehyde oxidoreductase from Clostridium formicoaceticum

Archives of Microbiology, 1993
Clostridium formicoaceticum grown in the presence of 1 mM molybdate and about 1.5×10-5 mM tungsten (present in the 5 g yeast extract/l of the growth medium) forms two reversible aldehyde oxidoreductases in an activity ratio of about 45:55. The fraction of 45% does not bind to the octyl-Sepharose column, whereas the 55% aldehyde oxidoreductase binds to ...
Richard Feicht, Claudia Huber, Helmut Simon, Hiltrud White   +3 more
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