Results 221 to 230 of about 943,763 (288)
The emerging role of aldehyde:ferredoxin oxidoreductases in microbially-catalyzed alcohol production
Journal of Biotechnology, 2019 The development of a bio-refinery industry based on liquid fuels is presumably key to successful replacement of fossil fuels and a reduction of carbon dioxide (CO2) emissions. Ethanol and longer-chain alcohols are supposed to play a key role since they are relatively easy to produce, using microorganisms as whole-cell biocatalysts.
Laura Sofie Nissen, Mirko Basen
semanticscholar +4 more sources
Sugar oxidoreductases and veratryl alcohol oxidase as related to lignin degradation
Journal of Biotechnology, 1997 Properties of cellobiose:quinone oxidoreductase (CBQ), cellobiose dehydrogenase (CDH), glyoxal oxidase (GLOX), glucose oxidases and veratryl alcohol oxidase (VAO) are reviewed. There is strong evidence that CDH reduces quinones, phenoxy and cation radicals.
Paul Ander, Liberato Marzullo
semanticscholar +5 more sources
Nicotinoprotein Alcohol/Aldehyde Oxidoreductases
Advances in experimental medicine and biology, 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).
Sander R. Piersma +2 more
semanticscholar +5 more sources
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000 Aryl-alcohol oxidase (AAO), an FAD-dependent enzyme involved in lignin degradation, has been cloned from Pleurotus eryngii. The AAO protein is composed of 593 amino acids, 27 of which form a signal peptide. It shows 33% sequence identity with glucose oxidase from Aspergillus niger and lower homology with other oxidoreductases.
Elisa Varela +2 more
semanticscholar +4 more sources
Microbial Alcohol, Aldehyde and Formate Ester Oxidoreductases
Advances in Experimental Medicine and Biology, 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
semanticscholar +4 more sources
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.
Arie Geerlof +3 more
semanticscholar +3 more sources
Analytica Chimica Acta, 1978 Flowthrough enzyme electrodes are reported for determinations of alcohol, lactate and glutamate. Oxidoreductases mixed with immobilized NAD+ cofactor are held between a suitable platinum electrode and a semipermeable membrane. The coenzyme is readily regenerated either directly by electrochemical oxidation or by using phenazine methosulphate (PMS+) as ...
Albertas Malinauskas, Juozas Kulys
semanticscholar +3 more sources
Alcohol dehydrogenase (alcohol: NAD oxidoreductase) from the pea seedling
Phytochemistry, 1966 Abstract Alcohol: NAD oxidoreductase (alcohol dehydrogenase, ADH), was partially purified from pea seedlings, and with acetaldehyde gave a Michaelis constant of 4·3 × 10 −4 M. Activity was inhibited by p -chloromercuriphenylsulphonic acid, phenylmercuric acetate, O -iodosobenzoate, ferron, and other metal-binding agents.
Yonezo Suzuki
openalex +2 more sources
Quinoprotein oxidoreductases for the oxidation of alcohols, sugars and amines
, 1994 Quinoproteins are enzymes containing a quinone cofactor, that is the non-covalently bound PQQ or the protein-chain-integrated TPQ or TTQ. Quinoprotein dehydrogenases play a role in non-phosphorylative degradation of sugars, alcohols, aldehydes, ketones, and amines by Gram-negative bacteria, providing useful energy to the organism by their capacity to ...
Johannis A. Duine +2 more
openalex +2 more sources
Archives of Biochemistry and Biophysics, 1996 Quinone oxidoreductase, zeta-crystallin, glucose dehydrogenase, and alcohol dehydrogenase belong to a superfamily of medium-chain dehydrogenase/reductases. The crystal structures of Escherichia coli quinone oxidoreductase (QOR) and Thermoplasma acidophilum glucose dehydrogenase have recently been determined and are compared here with the well-known ...
Karen J. Edwards +5 more
openalex +3 more sources