Results 161 to 170 of about 195,873 (193)

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
openaire   +3 more sources

A Novel Fluorescent Probe-Based High-Throughput Screening Approach for Nicotinamide Cofactor Biomimetics-Dependent Oxidoreductases.

Analytical Chemistry
This study demonstrates the successful development of a high-throughput screening platform for nicotinamide cofactor biomimetics (NCBs)-dependent oxidoreductases using a fluorescent probe ((E)-1-methyl-3-(2-(1,3,3-trimethyl-3H-indol-1-ium-2-yl)vinyl)-4 ...
Huiru Wang, Jieyu Zhou, Xiangyuan Gu, Hao Han, Ye Ni   +4 more
semanticscholar   +1 more source

In silico designing of novel inhibitors for triple inhibition of Aldose Reductase, Aldose Reductase like protein 1, and Aldehyde Reductase.

Current Computer - Aided Drug Design, 2019
Cancer is a well-known and well-studied disease. There are environmental as well as genetic factors that trigger cancer. All forms of cancer are associated with deregulation of genes and proteins.
Arpita Devi
semanticscholar   +1 more source

Evaluation of the Effect of Aldehyde Oxidase Inhibitors on 6-Mercaptopurine Metabolism.

Biological and Pharmaceutical Bulletin
Thiopurines, such as 6-mercaptopurine (6-MP) and azathioprine, are converted to the inactive metabolites 6-thioxanthin (6-TX) and 6-thiouric acid (6-TUA).
Hinata Ueda, Katsuya Narumi, Ayako Furugen, Keisuke Okamoto, Yoshitaka Saito, Masaki Kobayashi   +5 more
semanticscholar   +1 more source

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 ...
Hiltrud White, Claudia Huber, Richard Feicht, Helmut Simon   +3 more
openaire   +1 more source

Modelling the Electron‐Transfer Complex Between Aldehyde Oxidoreductase and Flavodoxin

European Journal of Inorganic Chemistry, 2006
AbstractThree‐dimensional protein structures of the xanthine oxidase family show different solutions for the problem of transferring electrons between the flavin adenine dinucleotide (FAD) group and the molybdenum cofactor. In xanthine oxidase all the cofactors lie within domains of the same protein chain, whereas in CO dehydrogenase the Fe–S centres ...
Ludwig Krippahl, P. Nuno Palma, Isabel Moura, José J. G. Moura   +3 more
openaire   +1 more source

Comparative localization of aldehyde oxidase and xanthine oxidoreductase activity in rat tissues

The Histochemical Journal, 1998
The distribution of aldehyde oxidase activity was evaluated in unfixed cryostat sections from tissues of male Wistar rats using a tissue protectant, polyvinyl alcohol, with Tetranitro BT as a final electron acceptor. The distribution of aldehyde oxidase activity was compared with that of xanthine oxidoreductase.
Y, Moriwaki, T, Yamamoto, J, Yamakita, S, Takahashi, K, Higashino   +4 more
openaire   +2 more sources

Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 Å

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.
J, Rebelo, J, Dias, R, Huber, J, Moura, M, Romão   +4 more
openaire   +3 more sources

The Tungsten-Containing Aldehyde Oxidoreductase fromClostridium thermoaceticumand its Complex with a Viologen-Accepting NADPH Oxidoreductase

Biological Chemistry Hoppe-Seyler, 1992
Purification of aldehyde oxidoreductase from C. thermoaceticum, the first detected enzyme able to reduce reversibly non-activated carboxylic acids to the corresponding aldehydes (White, H., Strobl, G., Feicht, R. & Simon, H. (1989) Eur. J. Biochem. 184, 89-96), results in the generation of multiple forms of the enzyme.
G, Strobl, R, Feicht, H, White, F, Lottspeich, H, Simon   +4 more
openaire   +2 more sources

Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum.

European journal of biochemistry, 2004
Aldehyde oxidoreductase of Eubacterium acidaminophilum was purified to homogeneity under strict anaerobic conditions using a four-step procedure. The purified enzyme was present as a monomer with an apparent molecular mass of 67 kDa and contained 6.0 +/- 0.1 iron, 1.1 +/- 0.2 tungsten, about 0.6 mol pterin cofactor and zinc, but no molybdenum.
David, Rauh, Andrea, Graentzdoerffer, Katrin, Granderath, Jan R, Andreesen, Andreas, Pich   +4 more
openaire   +1 more source