The Substrate Binding Site of Aldehyde Reductase from Pig Liver
نویسندگان
چکیده
منابع مشابه
Studies on the active site of pig kidney aldehyde reductase.
observed in enzyme-methotrexate complexes. The orientation that appears to be required for catalysis can be readily achieved by rotations of the pteridine of 180° around the C-6-C-9 bond and 30° about the C-9-N-10 bond. In this orientation, C-4 of the NADPH nicotinamide ring closely approaches C-6 of the substrate, and N-5 of the substrate is adjacent to aspartic acid-30 of the enzyme. It has b...
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The reduction of p-nitroso-N-dimethylaniline, p-nitroso-N-diethylaniline, p-nitrosophenol and p-nitroso-N-phenylaniline with NADPH in the presence of aldehyde reductases 1 and 2 is described. The reactivity of these nitroso substrates is increased by hydrophobic substituents and those promoting OH- elimination from the molecule of the reduced substrate. NN-Dimethylbenzoquinonedi-iminium cation ...
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Little is known about how substrates bind to CtXR (Candida tenuis xylose reductase; AKR2B5) and other members of the AKR (aldo-keto reductase) protein superfamily. Modelling of xylose into the active site of CtXR suggested that Trp23, Asp50 and Asn309 are the main components of pentose-specific substrate-binding recognition. Kinetic consequences of site-directed substitutions of these residues ...
متن کاملBiliverdin reductase of guinea pig liver.
The biosynthesis of the heme portion of hemoglobin by animal tissues has been studied extensively (1). In contrast, relatively little is known about the enzymes participating in the initial steps of the pathway for heme catabolism. Thus, the reaction in which heme and globin are separated remains essentially obscure, although it is known that heme undergoes ring cleavage with liberation of carb...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1982
ISSN: 0014-2956
DOI: 10.1111/j.1432-1033.1982.tb05802.x