Structure of aldehyde reductase complex: implications for inhibitor specificity
نویسندگان
چکیده
منابع مشابه
Structural features of the aldose reductase and aldehyde reductase inhibitor-binding sites.
The three-dimensional structures of aldose reductase and aldehyde reductase, members of the aldo-keto reductase superfamily, are composed of similar alpha/beta TIM-barrels. However, examination of the structures reveals that the inhibitor-binding site of aldose reductase differs from that of aldehyde reductase due to the participation of non-conserved residues in its formation. This information...
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Human aldo-keto reductase 1B15 (AKR1B15) is a newly discovered enzyme which shares 92% amino acid sequence identity with AKR1B10. While AKR1B10 is a well characterized enzyme with high retinaldehyde reductase activity, involved in the development of several cancer types, the enzymatic activity and physiological role of AKR1B15 are still poorly known. Here, the purified recombinant enzyme has be...
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Dihydrofolate reductase (EC 1.5.1.3) is a key enzyme in the folate biosynthetic pathway. Information regarding key residues in the dihydrofolate-binding site of Mycobacterium avium dihydrofolate reductase is lacking. On the basis of previous information, Asp31 and Leu32 were selected as residues that are potentially important in interactions with dihydrofolate and antifolates (e.g. trimethoprim...
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Aldehyde dehydrogenase from the bioluminescent bacterium, Vibrio harveyi, catalyses the oxidation of long-chain aliphatic aldehydes to acids. The enzyme is unique compared with other forms of aldehyde dehydrogenase in that it exhibits a very high specificity and affinity for the cofactor NADP(+). Structural studies of this enzyme and comparisons with other forms of aldehyde dehydrogenase provid...
متن کاملPig muscle aldehyde reductase. Identity of pig muscle aldehyde reductase with pig lens aldose reductase and with the low Km aldehyde reductase of pig brain and pig kidney.
A monomeric (Mr = 43,000) NADPH-dependent oxidoreductase with a broad substrate specificity for aliphatic and aromatic aldehydes and aldo sugars has been purified from the skeletal muscle of female and castrated pigs. The properties of this enzyme are consistent with those of aldose reductase (EC 1.1.1.21), and the enzyme is immunologically identical with aldose reductase from pig lens. However...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 2005
ISSN: 0108-7673
DOI: 10.1107/s0108767305092032