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- W70138861 abstract "This chapter discusses the substrate specificity and the hydrophobic site of liver alcohol dehydrogenase (L-ADH). Horse L-ADH has a very broad specificity for primary, secondary and cyclic alcohols, as does ADH from a variety of sources such as rat and human. The hydrophobic nature of the substrate binding site has been confirmed in the present study by the use of n-alkyl substituted aminoethanols, compounds which are known to be incorporated into liver and brain phospholipids. These substrates show higher reactivity as the groups around the n-alkyl substituted base become more hydrophobic. As observed with ethanol as substrate, formation of ternary abortive complexes of enzyme-NADH-amino-ethanol are seen at high concentrations of aminoethanols. The lipophilic nature of the association of aminoethanols with the binary enzyme-NADH and enzyme-NAD complexes has been studied and compared with the substrate analogue inhibitors, amides, and acids. As with acids and amides as inhibitors, the association of aminoethanol substrates with the binary complexes increases as the number and size of the substituted n-alkyl group increases." @default.
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- W70138861 date "1977-01-01" @default.
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- W70138861 title "SUBSTRATE SPECIFICITY AND THE HYDROPHOBIC SITE OF LIVER ALCOHOL DEHYDROGENASE (L-ADH)" @default.
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- W70138861 doi "https://doi.org/10.1016/b978-0-12-691402-3.50012-3" @default.
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