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- W125814099 abstract "Publisher Summary This chapter discusses the properties of horse liver alcohol dehydrogenase SS. Km values for SS isozyme with aliphatic substrates decrease with increasing chain length and in this respect SS isozyme resembles EE isozyme. However, the large Michaelis constants for 2 and 3 carbon substrates with SS isozyme are in sharp contrast to those for EE isozyme that are almost one order of magnitude lower. SS isozyme displays lower Km values for NADH than for NADPH when either a steroidal or a nonsteroidal substrate is kept constant indicating that SS isozyme like EE isozyme is NAD(H)-dependent. The maximal turnover numbers for nonsteroidal substrates are constant and independent of substrate structure for SS isozyme as for EE isozyme, although the values for SS isozyme are 30% of those for EE isozyme. As the maximal turnover in the oxidative direction for SS isozyme approaches the value of the off-velocity constant for NADH, the overall rate of the oxidation of aliphatic alcohols is probably limited by the rate of dissociation of reduced coenzyme." @default.
- W125814099 created "2016-06-24" @default.
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- W125814099 date "1977-01-01" @default.
- W125814099 modified "2023-09-23" @default.
- W125814099 title "PROPERTIES OF HORSE LIVER ALCOHOL DEHYDROGENASE SS" @default.
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- W125814099 doi "https://doi.org/10.1016/b978-0-12-691402-3.50013-5" @default.
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