89 species of plants from Bryophyta, Pteridophyta, Gymnosperms and Angiosperms examined, high levels of coniferyl alcohol dehydrogenase activity found among dicots and gymnosperms; specific activity is 0.831 U/mg protein
effect of storage of breaker tomatoes for 20 days at various temperatures on the activity of enzymes of phenylpropanoid metabolism, aromatic alcohol dehydrogenase in enzyme unit (EU)/mg protein: 0°C: 23.2, 2°C: 29.2, 5°C: 10.9, 10°C: 4.7
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crystal structure of the apoenzyme as well as its NADP+-bound state with resolutions down to 2.8 A. ADH displays a homotetrameric quaternary structure that can be described as a dimer of homodimers while in each subunit a seven-stranded parallel beta-sheet, flanked by three alpha-helices on each side, forms a Rossmann fold-type dinucleotide binding domain. NADP+ specificity is largely governed by the residues Asn15, Gly37, Arg38, and Arg39
the enzyme shows moderate thermostability with a half-life of 6.2 h at 55°C and 1.5 h at 60°C. The activity loss at 65°C is relatively rapid, and the enzyme retains 30.8% of the initial activity after 30 min of heat treatment
Ying, X.; Wang, Y.; Xiong, B.; Wu, T.; Xie, L.; Yu, M.; Wang, Z.
Characterization of an allylic/benzyl alcohol dehydrogenase from Yokenella sp. strain WZY002, an organism potentially useful for the synthesis of alpha,beta-unsaturated alcohols from allylic aldehydes and ketones