Larroy Carol, Parés Xavier, Biosca Josep A
Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Barcelona, Spain.
Eur J Biochem. 2002 Nov;269(22):5738-45. doi: 10.1046/j.1432-1033.2002.03296.x.
A new NADP(H)-dependent alcohol dehydrogenase (the YCR105W gene product, ADHVII) has been identified in Saccharomyces cerevisiae. The enzyme has been purified to homogeneity and found to be a homodimer of 40 kDa subunits and a pI of 6.2-6.4. ADHVII shows a broad substrate specificity similar to the recently characterized ADHVI (64% identity), although they show some differences in kinetic properties. ADHVI and ADHVII are the only members of the cinnamyl alcohol dehydrogenase family in yeast. Simultaneous deletion of ADH6 and ADH7 was not lethal for the yeast. Both enzymes could participate in the synthesis of fusel alcohols, ligninolysis and NADP(H) homeostasis.
在酿酒酵母中已鉴定出一种新的依赖烟酰胺腺嘌呤二核苷酸磷酸（NADP(H)）的乙醇脱氢酶（YCR105W基因产物，ADHVII）。该酶已被纯化至同质状态，发现它是由40 kDa亚基组成的同型二聚体，其等电点为6.2 - 6.4。ADHVII显示出与最近鉴定的ADHVI（序列同一性为64%）相似的广泛底物特异性，尽管它们在动力学性质上存在一些差异。ADHVI和ADHVII是酵母中肉桂醇脱氢酶家族仅有的成员。同时缺失ADH6和ADH7对酵母并不致命。这两种酶都可参与杂醇的合成、木质素分解以及NADP(H)的稳态调节。
