Britt A J, Bruce N C, Lowe C R
Institute of Biotechnology, University of Cambridge, UK.
FEMS Microbiol Lett. 1992 May 15;72(1):49-55. doi: 10.1016/0378-1097(92)90488-a.
A constitutive NAD(+)-linked alcohol dehydrogenase was purified 338-fold from cells of Pseudomonas maltophilia MB11L grown on glucose. Maximum activity was observed with cyclic and linear secondary alcohols, with little activity seen against primary or aromatic alcohols. Substrate oxidation activity was maximal at pH 10.0, while substrate reduction was optimal at pH 4.5. The Km values for propan-2-ol, NAD+ and acetone were 87, 413 and 143 microM respectively. The enzyme is a tetramer with subunit Mr of approximately 44,000. It has an isoelectric point of 4.75, and was inhibited by chelating agents, thiol reagents and certain metal ions.
从在葡萄糖上生长的嗜麦芽窄食单胞菌MB11L细胞中纯化出一种组成型NAD⁺连接的醇脱氢酶，纯化倍数为338倍。对环状和线性仲醇观察到最大活性，对伯醇或芳香醇的活性则很低。底物氧化活性在pH 10.0时最大，而底物还原在pH 4.5时最佳。丙-2-醇、NAD⁺和丙酮的Km值分别为87、413和143微摩尔。该酶是一种四聚体，亚基Mr约为44,000。其等电点为4.75，并且受到螯合剂、硫醇试剂和某些金属离子的抑制。
