人肝脏甲醛脱氢酶的产物抑制研究。

Product inhibition studies of human liver formaldehyde dehydrogenase.

作者信息

Uotila L, Mannervik B

出版信息

Biochim Biophys Acta. 1980 Dec 4;616(2):153-7. doi: 10.1016/0005-2744(80)90133-3.

Abstract

The steady-state kinetic mechanism of human liver formaldehyde dehydrogenase (formaldehyde:NAD+ oxidoreductase (glutathione-formylating), EC 1.2.1.1) was investigated by product inhibition of the forward and the reverse reactions catalyzed by the enzyme. The results are compatible with a mechanism which contains the random addition to the enzyme of NAD+ and S-hydroxymethylglutathione (the adduct of glutathione and formaldehyde), or NADH and S-formylglutathione, and free glutathione as the allosteric activator of the enzyme (Uotila, L. and Mannervik, B. (1979) Biochem. J. 177, 869-878).

摘要

通过产物抑制该酶催化的正向和反向反应，研究了人肝甲醛脱氢酶（甲醛：NAD⁺氧化还原酶（谷胱甘肽甲酰化），EC 1.2.1.1）的稳态动力学机制。结果与一种机制相符，该机制包括NAD⁺和S-羟甲基谷胱甘肽（谷胱甘肽与甲醛的加合物）、或NADH和S-甲酰谷胱甘肽随机添加到酶上，以及游离谷胱甘肽作为该酶的变构激活剂（乌奥蒂拉，L.和曼内维克，B.（1979年）《生物化学杂志》177卷，869 - 878页）。