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由3-二甲基氨基-1-丙炔与线粒体胺氧化酶的黄素相互作用形成的共价加合物的结构。

The structure of the covalent adduct formed by the interaction of 3-dimethylamino-1-propyne and the flavine of mitochondrial amine oxidase.

作者信息

Maycock A L, Abeles R H, Salach J I, Singer T P

出版信息

Biochemistry. 1976 Jan 13;15(1):114-25. doi: 10.1021/bi00646a018.

DOI:10.1021/bi00646a018
PMID:2278
Abstract

3-Dimethylamino-1-propyne irreversibly inactivates mitochondrial monoamine oxidase from bovine liver. The inactivation results in the loss of absorption in the 450-500-nm region of the flavine spectrum and a concomitant increase in absorbance at 410 nm. For the enzyme-bound adduct epsilon410 = 28000. The spectral properties of the adduct of the liver enzyme with 3-dimethylamino-1-propyne are similar to those observed when the pig kidney enzyme is inactivated with pargyline (Chuang et al. (1974), J. Biol. Chem. 249, 2381). From a proteolytic digest of the enzyme inactivated with labeled inhibitor a flavine peptide has been isolated which contains 1 mol of inactivator/mol of flavine. The chemical and spectral properties of the adduct are those of compounds containing the structure --N--CH==CH--CH==N+ less than. It was concluded that the flavine-inhibtor adduct is a N-5 substituted dihydroflavine and its structure has been determined.

摘要

3 - 二甲基氨基 - 1 - 丙炔可使牛肝线粒体单胺氧化酶不可逆地失活。这种失活导致黄素光谱在450 - 500纳米区域的吸收丧失,并伴随410纳米处吸光度的增加。对于酶结合加合物,ε410 = 28000。肝脏酶与3 - 二甲基氨基 - 1 - 丙炔形成的加合物的光谱性质,与用优降宁使猪肾酶失活时观察到的光谱性质相似(Chuang等人,(1974年),《生物化学杂志》249卷,2381页)。从用标记抑制剂失活的酶的蛋白水解消化物中分离出一种黄素肽,其每摩尔黄素含有1摩尔失活剂。加合物的化学和光谱性质是含有结构--N--CH==CH--CH==N⁺的化合物的性质。得出的结论是,黄素 - 抑制剂加合物是一种N - 5取代的二氢黄素,其结构已确定。

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