1,4-Diamino-2-butyne as the mechanism-based pea diamine oxidase inhibitor.
1,4-Diamino-2-butyne as the mechanism-based pea diamine oxidase inhibitor.
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1,4-二氨基-2-丁炔作为基于机制的豌豆二胺氧化酶抑制剂。
DOI：
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发表时间：
1992
期刊：
影响因子：
--
通讯作者：
I. Frébort
中科院分区：
文献类型：
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作者：
P. Peč;I. Frébort
1，4-二氨基-2-丁炔是来自豌豆子叶的二胺氧化酶（EC 1.4.3.6）的基于机制的抑制剂。它显示饱和动力学Km = 1 mM像一个底物，但它的相互作用导致时间依赖性损失的酶活性，这是不能恢复的凝胶过滤。底物1，4-二氨基丁烷和竞争性抑制剂1，4-二氨基-2-丁酮保护酶免于失活。结果表明，1，4-二氨基-2-丁炔与酶的作用机理是亲核试剂与酶反应时，吡咯与酶形成共价键结合的氨基丙二烯化合物。通过与埃利希试剂的反应证实了在失活酶中吡咯的存在。动力学数据表明，1，4-二氨基-2-丁炔是一种基于机理的灭活剂，其翻转次数r = 17，特征常数K' = 0.32 mM，k（in）= 4.89 min-1。
1,4-Diamino-2-butyne is a mechanism-based inhibitor of diamine oxidase (EC 1.4.3.6) from pea cotyledons. It shows saturation kinetics Km = 1 mM like a substrate, but its interaction leads to time-dependent loss of enzyme activity which is not restored by gel filtration. The substrate 1,4-diaminobutane and the competitive inhibitor 1,4-diamino-2-butanone protect the enzyme against inactivation. Changes in the enzyme electronic spectra with 1,4-diamino-2-butyne were found. The mechanism of the interaction involves an intermediate aminoallenic compound, which is formed with covalent bound pyrrole in the reaction of the nucleophile with the enzyme. The presence of a pyrrole in the inactivated enzyme was confirmed by reaction with Ehrlich's reagent. The kinetic data obtained in this study indicate that 1,4-diamino-2-butyne is a mechanism-based inactivator with number of turnovers, r = 17 and characteristic constants K' = 0.32 mM and k(in) = 4.89 min-1.
影响因子：
2.9
作者：
HARTMANN, C;KLINMAN, JP
通讯作者：
KLINMAN, JP
DOI：
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发表时间：
1991
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Brown,DE;McGuirl,MA;Dooley,DM;Janes,SM;Mu,D;Klinman,JP
通讯作者：
Klinman,JP
影响因子：
2.9
作者：
JANES, SM;KLINMAN, JP
通讯作者：
KLINMAN, JP