对硝基苯基氨基甲酸酯与脲酶的相互作用。
The interaction of p-nitrophenyl carbamate with urease.
作者信息
Bennett J, Wren E A
出版信息
Biochim Biophys Acta. 1977 Jun 10;482(2):421-6. doi: 10.1016/0005-2744(77)90256-x.
PMID:884123
Abstract
- p-Nitrophenyl carbamate and thiourea have been shown to be substrates for urease (urea amidohydrolase, EC 3.5.1.5) 2. Urease has been shown to have a lower Km, 0.67 mM, with p-nitrophenyl carbamate than with urea, 2.0 mM. 3. The V of urease for the hydrolysis of urea, p-nitrophenyl carbamate and thiourea has been shown to be the same, indicating a common rate-limiting step. 4. A mechanism has been proposed for urease where the initial rate-limiting step is the release of a molecule of ammonia from the substrates.
摘要
对硝基苯基氨基甲酸酯和硫脲已被证明是脲酶（尿素酰胺水解酶，EC 3.5.1.5）的底物。
已表明脲酶对氨基甲酸对硝基苯酯的米氏常数（Km）较低，为0.67 mM，而对尿素的Km为2.0 mM。
已表明脲酶水解尿素、对硝基苯基氨基甲酸酯和硫脲的最大反应速度（V）相同，这表明存在一个共同的限速步骤。
有人提出了一种脲酶作用机制，其中初始限速步骤是从底物中释放出一分子氨。
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