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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Biochem J. 1968 Nov;110(1):53-7. doi: 10.1042/bj1100053.

Ficin and stem-bromelain are irreversibly inhibited by 1,3-dibromoacetone, a reagent designed to react first with the active-site cysteine residue and subsequently with a second nucleophile. Evidence is presented that establishes that a histidine residue is within a 5A locus of the active-site cysteine residue in both enzymes. The histidine residue in both enzymes is alkylated at N-1 by dibromoacetone. It is suggested that, as with papain, the thiol and imidazole groups act in concert in the hydrolysis of substrates by these enzymes. 2. The inhibition of thiol-subtilisin with 1,3-dibromoacetone is shown to be due to the alkylation of a cysteine residue only.

无花果蛋白酶和茎菠萝蛋白酶会被1,3 - 二溴丙酮不可逆地抑制，1,3 - 二溴丙酮是一种设计用于首先与活性位点半胱氨酸残基反应，随后与第二个亲核试剂反应的试剂。有证据表明，在这两种酶中，一个组氨酸残基位于活性位点半胱氨酸残基的5埃范围内。这两种酶中的组氨酸残基在N - 1位被二溴丙酮烷基化。有人提出，与木瓜蛋白酶一样，巯基和咪唑基团在这些酶水解底物的过程中协同作用。2. 结果表明，1,3 - 二溴丙酮对巯基枯草杆菌蛋白酶的抑制作用仅归因于一个半胱氨酸残基的烷基化。

Biochem J. 1968 Nov;110(1):53-7. doi: 10.1042/bj1100053.

Ficin and stem-bromelain are irreversibly inhibited by 1,3-dibromoacetone, a reagent designed to react first with the active-site cysteine residue and subsequently with a second nucleophile. Evidence is presented that establishes that a histidine residue is within a 5A locus of the active-site cysteine residue in both enzymes. The histidine residue in both enzymes is alkylated at N-1 by dibromoacetone. It is suggested that, as with papain, the thiol and imidazole groups act in concert in the hydrolysis of substrates by these enzymes. 2. The inhibition of thiol-subtilisin with 1,3-dibromoacetone is shown to be due to the alkylation of a cysteine residue only.

无花果蛋白酶和茎菠萝蛋白酶会被1,3 - 二溴丙酮不可逆地抑制，1,3 - 二溴丙酮是一种设计用于首先与活性位点半胱氨酸残基反应，随后与第二个亲核试剂反应的试剂。有证据表明，在这两种酶中，一个组氨酸残基位于活性位点半胱氨酸残基的5埃范围内。这两种酶中的组氨酸残基在N - 1位被二溴丙酮烷基化。有人提出，与木瓜蛋白酶一样，巯基和咪唑基团在这些酶水解底物的过程中协同作用。2. 结果表明，1,3 - 二溴丙酮对巯基枯草杆菌蛋白酶的抑制作用仅归因于一个半胱氨酸残基的烷基化。