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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

Amemura A, Kitagawa H, Harda T

J Biochem. 1975 Mar;77(3):575-8. doi: 10.1093/oxfordjournals.jbchem.a130758.

Pullulanase [EC 3.2.1.4.] was inhibited by Hg2+, N-bromosuccinimide, 2-hydroxy-5-nitrobenzyl bromide, riboflavine 5'-phosphate, histamine, imidazole, and carbodiimide. 2. The tryptophan groups of the pullulanase were modified by N-bromosuccinimede. It was found that one or two of the 25 tryptophan groups seemed to be important for the activity. 3. Studies on difference spectra using various substrates suggested that the tryptophan groups were important for the formation of an enzyme-substrate complex.

支链淀粉酶[EC 3.2.1.4.]受到Hg2+、N-溴代琥珀酰亚胺、2-羟基-5-硝基苄基溴、核黄素5'-磷酸、组胺、咪唑和碳二亚胺的抑制。2. 支链淀粉酶的色氨酸基团被N-溴代琥珀酰亚胺修饰。发现25个色氨酸基团中的一两个对活性似乎很重要。3. 使用各种底物的差光谱研究表明，色氨酸基团对于酶-底物复合物的形成很重要。

Amemura A, Kitagawa H, Harda T

J Biochem. 1975 Mar;77(3):575-8. doi: 10.1093/oxfordjournals.jbchem.a130758.

Pullulanase [EC 3.2.1.4.] was inhibited by Hg2+, N-bromosuccinimide, 2-hydroxy-5-nitrobenzyl bromide, riboflavine 5'-phosphate, histamine, imidazole, and carbodiimide. 2. The tryptophan groups of the pullulanase were modified by N-bromosuccinimede. It was found that one or two of the 25 tryptophan groups seemed to be important for the activity. 3. Studies on difference spectra using various substrates suggested that the tryptophan groups were important for the formation of an enzyme-substrate complex.

支链淀粉酶[EC 3.2.1.4.]受到Hg2+、N-溴代琥珀酰亚胺、2-羟基-5-硝基苄基溴、核黄素5'-磷酸、组胺、咪唑和碳二亚胺的抑制。2. 支链淀粉酶的色氨酸基团被N-溴代琥珀酰亚胺修饰。发现25个色氨酸基团中的一两个对活性似乎很重要。3. 使用各种底物的差光谱研究表明，色氨酸基团对于酶-底物复合物的形成很重要。