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[泡盛曲霉糖化淀粉酶的活性中心]

[Active center of glycoamylase from Aspergillus awamori].

作者信息

Sergeevv V R, Firsov L M, Savelyev A N

出版信息

Biokhimiia. 1982 Mar;47(3):390-7.

PMID:6803848
Abstract

The maltooligosaccharides--triose, tetrose, pentose and hexose have been obtained by fractionation of partially hydrolyzed cyclohexamylose. The values of free energies for the binding of the first six sites of glucose residue binding in the enzyme active center were calculated according to the Hiromi model and were found to be equal to -0.6, -4.5, -1.68, -0.66, -0.25 and +-0.06 kcal/mole, respectively. The Hiromi model was extrapolated to p-nitrophenyl-alpha-D-glucoside, p-nitrophenyl-alpha-D-maltoside and methyl-alpha-D-glucoside. The energies for nitrophenol binding for the second, third and fourth centers and of the methyl group binding for the second and third centers were determined. The value of universal catalytic constant kcat is equal to 47.9 s-1 at 37 degrees.

摘要

麦芽低聚糖(丙糖、丁糖、戊糖和己糖)是通过对部分水解的环糊精进行分级分离得到的。根据弘美模型计算了酶活性中心葡萄糖残基结合的前六个位点的结合自由能值,发现分别等于-0.6、-4.5、-1.68、-0.66、-0.25和±0.06千卡/摩尔。弘美模型被外推到对硝基苯基-α-D-葡萄糖苷、对硝基苯基-α-D-麦芽糖苷和甲基-α-D-葡萄糖苷。测定了第二、第三和第四中心的硝基苯酚结合能以及第二和第三中心的甲基结合能。通用催化常数kcat在37摄氏度时的值等于47.9 s-1。

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1
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