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基于人血清白蛋白的过氧化物酶,在人工血红素口袋中具有铁原卟啉 IX。

Human serum albumin-based peroxidase having an iron protoporphyrin IX in artificial heme pocket.

机构信息

Department of Applied Chemistry, Faculty of Science and Engineering, Chuo University, 1-13-27 Kasuga, Bunkyo-ku, Tokyo 112-8551, Japan.

出版信息

Chem Asian J. 2012 Nov;7(11):2534-7. doi: 10.1002/asia.201200373. Epub 2012 Aug 21.

Abstract

Cooking up enzymes: Iron protoporphyrin IX (heme) is bound within a hydrophobic cavity in subdomain IB of human serum albumin (HSA). Site-specific mutations to introduce proximal and distal histidines into the heme pocket of HSA conferred a peroxidase activity to the prosthetic heme group. The catalytic activity of the recombinant HSA(mutant)-heme complex for guaiacol oxidation is 17-fold higher than that of HSA(wild type)-heme.

摘要

酶的制备

亚铁原卟啉 IX(血红素)结合在人血清白蛋白(HSA)亚结构域 IB 的疏水腔中。对 HSA 血红素口袋中引入近端和远端组氨酸的定点突变赋予了血红素辅基过氧化物酶活性。重组 HSA(突变)-血红素复合物对愈创木酚氧化的催化活性比 HSA(野生型)-血红素高 17 倍。

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