MECHANISM OF URICASE ACTION

被引：31

作者：

BONGAERTS, GPA ^{[1
]}

VOGELS, GD ^{[1
]}

机构：

[1] CATHOLIC UNIV NIJMEGEN,SCI UNIT,DEPT MICROBIOL,NIJMEGEN,NETHERLANDS

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 567卷 / 02期

关键词：

Allantoin; Stereospecificity; Uricase mechanism;

D O I：

10.1016/0005-2744(79)90115-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Uricase (urate:oxygen oxidoreductase, EC 1.7.3.3.) exposes a positional and steric specificity in the enzymic conversion of urate to allantoin. C-2 of urate was recovered as C-2 of allantoin. By the consecutive oxidation and hydrolysis reactions a levorotatory intermediate was formed, presumably (-)-2-oxo-4-hydroxy-4-carbohydroxy-5-ureido-imidazoline. The absorption and optical rotation dispersion spectra of the intermediate were established. In the presence of borate buffer, the intermediate was transformed to (+)-alloxanate. The decay of the former compound depends on general base and acid catalysis. RS-(±)-allantoin was formed by chemical decarboxylation and S-(+)-allantoin by enzymic decarboxylation. © 1979.

引用

页码：295 / 308

页数：14