来自金色链霉菌的无金属离子氧化还原酶具有α/β水解酶折叠结构。
The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold.
作者信息
Hecht H J, Sobek H, Haag T, Pfeifer O, van Pée K H
机构信息
GBF (Gesellschaft für Biotechnologische Forschung), Department of Molecular Structure Research, Braunschweig, Germany.
出版信息
Nat Struct Biol. 1994 Aug;1(8):532-7. doi: 10.1038/nsb0894-532.
The crystal structure of the bromoperoxidase A2 from Streptomyces aureofaciens (ATCC 10762) has been determined by isomorphous replacement and refined to 2.05 A resolution with an R-value of 18.4%. The enzyme catalyzes the bromination of organic compounds in the presence of bromide and peroxide. The structure confirms the absence of cofactors such as metal ions or haem groups and shows the general topology of the alpha/beta hydrolase fold. The active centre is at the end of a deep pocket and includes a catalytic triad of Ser 98, Asp 228 and His 257. The active centre is connected by a narrow tunnel to a second pocket on the enzyme surface.
来自金色链霉菌（ATCC 10762）的溴过氧化物酶A2的晶体结构已通过同晶置换法确定，并精修至2.05埃分辨率，R值为18.4%。该酶在溴化物和过氧化物存在的情况下催化有机化合物的溴化反应。该结构证实不存在金属离子或血红素基团等辅因子，并显示出α/β水解酶折叠的一般拓扑结构。活性中心位于一个深口袋的末端，包括由Ser 98、Asp 228和His 257组成的催化三联体。活性中心通过一条狭窄的通道与酶表面的第二个口袋相连。
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