Crystal structures of dye- decolorizing peroxidase with ascorbic acid and2,6-dimethoxyphenol.
Crystal structures of dye- decolorizing peroxidase with ascorbic acid and2,6-dimethoxyphenol.
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抗坏血酸和2,6-二甲氧基苯酚染料脱色过氧化物酶的晶体结构。
DOI：
10.1016/j.febslet.2012.10.049
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
Sugano Y.
中科院分区：
文献类型：
--
作者：
Yoshida T;Tsuge H;Hisabori T;Sugano Y.
染料脱色过氧化物酶（DyP）型过氧化物酶的结构不同于其他过氧化物酶家族，表明DyP型过氧化物酶具有不同的反应机制。我们分别用抗坏血酸和2，6-二甲氧基苯酚在1.5 ℃和1.4 ℃下测定了DyP的晶体结构。两种底物的共同结合位点位于从DyP分子表面到血红素的第二空腔的入口处。这导致每个底物和血红素远端侧之间的氢键网络连接。这个网络由占据第二个空腔的水分子、血红素6-丙酸酯、Arg 329和Asn 313组成。该网络与从底物到DyP的质子转移途径一致。
The structure of dye-decolorizing peroxidase (DyP)-type peroxidase differs from that of other peroxidase families, indicating that DyP-type peroxidases have a different reaction mechanism. We have determined the crystal structures of DyP with ascorbic acid and 2,6-dimethoxyphenol at 1.5 and 1.4Å, respectively. The common binding site for both substrates was located at the entrance of the second cavity leading from the DyP molecular surface to heme. This resulted in a hydrogen bond network connection between each substrate and the heme distal side. This network consisted of water molecules occupying the second cavity, heme 6-propionate, Arg329, and Asn313. This network is consistent with the proton transfer pathway from substrate to DyP.