Molecular Enzymology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747AG Groningen, The Netherlands.
Department of Microbiology and Immunology, Faculty of Pharmacy, Cairo University, Kasr El Aini 11562, Cairo, Egypt.
Molecules. 2019 Mar 27;24(7):1208. doi: 10.3390/molecules24071208.
DyP-type peroxidases are heme-containing enzymes that have received increasing attention over recent years with regards to their potential as biocatalysts. A novel DyP-type peroxidase (DyP) was discovered from the alkaliphilic cellulomonad, , which could be overexpressed in . The biochemical characterization of the recombinant enzyme showed that it is a heme-containing enzyme capable to act as a peroxidase on several dyes. With the tested substrates, the enzyme is most active at acidic pH values and is quite tolerant towards solvents. The crystal structure of DyP was solved which revealed atomic details of the dimeric heme-containing enzyme. A peculiar feature of DyP is the presence of a glutamate in the active site which in most other DyPs is an aspartate, being part of the DyP-typifying sequence motif GXXDG. The E201D DyP mutant was prepared and analyzed which revealed that the mutant enzyme shows a significantly higher activity on several dyes when compared with the wild-type enzyme.
DyP 型过氧化物酶是一类含血红素的酶，近年来因其作为生物催化剂的潜力而受到越来越多的关注。从嗜碱纤维单胞菌中发现了一种新型 DyP 型过氧化物酶（DyP），它可以在 中过表达。重组酶的生化特性表明，它是一种含血红素的酶，能够在几种染料上作为过氧化物酶发挥作用。在测试的底物中，该酶在酸性 pH 值下活性最高，对溶剂有很强的耐受性。DyP 的晶体结构已经解决，揭示了二聚血红素酶的原子细节。DyP 的一个特点是活性位点存在谷氨酸，而在大多数其他 DyP 中，谷氨酸是天冬氨酸，是 DyP 典型序列基序 GXXDG 的一部分。制备并分析了 E201D DyP 突变体，结果表明与野生型酶相比，该突变体在几种染料上的活性显著提高。
