کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
8305267 1538428 2014 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Identification and characterization of a novel multicopper oxidase from Acidomyces acidophilus with ferroxidase activity
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Identification and characterization of a novel multicopper oxidase from Acidomyces acidophilus with ferroxidase activity
چکیده انگلیسی
A new multicopper oxidase gene AaMco1 was identified in Acidomyces acidophilus, a pigmented extremophile ascomycete originally isolated from acidic water. Sequence analysis revealed that it encodes a 682 amino acid protein with an apparent molecular mass of 85 kDa as determined by denaturing SDS-PAGE. Interestingly, AaMco1 has a predicted N-terminal transmembrane helix and no signal peptide. To obtain an active and soluble protein, AaMco1 was truncated at its N-terminal to remove the transmembrane helix, but even in this form the protein was found in the insoluble fraction. AaMco1 and its truncated form were then denatured, purified and renatured before characterization. Structural analysis and protein characterization by enzymatic assays indicate that AaMco1 has ferroxidase activity. AaMco1 is also able to oxidize the DMPPDA compound and could be part of a new phylogenetic cluster, the ascomycete MCOs family, described for the first time here.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimie - Volume 102, July 2014, Pages 37-46
نویسندگان
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