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
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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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
Journal: Biochimie - Volume 102, July 2014, Pages 37-46
نویسندگان
France Boonen, Anne-Michèle Vandamme, Emilie Etoundi, Lise-Marie Pigneur, Isabelle Housen,