Characterization and Bioinformatics Analysis of C-4 Sterol Methyl Oxidase from Monascus purpureus

Jiang Ning Yao; Nan Qing Liao; Hao Ming Li

doi:10.4028/www.scientific.net/AMM.522-524.247

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HomeApplied Mechanics and MaterialsApplied Mechanics and Materials Vols. 522-524Characterization and Bioinformatics Analysis of...

Characterization and Bioinformatics Analysis of C-4 Sterol Methyl Oxidase from Monascus purpureus

Abstract:

A gene encoding a putative C-4 sterol methyl oxidase was obtained by screening Monascus purpureus cDNA library. Bioinformatics analysis showed that this protein has a primary structure, a hydrophobicity profile and a pattern of histidine-rich motifs which are typical of C-4 methyl sterol oxidases. The deduced C-4 sterol methyl oxidase protein of M. purpureus contained 259 amino acid, with molecular mass of 30,299Da. Sequence alignment analysis revealed that M. purpureus deduced C-4 sterol methyl oxidase was closely related to C-4 sterol methyl oxidase from Aspergillus, Penicillium and Byssochlamys, and highly homologous to aforementioned and other known C-4 sterol methyl oxidase. The deduced protein is of a membrane protein with two transmembrane helices, which belongs to the fatty acid hydroxylase superfamily. The consistency of the comparison results of the primary structure, secondary structure and physicochemical properties suggests that the dedued protein may well be C-4 sterol methyl oxidase.

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Periodical:

Applied Mechanics and Materials (Volumes 522-524)

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247-250

DOI:

https://doi.org/10.4028/www.scientific.net/AMM.522-524.247

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Online since:

February 2014

Authors:

Jiang Ning Yao, Nan Qing Liao, Hao Ming Li*

Keywords:

Bioinformatics Analysis, C-4 Sterol Methyl Oxidase, Monascus purpureus

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* - Corresponding Author

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