دورية أكاديمية

GfsA is a β1,5-galactofuranosyltransferase involved in the biosynthesis of the galactofuran side chain of fungal-type galactomannan in Aspergillus fumigatus.

التفاصيل البيبلوغرافية
العنوان: GfsA is a β1,5-galactofuranosyltransferase involved in the biosynthesis of the galactofuran side chain of fungal-type galactomannan in Aspergillus fumigatus.
المؤلفون: Yukako Katafuchi, Qiushi Li, Yutaka Tanaka, Saki Shinozuka, Yohei Kawamitsu, Minoru Izumi, Keisuke Ekino, Keiji Mizuki, Kaoru Takegawa, Nobuyuki Shibata, Masatoshi Goto, Yoshiyuki Nomura, Kazuyoshi Ohta, Takuji Oka
المصدر: Glycobiology; Jun2017, Vol. 27 Issue 6, p568-581, 14p
مصطلحات موضوعية: ASPERGILLUS fumigatus, BIOSYNTHESIS, GALACTOMANNANS, AMADORI compounds, BIOCHEMISTRY
مستخلص: Previously, we reported that GfsA is a novel galactofuranosyltransferase involved in the biosynthesis of O-glycan, the proper maintenance of fungal morphology, the formation of conidia and anti-fungal resistance in Aspergillus nidulans and A. fumigatus (Komachi Y et al., 2013. GfsA encodes a novel galactofuranosyltransferase involved in biosynthesis of galactofuranose antigen of O-glycan in Aspergillus nidulans and Aspergillus fumigatus. Mol. Microbiol. 90:1054-1073). In the present paper, to gain an in depth-understanding of the enzymatic functions of GfsA in A. fumigatus (AfGfsA), we established an in vitro assay to measure galactofuranosyltransferase activity using purified AfGfsA, UDP-α-D-galactofuranose as a sugar donor, and p-nitrophenyl-β-Dgalactofuranoside as an acceptor substrate. LC/MS, 1H-NMR and methylation analyses of the enzymatic products of AfGfsA revealed that this protein has the ability to transfer galactofuranose to the C-5 position of the β-galactofuranose residue via a β-linkage. AfGfsA requires a divalent cation of manganese for maximal activity and consumes UDP-α-D-galactofuranose as a sugar donor. Its optimal pH range is 6.5-7.5 and its optimal temperature range is 20-30°C. 1H-NMR, 13C-NMR and methylation analyses of fungal-type galactomannan extracted from the ΔAfgfsA strain revealed that AfGfsA is responsible for the biosynthesis of β1,5-galactofuranose in the galactofuran side chain of fungal-type galactomannan. Based on these results, we conclude that AfGfsA acts as a UDP-α-D-galactofuranose: β-D-galactofuranoside β1,5-galactofuranosyltransferase in the biosynthetic pathway of galactomannans. [ABSTRACT FROM AUTHOR]
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قاعدة البيانات: Complementary Index
الوصف
تدمد:09596658
DOI:10.1093/glycob/cwx028