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Putative Role of a Streptomyces Coelicolor-Derived α-mannosidase in Deglycosylation and Antibiotic Production

Putative Role of a Streptomyces Coelicolor-Derived α-mannosidase in Deglycosylation and Antibiotic Production

Thangamani Rajesh, Jong-Min Jeon, Eunjung Song, Hae-Min Park, Hyung Min Seo, Hyun-Joong Kim, Da-Hye Yi, Yong-Hyun Kim, Kwon-Young Choi, Yun-Gon Kim, Hyung-Yeon Park, Yoo Kyung Lee, Yung-Hun Yang

Appl Biochem Biotechnol. 2014 Feb;172(3):1639-51.

PMID: 24242072

Abstract:

SCO0948 was found to be the single open reading frame annotated to encode an α-mannosidase (AM1) in Streptomyces coelicolor M145. To characterize the protein, we overexpressed SCO0948 in Escherichia coli BL21(DE3). Recombinant AM1, with a molecular weight of 110 kDa, exhibited α-mannosidase activity toward 4-nitrophenyl-α-D-mannopyranoside with a K m of 4.61 mM, a V(max) of 101.6 mM/min, and a specific activity of 47.96 U/mg. Treatment of ovalbumin, a glycoprotein, with AM1 resulted in partial deglycosylation, as assessed by glycostaining and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The S. coelicolor deletion mutant for SCO0948 failed to produce α-mannosidase activity, confirming AM1 as the only α-mannosidase in S. coelicolor M145. Interestingly, the deletion mutant and a complementation strain produced lower levels of the antibiotics actinorhodin and undecylprodigiosin in glucose minimal media. The results indicate that AM1 as an α-mannosidase influences deglycosylation and antibiotic production in S. coelicolor M145.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP10357274	4-Nitrophenyl α-D-mannopyranoside		10357-27-4	Price

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