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Rajesh, Thangamani; Jeon, Jong-Min; Song, Eunjung; Park, Hae-Min; Seo, Hyung Min; Kim, Hyun-Joong; Yi, Da-Hye; Kim, Yong-Hyun; Choi, Kwon-Young; Kim, Yun-Gon; Park, Hyung-Yeon; Lee, Yoo Kyung; Yang, Yung-Hun
Applied biochemistry and biotechnology, 02/2014, Volume: 172, Issue: 3Journal Article
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.
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