Putative Role of a Streptomyces coelicolor-Derived alpha-Mannosidase in Deglycosylation and Antibiotic Production
- Authors
- 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
- Issue Date
- Feb-2014
- Publisher
- HUMANA PRESS INC
- Keywords
- Streptomyces coelicolor; alpha-Mannosidase; Deglycosylation; Antibiotic production
- Citation
- APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, v.172, no.3, pp.1639 - 1651
- Journal Title
- APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
- Volume
- 172
- Number
- 3
- Start Page
- 1639
- End Page
- 1651
- URI
- http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/10132
- DOI
- 10.1007/s12010-013-0635-y
- ISSN
- 0273-2289
- Abstract
- SCO0948 was found to be the single open reading frame annotated to encode an alpha-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 alpha-mannosidase activity toward 4-nitrophenyl-alpha-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 a-mannosidase activity, confirming AM1 as the only alpha-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 alpha-mannosidase influences deglycosylation and antibiotic production in S. coelicolor M145.
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