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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제21권 제6호
- 발행연도
- 2011.1
- 수록면
- 617 - 626 (10page)
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초록· 키워드
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Transglutaminase from Streptomyces mobaraensis is an enzyme of unknown function that cross-links proteins to high molecular weight aggregates. Previously, we characterized two intrinsic transglutaminase substrates with inactivating activities against subtilisin and dispase. This report now describes a novel substrate that inhibits papain, bromelain,and trypsin. Papain was the most sensitive protease; thus,the protein was designated Streptomyces papain inhibitor (SPI). To avoid transglutaminase-mediated glutamine deamidation during culture, SPI was produced by Streptomyces mobaraensis at various growth temperatures. The best results were achieved by culturing for 30-50 h at 42℃,which yielded high SPI concentrations and negligibly small amounts of mature transglutaminase. Transglutaminasespecific biotinylation displayed largely unmodified glutamine and lysine residues. In contrast, purified SPI from the 28℃culture lost the potential to be cross-linked, but exhibited higher inhibitory activity as indicated by a significantly lower K_i (60 nM vs. 140 nM). Despite similarities in molecular mass (12 kDa) and high thermostability, SPI exhibits clear differences in comparison with all members of the wellknown family of Streptomyces subtilisin inhibitors. The neutral protein (pI of 7.3) shares sequence homology with a putative protein from Streptomyces lavendulae, whose conformation is most likely stabilized by two disulfide bridges. However, cysteine residues are not localized in the typical regions of subtilisin inhibitors. SPI and the formerly characterized dispase-inactivating substrate are unique proteins of distinct Streptomycetes such as Streptomyces mobaraensis. Along with the subtilisin inhibitory protein,they could play a crucial role in the defense of vulnerable protein layers that are solidified by transglutaminase.
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참고문헌 (24)
참고문헌 신청
Ando, H / 1989 / Purification and characteristics of a novel transglutaminase derived from microorganisms / Agric. Biol. Chem 53 : 2613 ~ 2617
Bah, S / 2006 / Characterization of cysteine proteases in Malian medicinal plants / J. Ethnopharmacol 107 : 189 ~ 198
Bentley, S. D / 2002 / Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2) / Nature 417 : 141 ~ 147
Blackman, M. J / 2008 / Malarial proteases and host cell egress: An ‘emerging’ cascade / Cell. Microbiol 10 : 1925 ~ 1934
Bromme, D / 2004 / Production and activation of recombinant papain-like cysteine proteases / Methods 32 : 199 ~ 206
Bah, S / 2006 / Characterization of cysteine proteases in Malian medicinal plants / J. Ethnopharmacol 107 : 189 ~ 198
Bentley, S. D / 2002 / Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2) / Nature 417 : 141 ~ 147
Blackman, M. J / 2008 / Malarial proteases and host cell egress: An ‘emerging’ cascade / Cell. Microbiol 10 : 1925 ~ 1934
Bromme, D / 2004 / Production and activation of recombinant papain-like cysteine proteases / Methods 32 : 199 ~ 206
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