Processing of an intracellular immature pullulanase to the mature form involves enzymatic activation and stabilization in alkaliphilic Bacillus sp. S-1

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dc.contributor.authorMoon Joo Lee-
dc.contributor.authorBong Seok kang-
dc.contributor.authorDong Soo Kim-
dc.contributor.authorYong Tae Kim-
dc.contributor.authorSe Kwon Kim-
dc.contributor.authorKang Hyun Chung-
dc.contributor.authorJune Ki Kim-
dc.contributor.authorKyung Soo Nam-
dc.contributor.authorYoung Choon Lee-
dc.contributor.authorCheorl Ho Kim-
dc.date.accessioned2017-04-19T08:57:44Z-
dc.date.available2017-04-19T08:57:44Z-
dc.date.issued1997-
dc.identifier.issn1225-8687-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/5367-
dc.description.abstractAlkaliphilic Bacillus sp. S-1 secretes a large amount (approximately 80% of total pullulanase activity) of an extracellular pullulanase (PUL-E). The pullulanase exists in two forms: a precursor form (PUL-I: M, 180,000), and a processed form (PUL-E: M, 140,000). Two forms were purified to homogeneity and their properties were compared. PUL-I was different in molecular weight, isoelectric point, NH2-terminal amino acid sequence, and stabilities over pH and temperature ranges. The catalytic activities of PUL-I were also distinguishable in the Km and Vmax values for various substrates, and in the specific activity for pullulan hydrolysis. PUL-E showed 10-fold higher specific activities than PUL-I. However. PUL-I is immunologically identical to PUL-E, suggesting that PUL-I is initially synthesized and proteolytically processed to the mature form of PUL-E. Processing was inhibited by PMSF. but not by pepstatin, suggesting that some intracellular serine proteases could be responsible for processing of the PUL-I. PUL-I has a different conformational structure for antibody recognition from that of PUL-E. It is also postulated that the translocation of alkaline pullulanase (AP) in the bacterium possibly requires processing of the NH2-terminal region of the AP protein. Processing of the precursor involves a conformational shift, resulting in a mature form. Therefore, precursor processing not only cleaves the signal peptide, but also induces conformational shift, allowing development of active form of the enzyme.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleProcessing of an intracellular immature pullulanase to the mature form involves enzymatic activation and stabilization in alkaliphilic Bacillus sp. S-1-
dc.title.alternativeProcessing of an intracellular immature pullulanase to the mature form involves enzymatic activation and stabilization in alkaliphilic Bacillus sp. S-1-
dc.typeArticle-
dc.citation.titleBMB Reports-
dc.citation.number1-
dc.citation.endPage54-
dc.citation.startPage46-
dc.citation.volume30-
dc.contributor.affiliatedAuthorBong Seok kang-
dc.contributor.affiliatedAuthorYoung Choon Lee-
dc.contributor.alternativeName이문주-
dc.contributor.alternativeName강봉석-
dc.contributor.alternativeName김동수-
dc.contributor.alternativeName김용태-
dc.contributor.alternativeName김세권-
dc.contributor.alternativeName정강현-
dc.contributor.alternativeName김준기-
dc.contributor.alternativeName남경수-
dc.contributor.alternativeName이영춘-
dc.contributor.alternativeName김철호-
dc.identifier.bibliographicCitationBMB Reports, vol. 30, no. 1, pp. 46-54-
dc.subject.keywordactivation-
dc.subject.keywordalkaliphilic bacillus sp. S-1-
dc.subject.keywordconformation-
dc.subject.keywordprocessing-
dc.subject.keywordpullulanase-
dc.subject.localActivation-
dc.subject.localactivation-
dc.subject.localalkaliphilic Bacillus sp. S-1-
dc.subject.localalkaliphilic bacillus sp. S-1-
dc.subject.localconformation-
dc.subject.localConformation-
dc.subject.localprocessing-
dc.subject.localProcessing-
dc.subject.localpullulanase-
dc.description.journalClassY-
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