DC Field | Value | Language |
---|---|---|
dc.contributor.author | Moon Joo Lee | - |
dc.contributor.author | Bong Seok kang | - |
dc.contributor.author | Dong Soo Kim | - |
dc.contributor.author | Yong Tae Kim | - |
dc.contributor.author | Se Kwon Kim | - |
dc.contributor.author | Kang Hyun Chung | - |
dc.contributor.author | June Ki Kim | - |
dc.contributor.author | Kyung Soo Nam | - |
dc.contributor.author | Young Choon Lee | - |
dc.contributor.author | Cheorl Ho Kim | - |
dc.date.accessioned | 2017-04-19T08:57:44Z | - |
dc.date.available | 2017-04-19T08:57:44Z | - |
dc.date.issued | 1997 | - |
dc.identifier.issn | 1225-8687 | - |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/5367 | - |
dc.description.abstract | Alkaliphilic 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.publisher | Korea Soc-Assoc-Inst | - |
dc.title | Processing of an intracellular immature pullulanase to the mature form involves enzymatic activation and stabilization in alkaliphilic Bacillus sp. S-1 | - |
dc.title.alternative | Processing of an intracellular immature pullulanase to the mature form involves enzymatic activation and stabilization in alkaliphilic Bacillus sp. S-1 | - |
dc.type | Article | - |
dc.citation.title | BMB Reports | - |
dc.citation.number | 1 | - |
dc.citation.endPage | 54 | - |
dc.citation.startPage | 46 | - |
dc.citation.volume | 30 | - |
dc.contributor.affiliatedAuthor | Bong Seok kang | - |
dc.contributor.affiliatedAuthor | Young Choon Lee | - |
dc.contributor.alternativeName | 이문주 | - |
dc.contributor.alternativeName | 강봉석 | - |
dc.contributor.alternativeName | 김동수 | - |
dc.contributor.alternativeName | 김용태 | - |
dc.contributor.alternativeName | 김세권 | - |
dc.contributor.alternativeName | 정강현 | - |
dc.contributor.alternativeName | 김준기 | - |
dc.contributor.alternativeName | 남경수 | - |
dc.contributor.alternativeName | 이영춘 | - |
dc.contributor.alternativeName | 김철호 | - |
dc.identifier.bibliographicCitation | BMB Reports, vol. 30, no. 1, pp. 46-54 | - |
dc.subject.keyword | activation | - |
dc.subject.keyword | alkaliphilic bacillus sp. S-1 | - |
dc.subject.keyword | conformation | - |
dc.subject.keyword | processing | - |
dc.subject.keyword | pullulanase | - |
dc.subject.local | Activation | - |
dc.subject.local | activation | - |
dc.subject.local | alkaliphilic Bacillus sp. S-1 | - |
dc.subject.local | alkaliphilic bacillus sp. S-1 | - |
dc.subject.local | conformation | - |
dc.subject.local | Conformation | - |
dc.subject.local | processing | - |
dc.subject.local | Processing | - |
dc.subject.local | pullulanase | - |
dc.description.journalClass | Y | - |
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