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Title 

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

Authors 

Moon Joo LeeBong Seok kangDong Soo KimYong Tae KimSe Kwon KimKang Hyun ChungJune Ki KimKyung Soo NamYoung Choon LeeCheorl Ho Kim

Publisher 

Springer Verlag (Germany)

Issue Date 

1997

Citation 

Journal of Biochemistry and Molecular Biology, vol. 30, no. 1, pp. 46-54

Keywords 

activationalkaliphilic bacillus sp. S-1conformationprocessingpullulanase

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.

ISSN 

1225-8687

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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