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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제25권 제7호
- 발행연도
- 2015.1
- 수록면
- 1,070 - 1,083 (14page)
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초록· 키워드
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A gene (GT-SM3B) encoding a thermostable secreted oligoendopeptidase (GT-SM3B) was cloned from the thermophile Geobacillus thermoleovorans DSM 15325. GT-SM3B is 1,857 bp in length and encodes a single-domain protein of 618 amino acids with a 23-residue signal peptide having a calculated mass of 67.7 kDa after signal cleavage. The deduced amino acid sequence of GT-SM3B contains a conservative zinc metallopeptidase motif (His400-Glu401-X-XHis 404). The described oligopeptidase belongs to the M3B subfamily of metallopeptidases and displays the highest amino acid sequence identity (40.3%) to the oligopeptidase PepFBa from mesophilic Bacillus amyloliquefaciens 23-7A among the characterized oligopeptidases. Secretory production of GT-SM3B was used, exploiting successful oligopeptidase signal peptide recognition by Escherichia coli BL21 (DE3). The recombinant enzyme was purified from the culture fluid. Homodimerization of GT-SM3B was determined by SDS-PAGE. Both the homodimer and monomer were catalytically active within a pH range of 5.0–8.0, at pH 7.3 and 40°C, showing the Km, Vmax, and kcat values for carbobenzoxy-Gly-Pro-Gly-Gly-Pro-Ala-OH peptidolysis to be 2.17 ± 0.04 × 10-6 M, 2.65 ± 0.03 × 10-3 μM/min, and 5.99 ± 0.07 s-1, respectively. Peptidase remained stable at a broad pH range of 5.0–8.0. GT-SM3B was thermoactive, demonstrating 84% and 64% of maximum activity at 50°C and 60°C, respectively. The recombinant oligopeptidase is one of the most thermostable M3B peptidase, retaining 71% residual activity after incubation at 60°C for 1 h. GT-SM3B was shown to hydrolyze a collagenous peptide mixture derived from various types of collagen, but less preferentially than synthetic hexapeptide. This study is the first report on an extracellular thermostable metallo-oligopeptidase.
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참고문헌 (24)
참고문헌 신청
Agarwal V / 2013 / Streptococcus pneumoniae endopeptidase O (PepO) is a multifunctional plasminogen- and fibronectinbinding protein, facilitating evasion of innate immunity a
Akiyama K / 1999 / Cloning and sequencing of the Pz-peptidase gene from Bacillus licheniformis N22 / J. Biosci. Bioeng 87 : 231 ~ 233
Ansai T / 2003 / Construction of a pepO gene-deficient mutant of Porphyromonas gingivalis: potential role of endopeptidase O in the invasion of host cells / Oral Microbiol. I
Asdornnithee S / 1995 / Isolation and characterization of Pz-peptidase from Bacillus licheniformis N22 / J. Ferment. Bioeng 79 : 200 ~ 204
Awano S / 1999 / Sequencing, expression and biochemical characterization of the Porphyromonas gingivalis pepO gene encoding a protein homologous to human endothelinconverting
Akiyama K / 1999 / Cloning and sequencing of the Pz-peptidase gene from Bacillus licheniformis N22 / J. Biosci. Bioeng 87 : 231 ~ 233
Ansai T / 2003 / Construction of a pepO gene-deficient mutant of Porphyromonas gingivalis: potential role of endopeptidase O in the invasion of host cells / Oral Microbiol. I
Asdornnithee S / 1995 / Isolation and characterization of Pz-peptidase from Bacillus licheniformis N22 / J. Ferment. Bioeng 79 : 200 ~ 204
Awano S / 1999 / Sequencing, expression and biochemical characterization of the Porphyromonas gingivalis pepO gene encoding a protein homologous to human endothelinconverting
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