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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
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- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제25권 제1호
- 발행연도
- 2015.1
- 수록면
- 44 - 49 (6page)
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초록· 키워드
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Thermostable enzymes derived from Thermotoga maritima have attracted worldwide interest for their potential industrial applications. Structural analysis and docking studies were preformed on T. maritima β-glucosidase enzyme with cellobiose and pNP-linked substrates. The 3D structure of the thermostable β-glucosidase was downloaded from the Protein Data Bank database. Substrates were downloaded from the PubCehm database and were minimized using MOE software. Docking of BglA and substrates was carried out using MOE software. After analyzing docked enzyme/substrate complexes, it was found that Glu residues were mainly involved in the reaction, and other important residues such as Asn, Ser, Tyr, Trp, and His were involved in hydrogen bonding with pNP-linked substrates. By determining the substrate recognition pattern, a more suitable β-glucosidase enzyme could be developed, enhancing its industrial potential.
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참고문헌 (15)
참고문헌 신청
Afzal A / 2005 / Innovative kinetic and thermodynamic studies of a purified superactive xylanase from Scopulariopsis sp / Appl. Biochem. Biotechnol 120 : 51 ~ 70
Bhatia Y / 2002 / Microbial betaglucosidases:cloning, properties, and applications / Crit. Rev. Biotechnol 22 : 375 ~ 407
Gloster TM / 2007 / Structural basis for cyclophellitol inhibition of a beta-glucosidase / Org. Biomol. Chem 5 : 444 ~ 446
Haq I / 2012 / Cloning, characterization and molecular docking of a highly thermostable β-1,4-glucosidase from Thermotoga petrophila / Biotechnol. Lett 34 : 1703 ~ 1709
Ketudat Cairns JR / 2010 / Beta-glucosidases / Cell Mol. Life Sci 67 : 3389 ~ 3405
Bhatia Y / 2002 / Microbial betaglucosidases:cloning, properties, and applications / Crit. Rev. Biotechnol 22 : 375 ~ 407
Gloster TM / 2007 / Structural basis for cyclophellitol inhibition of a beta-glucosidase / Org. Biomol. Chem 5 : 444 ~ 446
Haq I / 2012 / Cloning, characterization and molecular docking of a highly thermostable β-1,4-glucosidase from Thermotoga petrophila / Biotechnol. Lett 34 : 1703 ~ 1709
Ketudat Cairns JR / 2010 / Beta-glucosidases / Cell Mol. Life Sci 67 : 3389 ~ 3405
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