Earticle

초록

영어

The SGNH superfamily is characterized by four highly conserved sequence blocks containing serine (S), glycine (G) asparagines (N), and histidine (H) residues, each of which is incorporated in active sites or oxyanion holes. High specificities of SGNH hydrolases could compounds and enantiomeric resolutions. Here, a novel SGNH hydrolase (BG42) from Burkhoderia glumae, which has a SGNH fold (Ser184, Thr266(Asn), His369) in its C-terminal domain, was expressed, purified, and characterized using biochemical and biophysical methods. A sequence comparison of BG42 with other SGNH members confirmed the presence of catalytic triad. The wild type enzyme was able to hydrolyzed p-nitrophenyl acetate, α-and β-naphthyl acetate. Structural and functional properties of BG42 were investigated using circular dichroism (CD), fluorescence, dynamic light scattering (DLS), electron microscopy (EM), and time of flight (TOF) mass spectrometry with site-directed mutagenesis. Sitedirected mutagenesis and crystallographic analysis is currently under progress for its industrial applications.

키워드

저자

• Song Yi BAE [ Department of Molecular Science and Technology Graduate School of Interdiscipliny program, Ajou University, Suwon, South Korea 443-749. ]
• Seul-Gi KIM [ Department of Molecular Science and Technology Graduate School of Interdiscipliny program, Ajou University, Suwon, South Korea 443-749. ]
• Nam Yong KIM [ Department of Molecular Science and Technology Graduate School of Interdiscipliny program, Ajou University, Suwon, South Korea 443-749. ]
• So Hyun PARK [ Department of Molecular Science and Technology Graduate School of Interdiscipliny program, Ajou University, Suwon, South Korea 443-749. ]
• T. Doohun KIM [ Department of Molecular Science and Technology Graduate School of Interdiscipliny program, Ajou University, Suwon, South Korea 443-749. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576