Earticle

초록

영어

The SG(A)NH superfamily is characterized by four highly conserved sequence blocks containing serine (S), alanine (A), asparagine (N), and histidine (H) residues, each of which is incorporated in active sites or oxyanion holes. High specificities of SG(A)NH hydrolases could be used for the preparations of chiral compounds and enantiomeric resolutions. Here, a novel SG(A)NH hydrolase (XAC833) from Xanthomonas axonopodis pv, which has a SANH fold (Ser34, Ala68, Asn51, His135) was expressed, purified, and characterized using biochemical and biophysical methods. A sequence comparison of XAC833 with other SG(A)NH members confirmed the presence of a catalytic triad and functionally important amino acids. The wild type enzyme was able to hydrolyzed p-nitrophenyl acetate, p-nitrophenyl butyrate and p-nitrophenyl valerate. Structural and functional properties of XAC833 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. Site-directed mutagenesis and crystallographic analysis is currently under progress for its industrial applications.

키워드

저자

• Namyong KIM [ Dept, of Molecular Science and Technology, Ajou University,Suwon, 443-749. ]
• Seulgi KIM [ Dept, of Molecular Science and Technology, Ajou University,Suwon, 443-749. ]
• Song Yi BAE [ Dept, of Molecular Science and Technology, Ajou University,Suwon, 443-749. ]
• So Hyun PARK [ Dept, of Molecular Science and Technology, Ajou University,Suwon, 443-749. ]
• T. Doohun KIM [ Dept, of Molecular Science and Technology, Ajou University,Suwon, 443-749. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576