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Charaterization of a novel SGNH family member from Xanthomonas axonopodis pv

원문정보

Namyong KIM, Seulgi KIM, Song Yi BAE, So Hyun PARK, T. Doohun KIM

한국생물공학회 한국생물공학회 학술대회 2010 추계학술대회 및 국제심포지움 2010.10 pp.182-182
피인용수 : 0건 (자료제공 : 네이버학술정보)

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

저자정보

  • 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.

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자료제공 : 네이버학술정보

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