119th General Meeting of the KCS

Type Poster Presentation
Area 생명화학
Room No. 포스터발표장
Time 4월 21일 (금요일) 13:00~14:30
Code BIO.P-308
Subject Characterization of a novel SGNH hydrolase (Nm21) from Neisseria meningitidis 053442
Authors 유완기, 김부영1, Wang Ying1, 김두헌2,*
성균관대학교 의과대학, Korea
1숙명여자대학교 화학과, Korea
2숙명여자대학교 이과대학 화학과, Korea
Abstract Nm21, a novel SGNH-hydrolase from Neisseria meningitidis 053442 was identified, purified, and characterized by biochemical and biophysical methods. Multiple sequence alignment of Nm21 with other SGNH family member proteins confirmed a putative catalytic triad (Ser29-Asp169-His172), and conserved sequence motif of Ser(S)29-Gly (G)87-Asn (N)89-His(H)172. In this paper, biochemical properties of Nm21 were studied with fluorescence analysis, dynamic light scattering (DLS), electron microscopy, and time of flight (TOF) mass spectrometry. It was found that Leu92 residue neighboring catalytic cavity is responsible for stabilization of hydrophobic moiety in substrates, while at the same time it hinders the pathway of bulky substrates to get in the active-site pocket. At last, immobilization of Nm21 exhibited good durability after repeated usages and improved catalytic efficiency. Collectively, this study emphasizes a potential of Nm21 as a biocatalyst in the pharmaceutical and chemical industries and provide a deeper insight at substrate specificity of SGNH-hydrolase.
E-mail vlqkshqk61@outlook.kr