|
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 |
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