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| Type |
Poster Presentation |
| Area |
생명화학 |
| Room No. |
포스터발표장 |
| Time |
4월 21일 (금요일) 13:00~14:30 |
| Code |
BIO.P-309 |
| Subject |
In situ simulation of pfEstA, a novel family VIII carboxylesterase, from Pseudomonas fluorescens KCTC 1767: a predictions of substrate selectivity through molecular modeling |
| Authors |
유완기, 김부영1, Wang Ying1, 김두헌2,*
성균관대학교 의과대학, Korea
1숙명여자대학교 화학과, Korea
2숙명여자대학교 이과대학 화학과, Korea
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| Abstract |
pfEstA, a novel family VIII carboxylesterase, is identified and analyzed in this study. Multiple sequence alignment and phylogenetic analysis confirmed that pfEstA is a member of family VIII carboxylesterase and a putative catalytic triad (Ser79-Lys82-Tyr168). Here, pfEstA was compared with other enzymes of the same family and Class-C β-lactamases which were retrieved from BLAST and DALI server. The computation simulation analysis of pfEstA with cephalothin and the result from hydrolysis of nitrocefin indicated that pfEstA would have little or no activity for hydrolysis of bulky β-lactam antibiotics. Structural analysis with other related enzymes and mutational study suggested that the structural individuality in the catalytic pocket elucidates the substrates selectivity of pfEstA rather than specific interaction between residues and substrates. |
| E-mail |
vlqkshqk61@outlook.kr |
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119th General Meeting of the KCS