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|
| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Grand Ballroom |
| Time |
10월 19일 (금요일) 11:00~12:30 |
| Code |
LIFE.P-451 |
| Subject |
Characterization of a novel penicillin-binding protein from Lactobacillus acidophilus NCFM
|
| Authors |
Ly Thi Huong Luu Le, Doo Hun Kim*
Department of Chemistry, Sookmyung Women's University, Korea
|
| Abstract |
A novel penicillin-binding protein, LaPBP from Lactobacillus acidophilus NCFM, which is composed of 364 amino acids with a molecular mass of 41 kDa, was identified, expressed and characterized. LaPBP displayed a significant sequence similarity with 1SDE, a hydrolases from Streptomyces strain R61. Further sequence analysis of LaPBP revealed a conserved of S-X-X-K motif and a putative catalytic triad of Ser85-Lys88-Tyr174. LaPBP hydrolyzed short-chain esters such as p-nitrophenyl acetate, butyrate. Finally, β-lactamase activity of LaPBP was investigated. Taken together, this study will contribute to improve our understanding, providing useful information in sequence, biophysical properties and catalytic activity into penicillin-binding proteins family. |
| E-mail |
ly.12000532@gmail.com |
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122nd General Meeting of the KCS