Comparison of the antibacterial properties of phage endolysins SAL-1 and LysK.
In spite of the high degree of amino acid sequence similarity between the newly discovered phage endolysin SAL-1 and the phage endolysin LysK, SAL-1 has an approximately 2-fold-lower MIC against several Staphylococcus aureus strains and higher bacterial cell-wall-hydrolyzing activity than LysK. The amino acid residue change contributing the most to this enhanced enzymatic activity is a change from glutamic acid to glutamine at the 114th residue.
iNtRON Biotechnology, Inc., Room 703, JungAng Induspia V, 138-6, Sangdaewon-dong, Jungwon-gu, Seongnam-si, Gyeonggi-do 462-120, Republic of Korea.
Soo Youn
SY
Jun
Gi Mo
GM
Jung
Jee-Soo
JS
Son
Seong Jun
SJ
Yoon
Yun-Jaie
YJ
Choi
Sang Hyeon
SH
Kang
D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000494:pharmacology*; D002473:Cell Wall / Q000187:drug effects; D010450:Endopeptidases / Q000737:chemistry / Q000494:pharmacology*; D008826:Microbial Sensitivity Tests; D013211:Staphylococcus aureus / Q000187:drug effects*
D000900:Anti-Bacterial Agents; D010450:Endopeptidases; C001143:endolysin
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