Abstract
An 11-residue peptide lactone, termed the gelatinase biosynthesis-activating pheromone (GBAP), triggers the production of the pathogenicit)-related extracellular proteases, gelatinase and serine protease, in Enterococcus faecalis. In this study, we synthesized GBAP and its analogs and examined their gelatinase biosynthesis-inducing activity. This study on the structure-activity relationship shows that a lactone ring was indispensable for the activity.
| Original language | English |
|---|---|
| Pages (from-to) | 2322-2325 |
| Number of pages | 4 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 65 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - Oct 1 2001 |
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All Science Journal Classification (ASJC) codes
- Food Science
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biotechnology
- Chemistry (miscellaneous)
- Applied Microbiology and Biotechnology
Cite this
Chemical synthesis and biological activity of the gelatinase biosynthesis-activating pheromone of enterococcus faecalis and its analogs. / Nakayama, Jiro; Cao, Yong; Horii, Takaaki; Sakuda, Shohei; Nagasawa, Hiromichi.
In: Bioscience, Biotechnology and Biochemistry, Vol. 65, No. 10, 01.10.2001, p. 2322-2325.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Chemical synthesis and biological activity of the gelatinase biosynthesis-activating pheromone of enterococcus faecalis and its analogs
AU - Nakayama, Jiro
AU - Cao, Yong
AU - Horii, Takaaki
AU - Sakuda, Shohei
AU - Nagasawa, Hiromichi
PY - 2001/10/1
Y1 - 2001/10/1
N2 - An 11-residue peptide lactone, termed the gelatinase biosynthesis-activating pheromone (GBAP), triggers the production of the pathogenicit)-related extracellular proteases, gelatinase and serine protease, in Enterococcus faecalis. In this study, we synthesized GBAP and its analogs and examined their gelatinase biosynthesis-inducing activity. This study on the structure-activity relationship shows that a lactone ring was indispensable for the activity.
AB - An 11-residue peptide lactone, termed the gelatinase biosynthesis-activating pheromone (GBAP), triggers the production of the pathogenicit)-related extracellular proteases, gelatinase and serine protease, in Enterococcus faecalis. In this study, we synthesized GBAP and its analogs and examined their gelatinase biosynthesis-inducing activity. This study on the structure-activity relationship shows that a lactone ring was indispensable for the activity.
UR - http://www.scopus.com/inward/record.url?scp=0035490516&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035490516&partnerID=8YFLogxK
U2 - 10.1271/bbb.65.2322
DO - 10.1271/bbb.65.2322
M3 - Article
C2 - 11758932
AN - SCOPUS:0035490516
VL - 65
SP - 2322
EP - 2325
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 10
ER -