Novel propeptin analog, propeptin-2, missing two amino acid residues from the propeptin C-terminus loses antibiotic potency.
A novel inhibitor of prolyl endopeptidase, the propeptin analog propeptin-2 (C105H130N24O(24)), missing two amino acid residues from the propeptin C-terminus was isolated from the fermentation broth of propeptin-producing Microbispora sp. SNA-115 grown using a large inoculum. It shows the same enzyme inhibition activity as propeptin against prolyl endopeptidase (Ki=1.5 microM), but its antimicrobial activity against Mycobacterium phlei is more than 100-fold lower.
Kimura
Ken-ichi
K
Faculty of Agriculture, Iwate University, Morioka 020-8550, Japan. kimurak@iwate-u.ac.jp
Yamazaki
Mai
M
Sasaki
Noriko
N
Yamashita
Tetsuro
T
Negishi
Shigenori
S
Nakamura
Takemichi
T
Koshino
Hiroyuki
H
D000192:Actinomycetales / Q000254:growth & development / Q000378:metabolism*; D000596:Amino Acids / Q000378:metabolism; D003470:Culture Media / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000378:metabolism* / Q000494:pharmacology; D008826:Microbial Sensitivity Tests; D009168:Mycobacterium phlei / Q000187:drug effects; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000378:metabolism* / Q000494:pharmacology; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases / Q000378:metabolism; D013329:Structure-Activity Relationship