MS-271, a novel inhibitor of calmodulin-activated myosin light chain kinase from Streptomyces sp.--I. Isolation, structural determination and biological properties of MS-271.
A novel cyclic peptide, MS-271, was isolated from the culture broth of an actinomycete, Streptomyces sp. M-271 as an inhibitor of smooth muscle myosin light chain kinase (MLCK). MS-271 inhibited the MLCK from chicken gizzard with an IC50 value of 8 microM. MS-271 did not inhibit cyclic AMP-dependent protein kinase, protein kinase C or calcium/calmodulin-dependent cyclic nucleotide phosphodiesterase at concentrations up to 400 microM. The primary structure of MS-271 was identical to that of siamycin I, an anti-HIV peptide isolated from a microbial source.
Yano
K
K
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co. Ltd, Japan.
Toki
S
S
Nakanishi
S
S
Ochiai
K
K
Ando
K
K
Yoshida
M
M
Matsuda
Y
Y
Yamasaki
M
M
D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000900:Anti-Bacterial Agents; D000935:Antifungal Agents; D002417:Cattle; D002645:Chickens; D017868:Cyclic AMP-Dependent Protein Kinases / Q000037:antagonists & inhibitors; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D005285:Fermentation; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D009219:Myosin-Light-Chain Kinase / Q000037:antagonists & inhibitors*; D010456:Peptides, Cyclic / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D051381:Rats; D013302:Streptomyces / Q000737:chemistry* / Q000378:metabolism
D000596:Amino Acids; D000900:Anti-Bacterial Agents; D000935:Antifungal Agents; D004791:Enzyme Inhibitors; C100562:MS 271; D010456:Peptides, Cyclic; D000255:Adenosine Triphosphate; D017868:Cyclic AMP-Dependent Protein Kinases; D009219:Myosin-Light-Chain Kinase