Piperastatin A, a new selective serine carboxypeptidase inhibitor produced by actinomycete. II. Physico-chemical properties and structure determination.
Piperastatin A, a new inhibitor of serine carboxypeptidase, was discovered in the culture broth of Streptomyces lavendofoliae MJ908-WF13. The molecular formula of piperastatin A was established as C38H67N9C10 by HRFAB-MS and elemental analysis. The structure was determined to be N-formyl-allo Ile-Thr-Leu-Val-Pip-Leu-Pip (Pip = hexahydropyridadine-3-carboxylic acid) by various spectral analyses of piperastatin A and piperastatin A methylester.
Murakami
S
S
Institute of Microbial Chemistry, Tokyo, Japan.
Takahashi
Y
Y
Naganawa
H
H
Takeuchi
T
T
Aoyagi
T
T
D000596:Amino Acids / Q000032:analysis / Q000737:chemistry; D002268:Carboxypeptidases / Q000037:antagonists & inhibitors*; D043402:Cathepsin A; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D015394:Molecular Structure; D008970:Molecular Weight; D009904:Optical Rotation; D011480:Protease Inhibitors / Q000737:chemistry*; D017421:Sequence Analysis; D013053:Spectrophotometry; D013302:Streptomyces / Q000737:chemistry*
D000596:Amino Acids; D011480:Protease Inhibitors; D002268:Carboxypeptidases; D043402:Cathepsin A