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Microbial Serine Carboxypeptidase Inhibitors--Comparative Analysis of Actions on Homologous Enzymes Derived From Man, Yeast and Wheat

Microbial Serine Carboxypeptidase Inhibitors--Comparative Analysis of Actions on Homologous Enzymes Derived From Man, Yeast and Wheat

Yurie Satoh, Yoshito Kadota, Yukako Oheda, Jun Kuwahara, Seiichi Aikawa, Fumiko Matsuzawa, Hirofumi Doi, Takaaki Aoyagi, Hitoshi Sakuraba, Kohji Itoh

J Antibiot (Tokyo). 2004 May;57(5):316-25.

PMID: 15303492

Abstract:

The actions of peptidase inhibitors derived from Streptomycete on human cathepsin A (hCath A), yeast carboxypeptidase Y (CPY), and wheat carboxypeptidase II (CPW) were analyzed comparatively. Lactacystin and omuralide (clasto-lactacystin beta-lactone), well-known cytoplasmic proteasome inhibitors, both had a potent and non-competitive inhibitory effect on these homologous serine carboxypeptidases, although they inhibited CPW and hCath A more effectively than CPY in vitro. Ebelactone B exhibited a mixed non-competitive inhibitory effect and selectivity for CPY. Piperastatin A showed competitive inhibition of CPY and hCath A but had little effect on CPW. In contrast, chymostatin inhibited CPW efficiently, while it had less effect on hCath A and CPY. In cell culture system, lactacystin was the most potent as to inactivation of the intralysosomal recombinant hCath A activity expressed in a genetically engineered fibroblastic cell line with galactosialidosis (hCath A deficiency). These results suggest that the specific inhibitory effects of lactacystin and its derivatives on hCath A might be applicable to elucidate the pathophysiological roles in the human deficinecy.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP76808167	Ebelactone A microbial		76808-16-7	Price

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