Benarthin: a new inhibitor of pyroglutamyl peptidase. II. Physico-chemical properties and structure determination.
Benarthin, a new inhibitor of pyroglutamyl peptidase (PG-peptidase), has been isolated from the culture broth of Streptomyces xanthophaeus MJ244-SF1. The structure of benarthin was determined to be L-(2,3-dihydroxybenzoyl)argininyl-L-threonine by analysis of spectral properties and through chemical studies.
Institute of Microbial Chemistry, Tokyo, Japan.
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Hatsu
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Naganawa
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Aoyagi
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Takeuchi
D004151:Dipeptides / Q000032:analysis / Q000737:chemistry*; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy; D011751:Pyroglutamyl-Peptidase I / Q000037:antagonists & inhibitors; D013055:Spectrophotometry, Infrared; D013302:Streptomyces / Q000378:metabolism
D004151:Dipeptides; C076470:benarthin; D011751:Pyroglutamyl-Peptidase I