The chemical structure was confirmed by NMR and HRMS.
Appplication
Benarthin was isolated from the fermentation broth of Streptomyces xanthophaerus MJ244-SF1.1) It inhibited pyroglutamyl peptidase and the binding of benarthin was competitive with substrate (Ki: 1.2 × 10-6 M).1) The structure-activity relationship study of synthesized benarthin analogues indicated that the catechol group of benarthin was essential moiety for the inhibition of pyroglutamyl peptidase.2,3)
References
1) Benarthin: a new inhibitor of pyroglutamyl peptidase. I. Taxonomy, production, isolation and biological activities. Aoyagi T, et al. J Antibiot. 1992 45(7) 1079-1083.
2) Benarthin: a new inhibitor of pyroglutamyl peptidase. II. Physico-chemical properties and structure determination. Hatsu M, et al. J Antibiot. 1992 45(7) 1084-1087.
3) Benarthin: a new inhibitor of pyroglutamyl peptidase. III. Synthesis and structure-activity relationships. Hatsu M, et al. J Antibiot. 1992 45(7) 1088-1095.