Structural elucidation of talopeptin (MK-I), a novel metallo proteinase inhibitor produced by streptomyces mozunensis MK-23

✍ Scribed by Ken-ichi Fukuhara; Sawao Murao; Tsunenori Nozawa; Masahiro Hatano

• Book ID: 104220830
• Publisher: Elsevier Science
• Year: 1982
• Tongue: French
• Weight: 225 KB
• Volume: 23
• Category: Article
• ISSN: 0040-4039
• DOI: 10.1016/s0040-4039(00)87331-1

✦ Synopsis

The structure of talopeptin (MK-I), a novel metallo proteinase inhibitor produced by Streptomyces mozunensis MK-23 was elucidated to be 6-deoxy-e-Ltalopyranosyloxyphospho-L-leucyl-L-tryptophan. As reported in the previous papers [1,2], a novel proteinase inhibitor talopeptin (MK-I), which shows a specific inhibitory activity against metallo proteinases, was isolated from the culture filtrate of Streptomyces mozunensis MK-23. It was also reported that talopeptin is composed of 6-deoxyaldohexose, phosphoric acid, leucine and tryptophan. In this paper, structural elucidation of talopeptin is reported.

Partial hydrolysis with 0.5N HCl (70°C, 1 hr), talopeptin gave 6-deoxyhexose, phosphoric acid and a peptide, which were separated from each other by column chromatographies.

The peptide component was separated by carbon chromatography: mp 133°(dec.);