The reactive site of marinostatin, a proteinase inhibitor from marine Alteromonas sp. B-10-31. |
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| Authors: | R Takano C Imada K Kamei S Hara |
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| Affiliation: | Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology. |
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| Abstract: | A new homologue of marinostatin, a peptide proteinase inhibitor, was isolated from marine Alteromonas sp. B-10-31 and designated as marinostatin D. Its amino acid sequence was determined to be Ala-Thr-Met-Arg-Tyr-Pro-Ser-Asp-Asp-Ser-Glu. The reactive site of marinostatin D was determined to be Met(3)-Arg(4) on the basis of the reversible cleavage and regeneration of the scissile bond catalyzed by TLCK-chymotrypsin. |
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