15 research outputs found

    Metamorphic zonation and formation granulite in the Shizunai area, the Hidaka Metamorphic Belt, Hokkaido, Japan

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    The central part of the Hidaka Metamorphic Belt (HMB) is divided into six metamorphic zones : lower-biotite, upper-biotite, garnet, sillimanite-muscovite, garnet-cordierite and orthopyroxene zones. A significant temperature gap with lithological contrast is recognized between the sillimanite-muscovite and garnet-cordierite zones. In the garnet-cordierite and orthopyroxene zones, marked prograde zoning profiles occur in garnets in amphibolites. Geothermometry and diffusion modeling for the zoning profiles of these garnets suggest that the rims were formed under upper amphibolite-facies and granulite-facies conditions, with a brief and rapid increase in temperature at peak metamorphism. The latest pulse of SHRIMP zircon dating of granulite (Early Miocene) in the Hidakahorobetsu River area may explain the granulite-facies metamorphism recorded the garnet rims, which occurred just before the uplift episode indicated by K-Ar ages

    The Aminolysis Reaction of Streptomyces S9 Aminopeptidase Promotes the Synthesis of Diverse Prolyl Dipeptides▿ †

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    Prolyl dipeptide synthesis by S9 aminopeptidase from Streptomyces thermocyaneoviolaceus (S9AP-St) has been demonstrated. In the synthesis, S9AP-St preferentially used l-Pro-OBzl as the acyl donor, yielding synthesized dipeptides having an l-Pro-Xaa structure. In addition, S9AP-St showed broad specificity toward the acyl acceptor. Furthermore, S9AP-St produced cyclo (l-Pro-l-His) with a conversion ratio of substrate to cyclo (l-Pro-l-His) higher than 40%

    One-Pot Synthesis of Diverse dl-Configuration Dipeptides by a Streptomyces d-Stereospecific Amidohydrolase ▿ †

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    The synthesis of diverse dl-configuration dipeptides in a one-pot reaction was demonstrated by using a function of the aminolysis reaction of a d-stereospecific amidohydrolase from Streptomyces sp., a clan SE, S12 family peptidase categorized as a peptidase with d-stereospecificity. The enzyme was able to use various aminoacyl derivatives, including l-aminoacyl derivatives, as acyl donors and acceptors. Investigations of the specificity of the peptide synthetic activity revealed that the enzyme preferentially used d-aminoacyl derivatives as acyl donors. In contrast, l-amino acids and their derivatives were preferentially used as acyl acceptors. Consequently, the synthesized dipeptides had a dl-configuration when d- and l-aminoacyl derivatives were mixed in a one-pot reaction. This report also describes that the enzyme produced cyclo(d–Pro-l-Arg), a specific inhibitor of family 18 chitinase, with a conversion rate for d-Pro benzyl ester and l-Arg methyl ester to cyclo(d-Pro–l-Arg) of greater than 65%. Furthermore, based on results of cyclo(d-Pro–l-Arg) synthesis, we propose a reaction mechanism for cyclo(d-Pro–l-Arg) production
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