PubMed:12162571 JSONTXT

{"project":"silkwormbase","denotations":[{"id":"T1","span":{"begin":44,"end":60},"obj":"Chemical:-"},{"id":"T10","span":{"begin":730,"end":737},"obj":"Chemical:MESH:D008543"},{"id":"T11","span":{"begin":822,"end":840},"obj":"Chemical:MESH:D008543"},{"id":"T2","span":{"begin":111,"end":116},"obj":"Chemical:MESH:D000588"},{"id":"T3","span":{"begin":289,"end":312},"obj":"Species:1914"},{"id":"T4","span":{"begin":341,"end":348},"obj":"Chemical:MESH:D008543"},{"id":"T5","span":{"begin":391,"end":407},"obj":"Chemical:-"},{"id":"T6","span":{"begin":454,"end":470},"obj":"Chemical:-"},{"id":"T7","span":{"begin":541,"end":550},"obj":"Chemical:MESH:D005973"},{"id":"T8","span":{"begin":685,"end":693},"obj":"Species:7091"},{"id":"T9","span":{"begin":698,"end":705},"obj":"Chemical:MESH:D008543"},{"id":"T14","span":{"begin":426,"end":431},"obj":"Chemical:MESH:D008543"}],"text":"Inhibition of transglutaminase by synthetic tyrosine melanin.\nTransglutaminases catalyze the cross-linking and amine incorporation of proteins, and are implicated in various biological phenomena. Previously, we found a high molecular mass transglutaminase-inhibitory substance produced by Streptomyces lavendulae Y-200 that appeared to be a melanin substance. Here, we report that synthetic tyrosine melanin inhibited various types of transglutaminases. Tyrosine melanin inhibited tissue-type transglutaminase in a competitive manner with a glutamine substrate, and also inhibited the cross-linking of casein catalyzed by a tissue-type transglutaminase. The melanized hemolymph of the silkworm and melanin solutions prepared from melanin precursors inhibited tissue-type transglutaminase. These results suggested that the melanin substances generally inhibit transglutaminases."}

{"project":"silkworm","denotations":[{"id":"T1","span":{"begin":44,"end":60},"obj":"Chemical:-"},{"id":"T2","span":{"begin":111,"end":116},"obj":"Chemical:MESH:D000588"},{"id":"T3","span":{"begin":289,"end":312},"obj":"Species:1914"},{"id":"T4","span":{"begin":341,"end":348},"obj":"Chemical:MESH:D008543"},{"id":"T5","span":{"begin":391,"end":407},"obj":"Chemical:-"},{"id":"T6","span":{"begin":454,"end":470},"obj":"Chemical:-"},{"id":"T7","span":{"begin":541,"end":550},"obj":"Chemical:MESH:D005973"},{"id":"T8","span":{"begin":685,"end":693},"obj":"Species:7091"},{"id":"T9","span":{"begin":698,"end":705},"obj":"Chemical:MESH:D008543"},{"id":"T10","span":{"begin":730,"end":737},"obj":"Chemical:MESH:D008543"},{"id":"T11","span":{"begin":822,"end":840},"obj":"Chemical:MESH:D008543"}],"text":"Inhibition of transglutaminase by synthetic tyrosine melanin.\nTransglutaminases catalyze the cross-linking and amine incorporation of proteins, and are implicated in various biological phenomena. Previously, we found a high molecular mass transglutaminase-inhibitory substance produced by Streptomyces lavendulae Y-200 that appeared to be a melanin substance. Here, we report that synthetic tyrosine melanin inhibited various types of transglutaminases. Tyrosine melanin inhibited tissue-type transglutaminase in a competitive manner with a glutamine substrate, and also inhibited the cross-linking of casein catalyzed by a tissue-type transglutaminase. The melanized hemolymph of the silkworm and melanin solutions prepared from melanin precursors inhibited tissue-type transglutaminase. These results suggested that the melanin substances generally inhibit transglutaminases."}