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DEHYDROALANYLLYSINE: IDENTICAL COOH-TERMINAL STRUCTURES IN THE PEPTIDE ANTIBIOTICS NISIN AND SUBTILIN

机译:脱氢丙二酸赖氨酸:肽抗菌素乳链菌肽和枯草杆菌蛋白酶中相同的CO-末端结构

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摘要

The recent finding of α,β-unsaturated amino acid residues by Gross and Morrel in the polypeptide antibiotic nisin has stimulated a wider investigation of other antibiotic peptides, particularly those known to contain lanthionine. Subtilin is similar to nisin in that it polymerizes easily and contains lanthionine and β-methyl lanthionine. Like nisin it was found to contain a carboxyl terminal dehydroalanyllysine sequence and to be split by the enzyme nisinase. An additional α,β-unsaturated amino acid residue was shown to be present in subtilin by reaction with excess methyl mercaptoacetate and subsequent hydrolysis and amino acid analysis. Nisin contains three dehydropeptide residues.
机译:Gross和Morrel在多肽抗生素乳链菌肽中最近发现的α,β-不饱和氨基酸残基刺激了对其他抗生素肽的更广泛研究,尤其是已知包含羊毛硫氨酸的那些。枯草杆菌蛋白酶与乳链菌肽相似,因为它易于聚合并含有羊毛硫氨酸和β-甲基羊毛硫氨酸。象乳链菌肽一样,发现它含有一个羧基末端脱氢丙氨酰赖氨酸序列,并被乳链菌肽酶分解。通过与过量巯基乙酸甲酯反应并随后进行水解和氨基酸分析,枯草杆菌蛋白酶中还存在一个额外的α,β-不饱和氨基酸残基。乳链菌肽含有三个脱氢肽残基。

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