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Dipeptidyl-peptidase IV secreted by Aspergillus fumigatus, a fungus pathogenic to humans.

机译:烟曲霉分泌的二肽基肽酶IV,这是一种对人类致病的真菌。

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A dipeptidyl-peptidase IV was purified from the culture medium of the human-pathogenic fungus Aspergillus fumigatus. The enzyme has an apparent molecular mass of 95 kDa and contained approximately 10 kDa of N-linked carbohydrate. This glycoprotein is antigenic and has all characteristics of the class IV dipeptidyl-peptidases: removal of Xaa-Pro and to a lesser extent Xaa-Ala dipeptides from the N termini of peptides, including bioactive peptides such as neuropeptide Y, [des-Arg1] bradykinin, and glucagon-like peptide 1, activity at neutral pH, and presence in the amino acid sequence of the Gly-X-Ser-X-Gly consensus motif of the serine-hydrolases and the putative catalytic triad (Ser613, Asp690, His725) of the dipeptidyl-peptidases. Moreover, the last 200 amino acids displayed 60 to 65% similarity with the other dipeptidyl-peptidases IV from rat, mouse, human, and yeast. However, unlike the other dipeptidyl-peptidases, the dipeptidyl-peptidase IV of A. fumigatus is a secreted enzyme with a cleavable signal peptide. Expression of a recombinant dipeptidyl-peptidase IV of A. fumigatus has been attained in the yeast Pichia pastoris.
机译:从人病原性真菌烟曲霉的培养基中纯化二肽基肽酶IV。该酶的表观分子量为95 kDa,含有约10 kDa的N-连接的碳水化合物。该糖蛋白具有抗原性,并具有IV类二肽基肽酶的所有特征:从肽N末端(包括生物活性肽,例如神经肽Y,[des-Arg1])的Xaa-Pro和较小程度的Xaa-Ala二肽去除。缓激肽和胰高血糖素样肽1,在中性pH下具有活性,并在氨基酸序列中存在丝氨酸水解酶和推定的催化三联体(Ser613,Asp690,His725的Gly-X-Ser-X-Gly共有基序) )的二肽基肽酶。此外,最后200个氨基酸与来自大鼠,小鼠,人和酵母的其他二肽基肽酶IV表现出60%至65%的相似性。但是,与其他二肽基肽酶不同,烟曲霉的二肽基肽酶IV是一种具有可裂解信号肽的分泌酶。烟曲霉的重组二肽基肽酶IV已经在酵母毕赤酵母中获得表达。

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