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以腺苷酸的N-(甲酰)蛋氨酸酯作为肽供体,由大肠杆菌核糖体的50S亚基催化肽键形成。

Catalysis of the peptide bond formation by 50 S subunits of E. coli ribosomes with N-(formyl) methionine ester of adenylic acid as peptide donor.

作者信息

Kotusov V V, Kukhanova M K, Krayevsky A A, Gottikh B P

出版信息

Mol Biol Rep. 1976 Nov;3(2):151-6. doi: 10.1007/BF00423229.

Abstract

50 S subunits of E. coli ribosomes catalyze the reaction of the 2'(3')-N-(formyl) methionine ester of adenosine 5'-phosphate and Phe-tRNA resulting in peptide bond synthesis. Cytidine 5'-phosphate stimulates this process on 50 S ribosomal subunits as well as on intact ribosomes. The obtained data show that the areas of the peptidyltransferase donor site which binds the 3'-terminal fragment of peptidyl-tRNA possess completely formed structures on 50 S ribosomal subunits.

摘要

大肠杆菌核糖体的50 S亚基催化5'-磷酸腺苷的2'(3')-N-(甲酰)甲硫氨酸酯与苯丙氨酰-tRNA的反应,从而导致肽键合成。5'-磷酸胞苷在50 S核糖体亚基以及完整核糖体上均能刺激这一过程。所得数据表明,在50 S核糖体亚基上,与肽酰-tRNA的3'-末端片段结合的肽基转移酶供体位点区域具有完全形成的结构。

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