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酶结合的甲酰缬氨酸和甲酰缬氨酰甘氨酸;短杆菌肽A生物合成的起始复合物。

Enzyme-bound formylvaline and formylvalylglycine; an initiation complex for gramicidin A biosynthesis.

作者信息

Akashi K, Kurahashi K

出版信息

J Biochem. 1978 May;83(5):1219-29. doi: 10.1093/oxfordjournals.jbchem.a132029.

Abstract

Gramicidin A is an antibiotic peptide produced by Bacillus brevis ATCC 8185, which also produces tyrocidines. An attempt was made to establish a cell-free enzyme system for gramicidin A synthesis. An enzyme fraction, Component I, was partially purified from crude extracts of the organism and proven to be involved in the synthesis of the formyl-Val-Gly- region of gramicidin A. The initiation of gramicidin A biosynthesis is a function of Component I, which activates valine and binds it as a thioester, and further formylates it in the presence of formyltetrahydrofolic acid. The formylvaline thus synthesized is transferred to the glycine moiety, which is also thioesterified to Component I. Elongation of the peptide chain takes place by a mechanism similar to those found for tyrocidines, gramicidin S, and bacitracin.

摘要

短杆菌肽A是由短短芽孢杆菌ATCC 8185产生的一种抗生素肽,该菌还能产生短杆菌酪肽。人们试图建立一种用于短杆菌肽A合成的无细胞酶系统。一种酶组分,即组分I,从该生物体的粗提取物中部分纯化出来,并被证明参与短杆菌肽A中甲酰基 - 缬氨酸 - 甘氨酸区域的合成。短杆菌肽A生物合成的起始是组分I的功能,组分I激活缬氨酸并将其作为硫酯结合,然后在甲酰四氢叶酸存在的情况下进一步将其甲酰化。如此合成的甲酰缬氨酸被转移到甘氨酸部分,甘氨酸也被硫酯化到组分I上。肽链的延伸通过与短杆菌酪肽、短杆菌肽S和杆菌肽类似的机制进行。

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