PEPTIDYL TRANSFERS IN GRAMICIDIN S BIOSYNTHESIS FROM ENZYME-BOUND THIOESTER INTERMEDIATES
PEPTIDYL TRANSFERS IN GRAMICIDIN S BIOSYNTHESIS FROM ENZYME-BOUND THIOESTER INTERMEDIATES
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DOI：
10.1073/pnas.63.4.1335
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发表时间：
1969-01-01
影响因子：
11.1
通讯作者：
LIPMANN, F
中科院分区：
文献类型：
--
作者：
GEVERS, W;KLEINKAUF, H;LIPMANN, F
肽类抗生素短杆菌肽S的生物合成包括与两个活性酶组分I和II的硫酯键结合的中间体之间的连续肽基转移反应。组分II激活并再化学化苯丙氨酸，然后通过催化与酶促巯基结合的D-苯丙氨酸的羧基与L-脯氨酸的游离亚氨基之间的反应来引发肽基转移，L-脯氨酸是四种L-氨基酸之一，它们都通过羧基官能团连接到组分I上的单独巯基。在组分I的多酶复合物的活性中心中，这种类型的连续反应导致形成硫酯键合的新生肽链，并最终形成抗生素产物。
The biosynthesis of the peptide antibiotic gramicidin S involves successive peptidyl transfer reactions between intermediates bound in thioester linkages to two active enzyme fractions, I and II. Fraction II activates and recemizes phenylalanine, and then initiates peptidyl transfer by catalyzing a reaction between the carboxyl group of D-phenylalanine, bound to an enzymic sulfhydryl group, and the free imino group of L-proline, one of four L-amino acids all linked by their carboxyl functions to separate sulfhydryl groups on fraction I. Successive reactions of this type in the active centers of the multienzyme complex of fraction I lead to the formation of thioester-bonded nascent peptide chains and, ultimately, of the antibiotic product.