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B6db references: 25026542

type Journal Article
authors Kulikovsky A, Serebryakova M, Bantysh O, Metlitskaya A, Borukhov S, Severinov K, Dubiley S.
title The molecular mechanism of aminopropylation of peptide-nucleotide antibiotic microcin C
journal J Am Chem Soc
Activity mcce
Family mcce
sel selected
ui 25026542
year (2014)
volume 136
number 31
pages 11168-75
abstract Translation inhibitor microcin C (McC) is a heptapeptide with an aspartate α-carboxyl group linked to AMP via phosphoramidate bond. Modification of the McC phosphate by an aminopropyl moiety increases the biological activity by ~10-fold. Here, we determine the pathway of the aminopropylation reaction of McC. We show that the MccD enzyme uses S-adenosyl methionine to transfer 3-amino-3-carboxypropyl group onto a phosphate of an McC maturation intermediate consisting of adenylated heptapeptide. The carboxyl group is removed by the MccE enzyme, yielding mature McC. MccD is an inefficient enzyme that requires for its action the product of Escherichia coli mtn gene, a 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase, which hydrolyses 5'-methylthioadenosine, the product of MccD-catalyzed reaction, thus stimulating the amino-3-carboxypropylation reaction. Both MccD and MccE are capable of modifying McC-like compounds with divergent peptide moieties, opening way for preparation of more potent peptidyl-adenylates.
last changed 2017/12/05 11:02

B6db references