YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations

Cyclodehydrations in thiazole/oxazole-modified microcin biosynthesis are known to require a multiprotein complex, but full details of the reaction were not clear. Substrate analogs and isotopic labeling now show the D protein, thought to serve a scaffolding function, catalyzes ring formation and use...

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Veröffentlicht in:	Nature chemical biology 2012-04, Vol.8 (6), p.569-575
Hauptverfasser:	Dunbar, Kyle L, Melby, Joel O, Mitchell, Douglas A
Format:	Artikel
Sprache:	eng
Schlagworte:	631/92/349 631/92/60 Adenosine Triphosphate - metabolism Amides - metabolism Amino Acid Sequence Anti-Bacterial Agents - biosynthesis Anti-Bacterial Agents - chemistry ATP Bacterial Proteins - metabolism Bacteriocins - biosynthesis Bacteriocins - chemistry Bacteriocins - genetics Biochemical Engineering Biochemistry Biology Bioorganic Chemistry Biosynthesis Catalytic Domain Cell Biology Chemistry Chemistry and Materials Science Chemistry/Food Science Cyclization Dehydrogenases Enzymes Hydrolysis Hypotheses Molecular Sequence Data Multienzyme Complexes - metabolism Multigene Family Natural products Oxazoles - metabolism Peptide Biosynthesis Peptides Peptides, Cyclic - biosynthesis Peptides, Cyclic - chemistry Phosphorylation Proteins Substrate Specificity Thiazoles - metabolism
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