Moving posttranslational modifications forward to biosynthesize the glycosylated thiopeptide nocathiacin I in Nocardia sp. ATCC202099.
Characterization of the biosynthetic gene cluster of glycosylated antibiotic nocathiacin I (NOC-I) here adds new insights to thiopeptide biosynthesis, showing the NOC-specific tailoring and unusual sugar formation. NOC-I biosynthesis shares the paradigm for forming a common thiopeptide core and the generality for converting to an e series member, as that of the parent compound nosiheptide (NOS). This may permit the production of NOC-I in the genetically amenable, NOS-producing strain by building NOC-specific genes for pathway engineering.
Ding
Ying
Y
Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 345 Lingling Rd., Shanghai 200032, China.
Yu
Yi
Y
Pan
Haixue
H
Guo
Heng
H
Li
Yeming
Y
Liu
Wen
W
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D053898:Biosynthetic Pathways; D003001:Cloning, Molecular; D023061:Gene Order; D006031:Glycosylation; D036341:Intercellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D015394:Molecular Structure; D005810:Multigene Family; D009615:Nocardia / Q000235:genetics / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; C463319:nocathiacin I