Premium
Characterization of NovP and NovN: Completion of Novobiocin Biosynthesis by Sequential Tailoring of the Noviosyl Ring
Author(s) -
Freel Meyers Caren L.,
Oberthür Markus,
Xu Hui,
Heide Lutz,
Kahne Daniel,
Walsh Christopher T.
Publication year - 2003
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200352626
Subject(s) - novobiocin , dna gyrase , biosynthesis , escherichia coli , biochemistry , biology , methyltransferase , streptomyces , enzyme , dna , chemistry , antibiotics , genetics , bacteria , gene , methylation
Two steps forward : The glycosylated aminocoumarin antibiotic novobiocin ( 1 ) is produced by Streptomyces spheroides and inhibits the bacterial type II topoisomerase DNA gyrase. The sugar‐tailoring enzymes NovP and NovN that catalyze the final two steps in novobiocin biosynthesis were overproduced in Escherichia coli and characterized as a methyltransferase and carbamoyltransferase, respectively.