title: Enzymatic timing and tailoring of macrolactamization in syringolin biosynthesis.
abstract: The enzymatic activation of 3,4-dehydrolysine and subsequent formation of the 12-membered syringolin macrolactam were investigated. The timing of the desaturation was elucidated through the analysis of the initial adenylation domain of SylD. The SylD-TTE didomain was characterized and demonstrated to be the catalyst for formation of 12-membered macrocycles. When the SylD thioesterase domain was reacted with a family of acyclic CoA both natural and unnatural macrocycles were generated.
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
authors.forename: William M
authors.initials: WM
authors.lastname: Wuest
authors.forename: Daniel
authors.initials: D
authors.lastname: Krahn
authors.forename: Markus
authors.initials: M
authors.lastname: Kaiser
authors.forename: Christopher T
authors.initials: CT
authors.lastname: Walsh
mesh_terms: D015394:Molecular Structure; D010456:Peptides, Cyclic / Q000096:biosynthesis* / Q000737:chemistry; D013237:Stereoisomerism; D013869:Thiolester Hydrolases / Q000737:chemistry / Q000378:metabolism*; D014508:Urea / Q000031:analogs & derivatives* / Q000737:chemistry
chemical_list: D010456:Peptides, Cyclic; C407267:syringolin A; C540864:syringolin B; D014508:Urea; D013869:Thiolester Hydrolases