201335-88-8Relevant articles and documents
Fungal Dioxygenase AsqJ Is Promiscuous and Bimodal: Substrate-Directed Formation of Quinolones versus Quinazolinones
Einsiedler, Manuel,Jamieson, Cooper S.,Maskeri, Mark A.,Houk, Kendall N.,Gulder, Tobias A. M.
supporting information, p. 8297 - 8302 (2021/03/01)
Previous studies showed that the FeII/α-ketoglutarate dependent dioxygenase AsqJ induces a skeletal rearrangement in viridicatin biosynthesis in Aspergillus nidulans, generating a quinolone scaffold from benzo[1,4]diazepine-2,5-dione substrates. We report that AsqJ catalyzes an additional, entirely different reaction, simply by a change in substituent in the benzodiazepinedione substrate. This new mechanism is established by substrate screening, application of functional probes, and computational analysis. AsqJ excises H2CO from the heterocyclic ring structure of suitable benzo[1,4]diazepine-2,5-dione substrates to generate quinazolinones. This novel AsqJ catalysis pathway is governed by a single substituent within the complex substrate. This unique substrate-directed reactivity of AsqJ enables the targeted biocatalytic generation of either quinolones or quinazolinones, two alkaloid frameworks of exceptional biomedical relevance.
Direct synthesis of Fmoc-protected amino acids using organozinc chemistry: Application to polymethoxylated phenylalanines and 4-oxoamino acids
Deboves,Montalbetti,Jackson
, p. 1876 - 1884 (2007/10/03)
The newN-Fmoc 3-iodoalaninetert-butyl ester derived organozinc reagent1, obtained in 7 steps from optically pure 3-serine, was coupled to a range of electrophiles under palladium catalysis to give substituted phenylalanines and 4-oxoamino acids in variabl
Site-specific incorporation of non-natural residues into peptides: Effect of residue structure on suppression and translation efficiencies
Bain,Wacker, Dean A.,Kuo, Eric E.,Chamberlin, A. Richard
, p. 2389 - 2400 (2007/10/02)
A systematic survey of the structural requirements for biosynthetic incorporation of non-natural residues into a polypeptide is presented. Relative translation efficiencies for a series of 12 semi-synthetic acylated suppressor tRNAs ranged from 0 to 91% depending on the structure of the residue incorporated.