Allostery, engineering and inhibition of tryptophan synthase.
Curr Opin Struct Biol
; 82: 102657, 2023 10.
Article
em En
| MEDLINE
| ID: mdl-37467527
ABSTRACT
The final two steps of tryptophan biosynthesis are catalyzed by the enzyme tryptophan synthase (TS), composed of alpha (αTS) and beta (ßTS) subunits. Recently, experimental and computational methods have mapped "allosteric networks" that connect the αTS and ßTS active sites. In αTS, allosteric networks change across the catalytic cycle, which might help drive the conformational changes associated with its function. Directed evolution studies to increase catalytic function and expand the substrate profile of stand-alone ßTS have also revealed the importance of αTS in modulating the conformational changes in ßTS. These studies also serve as a foundation for the development of TS inhibitors, which can find utility against Mycobacterium tuberculosis and other bacterial pathogens.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Triptofano Sintase
Idioma:
En
Revista:
Curr Opin Struct Biol
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2023
Tipo de documento:
Article