Conformational interdomain flexibility in a bacterial α-isopropylmalate synthase is necessary for leucine biosynthesis

α-Isopropylmalate synthase (IPMS) catalyzes the first step in leucine (Leu) biosynthesis and is allosterically regulated by the pathway end product, Leu. IPMS is a dimeric enzyme with each chain consisting of catalytic, accessory, and regulatory domains, with the accessory and regulatory domains of...

Descripción completa

Detalles Bibliográficos
Autores principales: Bai, Yu, Jiao, Wanting, Vörster, Jan, Parker, Emily J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2022
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9860122/
https://www.ncbi.nlm.nih.gov/pubmed/36509144
http://dx.doi.org/10.1016/j.jbc.2022.102789

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9860122/
https://www.ncbi.nlm.nih.gov/pubmed/36509144
http://dx.doi.org/10.1016/j.jbc.2022.102789

Ejemplares similares