Cargando…
Comparative thermodynamic studies on substrate and product binding of O-Acetylserine Sulfhydrylase reveals two different ligand recognition modes(†)
BACKGROUND: The importance of understanding the detailed mechanism of cysteine biosynthesis in bacteria is underscored by the fact that cysteine is the only sulfur donor for all cellular components containing reduced sulfur. O-acetylserine sulfhydrylase (OASS) catalyzes this crucial last step in the...
Autores principales: | Banerjee, Shrijita, Ekka, Mary K, Kumaran, Sangaralingam |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3141655/ https://www.ncbi.nlm.nih.gov/pubmed/21631959 http://dx.doi.org/10.1186/1471-2091-12-31 |
Ejemplares similares
-
Inhibition of O-acetylserine sulfhydrylase by fluoroalanine derivatives
por: Franko, Nina, et al.
Publicado: (2018) -
Isozyme-Specific Ligands for O-acetylserine sulfhydrylase, a Novel Antibiotic Target
por: Spyrakis, Francesca, et al.
Publicado: (2013) -
Impact of overexpression of cytosolic isoform of O-acetylserine sulfhydrylase on soybean nodulation and nodule metabolome
por: Krishnan, Hari B., et al.
Publicado: (2018) -
Refining the structure−activity relationships of 2-phenylcyclopropane carboxylic acids as inhibitors of O-acetylserine sulfhydrylase isoforms
por: Magalhães, Joana, et al.
Publicado: (2018) -
Inhibitors of O-Acetylserine Sulfhydrylase with a Cyclopropane-Carboxylic Acid Scaffold Are Effective Colistin Adjuvants in Gram Negative Bacteria
por: Annunziato, Giannamaria, et al.
Publicado: (2022)