Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site
Siroheme is an essential bacterial iron tetrapyrrole used by siroheme-dependent sulfite and nitrite reductases. Here the authors shed light on the catalytic mechanisms of siroheme synthase through the structures of the bifunctional dehydrogenase/chelatase CysG module bound to its substrate, precorri...
Guardado en:
Autores principales: | Joseph M. Pennington, Michael Kemp, Lauren McGarry, Yu Chen, M. Elizabeth Stroupe |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2020
|
Materias: | |
Acceso en línea: | https://doaj.org/article/ea8b31747188498a8b3a178dfb2ba7c0 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Curbing action potential generation or ATP-synthase leads to a decrease in in-cell pyruvate dehydrogenase activity in rat cerebrum slices
por: Benjamin Grieb, et al.
Publicado: (2021) -
Generation of amine dehydrogenases with increased catalytic performance and substrate scope from ε-deaminating L-Lysine dehydrogenase
por: Vasilis Tseliou, et al.
Publicado: (2019) -
Association of the malate dehydrogenase-citrate synthase metabolon is modulated by intermediates of the Krebs tricarboxylic acid cycle
por: Joy Omini, et al.
Publicado: (2021) -
Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion
por: Jana Škerlová, et al.
Publicado: (2021) -
Discovery of novel highly active and stable aspartate dehydrogenases
por: Hao Li, et al.
Publicado: (2017)