Cargando…
Exploring nicotinamide cofactor promiscuity in NAD(P)H-dependent flavin containing monooxygenases (FMOs) using natural variation within the phosphate binding loop. Structure and activity of FMOs from Cellvibrio sp. BR and Pseudomonas stutzeri NF13
Flavin-containing monooxygenases (FMOs) catalyse asymmetric oxidation reactions that have potential for preparative organic synthesis, but most use the more expensive, phosphorylated nicotinamide cofactor NADPH to reduce FAD to FADH(2) prior to formation of the (hydro)peroxy intermediate required fo...
Autores principales: | Jensen, Chantel N., Ali, Sohail T., Allen, Michael J., Grogan, Gideon |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Science
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4220118/ https://www.ncbi.nlm.nih.gov/pubmed/25383040 http://dx.doi.org/10.1016/j.molcatb.2014.08.019 |
Ejemplares similares
-
FLAVIN-CONTAINING MONOOXYGENASES (FMOS): LONGEVITY-PROMOTING ENZYMES OR ATHEROSCLEROSIS RISK FACTOR?
por: Rossner, Ryan J, et al.
Publicado: (2019) -
Mutations of an NAD(P)H-dependent flavoprotein monooxygenase that influence cofactor promiscuity and enantioselectivity()
por: Jensen, Chantel N., et al.
Publicado: (2013) -
Developing and enhancing promiscuous activity for NAD(P)H-dependent flavin reductase via elimination of cofactor
por: Navaser, Amene, et al.
Publicado: (2023) -
A Regulatory Role of NAD Redox Status on Flavin Cofactor Homeostasis in S. cerevisiae Mitochondria
por: Giancaspero, Teresa Anna, et al.
Publicado: (2013) -
Structural and functional variation of chitin-binding domains of a lytic polysaccharide monooxygenase from Cellvibrio japonicus
por: Madland, Eva, et al.
Publicado: (2021)