Cargando…
Heterologous caffeic acid biosynthesis in Escherichia coli is affected by choice of tyrosine ammonia lyase and redox partners for bacterial Cytochrome P450
BACKGROUND: Caffeic acid is industrially recognized for its antioxidant activity and therefore its potential to be used as an anti-inflammatory, anticancer, antiviral, antidiabetic and antidepressive agent. It is traditionally isolated from lignified plant material under energy-intensive and harsh c...
Autores principales: | Haslinger, Kristina, Prather, Kristala L. J. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7011507/ https://www.ncbi.nlm.nih.gov/pubmed/32046741 http://dx.doi.org/10.1186/s12934-020-01300-9 |
Ejemplares similares
-
Evolution of Cytochrome P450 Enzymes and Their Redox Partners in Archaea
por: Ngcobo, Phelelani Erick, et al.
Publicado: (2023) -
Engineering of versatile redox partner fusions that support monooxygenase activity of functionally diverse cytochrome P450s
por: Bakkes, Patrick J., et al.
Publicado: (2017) -
Sequential Allylic Alcohol Formation by a Multifunctional Cytochrome P450 Monooxygenase with Rare Redox Partners
por: Kim, Hak Joong, et al.
Publicado: (2022) -
Discovery of Novel Tyrosine Ammonia Lyases for the Enzymatic Synthesis of p‐Coumaric Acid
por: Brack, Yannik, et al.
Publicado: (2022) -
Tyrosine Hydroxylation in Betalain Pigment Biosynthesis Is Performed by Cytochrome P450 Enzymes in Beets (Beta vulgaris)
por: Sunnadeniya, Rasika, et al.
Publicado: (2016)