Cargando…
Biochemical and Biophysical Characterization of Recombinant Human 3-Phosphoglycerate Dehydrogenase
The human enzyme D-3-phosphoglycerate dehydrogenase (hPHGDH) catalyzes the reversible dehydrogenation of 3-phosphoglycerate (3PG) into 3-phosphohydroxypyruvate (PHP) using the NAD(+)/NADH redox cofactor, the first step in the phosphorylated pathway producing L-serine. We focused on the full-length e...
Autores principales: | Murtas, Giulia, Marcone, Giorgia Letizia, Peracchi, Alessio, Zangelmi, Erika, Pollegioni, Loredano |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8073719/ https://www.ncbi.nlm.nih.gov/pubmed/33921788 http://dx.doi.org/10.3390/ijms22084231 |
Ejemplares similares
-
L‐serine biosynthesis in the human central nervous system: Structure and function of phosphoserine aminotransferase
por: Marchesani, Francesco, et al.
Publicado: (2023) -
Biochemical Properties of Human D-Amino Acid Oxidase
por: Murtas, Giulia, et al.
Publicado: (2017) -
Biochemical Properties and Physiological Functions of pLG72: Twenty Years of Investigations
por: Murtas, Giulia, et al.
Publicado: (2022) -
Human D-Amino Acid Oxidase: Structure, Function, and Regulation
por: Pollegioni, Loredano, et al.
Publicado: (2018) -
D-Amino Acids and Cancer: Friends or Foes?
por: Murtas, Giulia, et al.
Publicado: (2023)