Cargando…
Biochemical characterisation of fumarase C from a unicellular cyanobacterium demonstrating its substrate affinity, altered by an amino acid substitution
The tricarboxylic acid cycle produces NADH for oxidative phosphorylation and fumarase [EC 4.2.1.2] is a critical enzyme in this cycle, catalysing the reversible conversion of fumarate and l-malate. Fumarase is applied to industrial l-malate production as a biocatalyst. l-malate is used in a wide ran...
Autores principales: | Katayama, Noriaki, Takeya, Masahiro, Osanai, Takashi |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6650407/ https://www.ncbi.nlm.nih.gov/pubmed/31337820 http://dx.doi.org/10.1038/s41598-019-47025-7 |
Ejemplares similares
-
Substrate Specificity and Allosteric Regulation of a d-Lactate Dehydrogenase from a Unicellular Cyanobacterium are Altered by an Amino Acid Substitution
por: Ito, Shoki, et al.
Publicado: (2017) -
Three-dimensional ultrastructure of a unicellular cyanobacterium
Publicado: (1983) -
Purification and Characterisation of Malate Dehydrogenase From Synechocystis sp. PCC 6803: Biochemical Barrier of the Oxidative Tricarboxylic Acid Cycle
por: Takeya, Masahiro, et al.
Publicado: (2018) -
Genetic manipulation of a metabolic enzyme and a transcriptional regulator increasing succinate excretion from unicellular cyanobacterium
por: Osanai, Takashi, et al.
Publicado: (2015) -
Corrigendum: Purification and Characterisation of Malate Dehydrogenase From Synechocystis sp. PCC 6803: Biochemical Barrier of the Oxidative Tricarboxylic Acid Cycle
por: Takeya, Masahiro, et al.
Publicado: (2021)