Cargando…
Substrate Promiscuity of N-Acetylhexosamine 1-Kinases
N-Acetylhexosamine 1-kinase (NahK) catalyzes the direct addition of a phosphate from adenosine 5'-triphosphate (ATP) to the anomeric position of N-acetylhexosamine and shows similar activity towards N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc). Herein we report the cloning, c...
Autores principales: | Li, Yanhong, Yu, Hai, Chen, Yi, Lau, Kam, Cai, Li, Cao, Hongzhi, Tiwari, Vinod Kumar, Qu, Jingyao, Thon, Vireak, Wang, Peng George, Chen, Xi |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6264712/ https://www.ncbi.nlm.nih.gov/pubmed/21799473 http://dx.doi.org/10.3390/molecules16086396 |
Ejemplares similares
-
Differential Response of Chondrocytes and Chondrogenic-Induced Mesenchymal Stem Cells to C1-OH Tributanoylated N-Acetylhexosamines
por: Coburn, Jeannine M., et al.
Publicado: (2013) -
NRPS Substrate Promiscuity Diversifies the Xenematides
por: Crawford, Jason M., et al.
Publicado: (2011) -
MTH1 Substrate Recognition—An Example of Specific Promiscuity
por: Nissink, J. Willem M., et al.
Publicado: (2016) -
Discovery of novel geranylgeranyl reductases and characterization of their substrate promiscuity
por: Meadows, Corey W., et al.
Publicado: (2018) -
Enzyme promiscuity shapes adaptation to novel growth substrates
por: Guzmán, Gabriela I, et al.
Publicado: (2019)