Glu-108 is essential for subunit assembly and dimer stability of d-phosphoglycerate dehydrogenase from Entamoeba histolytica
Author:
Funder
CSIR New Delhi
Publisher
Elsevier BV
Subject
Molecular Biology,Parasitology
Reference29 articles.
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3. Novel mutations in 3-phosphoglycerate dehydrogenase (PHGDH) are distributed throughout the protein and result in altered enzyme kinetics;Tabatabaie;Hum Mutat,2009
4. Crystal structure of Mycobacterium tuberculosis d-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits;Dey;J Biol Chem,2005
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2. Dimerization of PHGDH via the catalytic unit is essential for its enzymatic function;Journal of Biological Chemistry;2021-01
3. Iron-modulated virulence factors of Entamoeba histolytica;Future Microbiology;2018-09
4. Oligomerization of the Sec7 domain Arf guanine nucleotide exchange factor GBF1 is dispensable for Golgi localization and function but regulates degradation;American Journal of Physiology-Cell Physiology;2016-03-15
5. Characterization of pH-induced transitions of Entamoeba histolytica d-phosphoglycerate dehydrogenase;International Journal of Biological Macromolecules;2015-08
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