Ontology highlight
ABSTRACT:
SUBMITTER: Zhang L
PROVIDER: S-EPMC7470045 | biostudies-literature | 2020 Sep
REPOSITORIES: biostudies-literature
Zhang L L Liu M R MR Yao Y C YC Bostrom I K IK Wang Y D YD Chen A Q AQ Li J X JX Gu S H SH Ji C N CN
Acta crystallographica. Section F, Structural biology communications 20200819 Pt 9
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in the glycolytic pathway that catalyzes the conversion of D-glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Here, the full-length GAPDH type 1 from Escherichia coli (EcGAPDH1) was cloned and overexpressed, and the protein was purified. Biochemical analyses found that the optimum reaction temperature and pH of EcGAPDH1 were 55°C and 10.0, respectively. The protein has a certain amount of thermostability. Crystals of EcGAPDH1 ...[more]