Ontology highlight
ABSTRACT:
SUBMITTER: Joyce MA
PROVIDER: S-EPMC3388811 | biostudies-literature | 2012 Jul
REPOSITORIES: biostudies-literature
Joyce Michael A MA Hayakawa Koto K Wolodko William T WT Fraser Marie E ME
Acta crystallographica. Section D, Biological crystallography 20120615 Pt 7
Succinyl-CoA synthetase (SCS) from Thermus aquaticus was characterized biochemically via measurements of the activity of the enzyme and determination of its quaternary structure as well as its stability and refolding properties. The enzyme is most active between pH 8.0 and 8.4 and its activity increases with temperature to about 339 K. Gel-filtration chromatography and sedimentation equilibrium under native conditions demonstrated that the enzyme is a heterotetramer of two α-subunits and two β-s ...[more]