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Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy
TLDR
It is shown that the S. aureus transpeptidase sortase A can be used to catalyze the ligation of two separately expressed domains of the same protein, MecA (B. subtilis), and the resultant HSQC spectrum obtained from this domain-labeled conjugate demonstrates successful application ofsortase A for segmental labeling of multi-domain proteins for solution NMR study.
The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase.
TLDR
The electrostatic surface potentials of the human GART domain and Escherichia coli enzyme explain differences in the binding affinity of polyglutamylated folates, and these differences have implications to future chemotherapeutic agent design.
The human trifunctional enzyme of de novo purine biosynthesis: heterologous expression, purification, and preliminary characterization.
TLDR
The correspondence of data obtained for the glycinamide ribonucleotide transformylase activity of the mammalian trifunctional enzyme indicates that the recombinant enzyme is fully functional.
Isotope-tapping experiments with rabbit liver fructose bisphosphatase.
TLDR
Rapid-quench isotope-trapping experiments confirm the requirement for structural Mn2+ ions for productive binding to occur and show that an ordered formation of the enzyme-Mn2+ s-D-fructose 1, 6-bisphosphate ternary complex constitutes a catalytically competent pathway in the mechanism of fructose 1,6-bisPhosphatase.
Mammalian glycinamide ribonucleotide transformylase: purification and some properties.
Glycinamide ribonucleotide transformylase, the first of the two formyl group transferases of de novo purine biosynthesis requiring 10-formyltetrahydrofolate, has been purified 1500-fold, nearly to
Binding and kinetic data for rabbit liver fructose-1,6-bisphosphatase with Zn2+ as cofactor.
TLDR
Observations suggest that fructose-1,6-bisphosphatase may function in vivo as a Zn(2+) metalloprotein, thus eliminating mixed metal species.
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