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The solution structure of the native K50 Bicoid homeodomain bound to the consensus TAATCC DNA-binding site.
Purification of a complex catalyzing folate cofactor synthesis and transformylation in de novo purine biosynthesis.
Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy
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.
Carbocyclic glycinamide ribonucleotide is a substrate for glycinamide ribonucleotide transformylase.
The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase.
- T. Dahms, G. Sainz, E. Giroux, C. Caperelli, Janet L. Smith
- Biology, ChemistryBiochemistry
- 26 July 2005
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.
The correspondence of data obtained for the glycinamide ribonucleotide transformylase activity of the mammalian trifunctional enzyme indicates that the recombinant enzyme is fully functional.
PvdF of pyoverdin biosynthesis is a structurally unique N10-formyltetrahydrofolate-dependent formyltransferase.
Isotope-tapping experiments with rabbit liver fructose bisphosphatase.
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.
- C. Caperelli
- 12 March 1985
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.
- P. Benkovic, C. Caperelli, M. D. de Maine, S. Benkovic
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 1 May 1978
Observations suggest that fructose-1,6-bisphosphatase may function in vivo as a Zn(2+) metalloprotein, thus eliminating mixed metal species.