The mechanism of nitrogen transfer in glutamine-dependent amidotransferases remains to
be unambiguously established. We now report the overexpression, purification, and kinetic …

Although Arg-30, Asn-74, and Asn-79 appear totally conserved throughout the purF
glutamine-dependent amidotransferases, their potential roles in catalysis and binding …

In the absence of crystallographic data, the mechanism of nitrogen transfer from glutamine in
asparagine synthetase (AS) remains under active investigation. Surprisingly, the glutamine …

Escherichia coli asparagine synthetase B (AS-B) catalyzes the synthesis of asparagine from
aspartic acid and glutamine in an ATP-dependent reaction. The ability of this enzyme to …

Cys-1 mutants of recombinant human asparagine synthetase were constructed and their
ability to catalyze the glutamine-dependent nitrogen transfer reaction required for …

Escherichia coli asparagine synthetase B (AS-B) catalyzes the synthesis of asparagine from
aspartate, glutamine, and ATP. A combination of kinetic, isotopic-labeling, and stoichiometry …

Escherichia coli asparagine synthetase B (AS-B) catalyzes the formation of asparagine from
aspartate in an ATP-dependent reaction for which glutamine is the in vivo nitrogen source. In …

In experiments aimed at determining the mechanism of nitrogen transfer in purF
amidotransferase enzymes, 13C and 15N kinetic isotope effects have been measured for …

X-ray crystal structures of glutamine-dependent amidotransferases in their “active”
conformation have revealed the existence of multiple active sites linked by solvent …

Asparagine synthetase B catalyzes the assembly of asparagine from aspartate, Mg2+ ATP,
and glutamine. Here, we describe the three-dimensional structure of the enzyme from …