An alternative mechanism for the nitrogen transfer reaction in asparagine synthetase.
In the absence of crystallographic data, the mechanism of nitrogen transfer from glutamine in asparagine synthetase (AS) remains under active investigation. Surprisingly, the glutamine-dependent AS from Escherichia coli (AsnB) appears to lack a conserved histidine residue, necessary for nitrogen transfer if the reaction proceeds by the accepted pathway in other glutamine amidotransferases, but retains the ability to synthesize asparagine. We propose an alternative mechanism for nitrogen transfer in AsnB which obviates the requirement for participation of histidine in this step. Our hypothesis may also be more generally applicable to other glutamine-dependent amidotransferases.
Department of Chemistry, University of Florida, Gainesville 32611.
N G
NG
Richards
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SM
Schuster
D000595:Amino Acid Sequence; D001217:Aspartate-Ammonia Ligase / Q000378:metabolism*; D005973:Glutamine / Q000378:metabolism*; D008969:Molecular Sequence Data; D009584:Nitrogen / Q000378:metabolism*
D005973:Glutamine; D001217:Aspartate-Ammonia Ligase; D009584:Nitrogen