Year: 1992
Type: article
Abstract: 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.
Source: FEBS Letters
Authors: Nigel G.J. Richards, Sheldon M. Schuster
Institution: University of Florida
Language: English
Subfield: Biochemistry
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W2056157112