An alternative mechanism for the nitrogen transfer reaction in asparagine synthetase

FEBS Letters

Richards, Nigel G.J.²  Schuster, Sheldon M.¹ 

[1] Department of Biochemistry and Molecular Biology, J. Hillis Miller Health Center, University of Florida, Gainesville, FL 32610, USA;Department of Chemistry, University of Florida, Gainesville, FL 32611, USA

关键词: Asparagine synthetase;    Nitrogen transfer;    Thiol protease;    Glutamine;    Escherichia coli;   

DOI  :  10.1016/0014-5793(92)81421-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 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.

【 授权许可】

Unknown