AN ALTERNATIVE MECHANISM FOR THE NITROGEN TRANSFER-REACTION IN ASPARAGINE SYNTHETASE

被引:28
作者
RICHARDS, NGJ [1 ]
SCHUSTER, SM [1 ]
机构
[1] UNIV FLORIDA,J HILLIS MILLER HLTH CTR,DEPT BIOCHEM & MOLEC BIOL,GAINESVILLE,FL 32610
关键词
ASPARAGINE SYNTHETASE; NITROGEN TRANSFER; THIOL PROTEASE; GLUTAMINE; ESCHERICHIA-COLI;
D O I
10.1016/0014-5793(92)81421-H
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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 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.
引用
收藏
页码:98 / 102
页数:5
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