Identification of histidyl and cysteinyl residues essential for catalysis by 5′‐nucleotidase

FEBS Letters

Newby, Andrew C.¹  Paul Luzio, J.¹  Worku, Yesehak¹ 

[1] Department of Clinical Biochemistry, University of Cambridge, Addenbrooke's Hospital, Hills Road, Cambridge CB2 2QR, England

关键词: 5′Nucleotidase;    Diethylpyrocarbonate;    Histidine;    Cysteine;    Phosphatase;    Catalytic mechanism;   

DOI  :  10.1016/0014-5793(84)80133-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Inactivation of both cytosolic 5′-nucleotidase and ecto-5′-nucleotidase by diethylpyrocarbonate indicated the presence of an essential histidyl residue which in the cytosolic enzyme was conclusively located at the active site. Inactivation by thiol reagents indicated the presence of an essential cysteinyl residue in both enzymes. The data suggest that both 5′-nucleotidases belong to a group of histidine phosphatases which also includes glucose-6-phosphatase and acid phosphatase. A working hypothesis for the catalytic mechanism of these enzymes is proposed.

【 授权许可】

Unknown