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Identification of histidyl and cysteinyl residues essential for catalysis by 5′‐nucleotidase
Author(s) -
Worku Yesehak,
Paul Luzio J.,
Newby Andrew C.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80133-7
Subject(s) - 5' nucleotidase , biochemistry , histidine , phosphatase , enzyme , chemistry , residue (chemistry) , nucleotidase , active site , cytosol , stereochemistry
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.