Identification of histidyl and cysteinyl residues essential for catalysis by 5'-nucleotidase.
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.
D015720:5'-Nucleotidase; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D002462:Cell Membrane / Q000201:enzymology; D003545:Cysteine; D003600:Cytosol / Q000201:enzymology; D006639:Histidine; D008099:Liver / Q000201:enzymology; D009708:Nucleotidases / Q000037:antagonists & inhibitors; D051381:Rats; D013439:Sulfhydryl Reagents / Q000494:pharmacology
D013439:Sulfhydryl Reagents; D006639:Histidine; D009708:Nucleotidases; D015720:5'-Nucleotidase; D003545:Cysteine