Identification of histidyl and cysteinyl residues essential for catalysis by 5′‐nucleotidase
- 27 February 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 167 (2), 235-240
- https://doi.org/10.1016/0014-5793(84)80133-7
Abstract
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.Keywords
This publication has 27 references indexed in Scilit:
- Purification and Characterization of Bovine Brain 5′‐NucleotidaseJournal of Neurochemistry, 1982
- What do ectoenzymes do?Trends in Biochemical Sciences, 1982
- A monoclonal antibody inhibiting rat liver 5′-nucleotidaseFEBS Letters, 1981
- Purification and some properties of cytosol 5′-nucleotidase from rat liverBiochimica et Biophysica Acta (BBA) - Enzymology, 1981
- Effect of sodium deoxycholate on 5′-nucleotidaseBiochimica et Biophysica Acta (BBA) - Biomembranes, 1976
- Detection and characterization of the phosphorylated form of microsomal glucose-6-phosphataseBiochemical and Biophysical Research Communications, 1969
- Reactions of Nucleophilic Reagents with Phosphoramidate1Journal of the American Chemical Society, 1965
- Sulfonyl Fluorides as Inhibitors of Esterases. I. Rates of Reaction with Acetylcholinesterase, α-Chymotrypsin, and TrypsinJournal of the American Chemical Society, 1963
- Some Consequences of the “Non-competitive” Inhibition by Glucose of Rat Liver Glucose 6-Phosphatase1Journal of the American Chemical Society, 1959
- Isotopic exchange criteria for enzyme mechanismsDiscussions of the Faraday Society, 1955