Characterization of a novel nucleolytic activity of acylphosphatases.
A novel enzymatic activity on nucleic acids was discovered in both muscle type (MT) and erythrocyte or common type (CT) isoforms of acylphosphatase, an enzyme that was previously known as a hydrolase (E.C.3.6.1.7). Both deoxyribonucleic and ribonucleic hydrolitic activity were assayed on a variety of substrates. Our results demonstrate that acylphosphatase possesses both Mg++ dependent deoxyribonuclease and ribonuclease activities, at pH ranging from 5.0 to 6.8. Furthermore, we present evidences, for both isoenzymatic forms, of the coexistence of exonucleolytic and endonucleolytic activities on DNA.
Chiarugi
P
P
Department of Biochemical Sciences, University of Florence, Italy.
Raugei
G
G
Fiaschi
T
T
Taddei
L
L
Camici
G
G
Ramponi
G
G
D017766:Acid Anhydride Hydrolases / Q000378:metabolism*; D004247:DNA / Q000378:metabolism*; D004587:Electrophoresis, Agar Gel; D004912:Erythrocytes / Q000201:enzymology; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism*; D008274:Magnesium / Q000378:metabolism; D009132:Muscles / Q000201:enzymology; D010957:Plasmids / Q000378:metabolism; D012313:RNA / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D004247:DNA; D007527:Isoenzymes; D008274:Magnesium; D012313:RNA; D015032:Zinc; D000097024:Acylphosphatase