Literature DB >> 8886272

Characterization of a novel nucleolytic activity of acylphosphatases.

P Chiarugi1, G Raugei, T Fiaschi, L Taddei, G Camici, G Ramponi.   

Abstract

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.

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Year:  1996        PMID: 8886272     DOI: 10.1080/15216549600201552

Source DB:  PubMed          Journal:  Biochem Mol Biol Int        ISSN: 1039-9712


  3 in total

1.  Mechanism of acylphosphatase inactivation by Woodward's reagent K.

Authors:  P Paoli; T Fiaschi; P Cirri; G Camici; G Manao; G Cappugi; G Raugei; G Moneti; G Ramponi
Journal:  Biochem J       Date:  1997-12-15       Impact factor: 3.857

2.  Common-type acylphosphatase: steady-state kinetics and leaving-group dependence.

Authors:  P Paoli; P Cirri; L Camici; G Manao; G Cappugi; G Moneti; G Pieraccini; G Camici; G Ramponi
Journal:  Biochem J       Date:  1997-10-01       Impact factor: 3.857

3.  Acylphosphatase possesses nucleoside triphosphatase and nucleoside diphosphatase activities.

Authors:  P Paoli; G Camici; G Manao; E Giannoni; G Ramponi
Journal:  Biochem J       Date:  2000-07-01       Impact factor: 3.857

  3 in total

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