[5'-methylthioadenosine phosphorylase from Caldariella acidophila. 1. Purification and partial characterization]

Boll Soc Ital Biol Sper. 1978 Dec 15;54(23):2355-61.
[Article in Italian]

Abstract

5'-Methylthioadenosine phosphorylase has been isolated from C.acidophila, a thermophilic bacterium living in acid hot springs at temperatures ranging from 63 to 89 degrees C. The enzyme has been purified to homogeneity in 32% yield. The enzyme shows a high degree of thermophilicity, its temperature optimum being 93 degrees C in the in vitro assay. The enzyme is exceptionally stable; no loss of activity was observable after exposure for 1 h at 100 degrees C. The optimum pH is about 7,2, with one-half of the maximal activity occurring at pH 6 and 9. The apparent Km for the substrates are: 8,3 x 10(-5) M for MTA and 4,3 x 10(-4) M for phosphate ions.

MeSH terms

  • Adenosine / analogs & derivatives
  • Bacteria / enzymology*
  • Chemical Precipitation
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Indicators and Reagents
  • Kinetics
  • Pentosyltransferases / isolation & purification*
  • Purine-Nucleoside Phosphorylase / isolation & purification*
  • Thionucleosides

Substances

  • Indicators and Reagents
  • Thionucleosides
  • Pentosyltransferases
  • Purine-Nucleoside Phosphorylase
  • 5'-methylthioadenosine phosphorylase
  • Adenosine