PMID: 41533Dec 15, 1978

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

Bollettino della Società italiana di biologia sperimentale
A OlivaA Gambacorta

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.

Related Concepts

Chlamydomonas acidophila
Phosphate Measurement
Pentosyltransferase
5'-Methylthioadenosine phosphorylase
Purification Aspects
Nicotinamide Riboside Phosphorylase
Thionucleosides
Assay
S-Methyl-5'-Thioadenosine Phosphorylase
Phosphate ion

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