Partial Purification and Properties of a Highly Specific Trehalose Phosphate Phosphatase from Mycobacterium smegmatis
AUTOR(ES)
Matula, Mike
RESUMO
A specific trehalose phosphate phosphatase was purified approximately 50-fold from Mycobacterium smegmatis. The enzyme had a pH optimum of about 7.0 and was stimulated by Mg2+. The optimum concentration of Mg2+ was about 1.5 × 10−3m. Of other divalent cations tested, only Co2+ showed some activity. The Km for trehalose phosphate was found to be about 1.5 × 10−3m. The enzyme showed slight activity toward mannose-6-P and fructose-6-P but was inactive on a large number of other phosphorylated compounds. Citrate was a competitive inhibitor of the enzyme both with respect to trehalose phosphate concentration and Mg2+ concentration. This inhibition appears to be due to chelation of Mg2+ by this compound. Ethylenediaminetetraacetic acid and NaF were also inhibitors of the enzyme, but these inhibitions were noncompetitive.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=246907Documentos Relacionados
- Purification and partial characterization of a penicillin-binding protein from Mycobacterium smegmatis.
- Levels of Glycogen and Trehalose in Mycobacterium smegmatis and the Purification and Properties of the Glycogen Synthetase
- Purification, Properties, and Cytotoxic Effect of a Bacteriocin from Mycobacterium smegmatis
- Purification of a novel coenzyme F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis.
- Purification and properties of phytate-specific phosphatase from Bacillus subtilis.
