Purification and characterization of an inorganic pyrophosphatase from the extreme thermophile Thermus aquaticus.
AUTOR(ES)
Verhoeven, J A
RESUMO
An inorganic pyrophosphatase was purified over 600-fold to homogeneity as judged by polyacrylamide gel electrophoresis. The enzyme is a tetramer of Mr = 84,000, has a sedimentation coefficient of 5.8S, a Stokes radius of 3.5 nm, and an isoelectric point of 5.7. Like the enzyme of Escherichia coli, the pyrophosphatase appears to be made constitutively. The pH and temperature optima are 8.3 and 80 degrees C, respectively. The Km for PPi is 0.6 mM. A divalent cation is essential, with Mg2+ preferred. The enzyme uses only PPi as a substrate.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=213453Documentos Relacionados
- Deoxyribonucleic acid polymerase from the extreme thermophile Thermus aquaticus.
- Protein turnover in the extreme thermophile Thermus aquaticus.
- Fine Structure of Thermus aquaticus, an Extreme Thermophile
- Thermus aquaticus gen. n. and sp. n., a Nonsporulating Extreme Thermophile
- Thermostable polynucleotide phosphorylases from Bacillus stearothermophilus and Thermus aquaticus.