Purification and properties of acetate kinase fromClostridium thermoaceticum

✍ Scribed by Annabella Schaupp; Lars G. Ljungdahl

• Publisher: Springer
• Year: 1974
• Tongue: English
• Weight: 526 KB
• Volume: 100
• Category: Article
• ISSN: 0302-8933
• DOI: 10.1007/bf00446312

✦ Synopsis

Acetate kinase (ATP: acetate phosphotransferase E C 2.7.2.1) has been purified from Clostrldium thermoaceticum. The enzyme of a specific activity of 282 ~moles rain -1 nag -1 appeared homogeneous as judged from Sephadex chromate. graphy and sedimentation velocity. Polyacrytamide gel electrophoretic patterns at ptI 9.0 and 9.5 showed heterogeneity. Velocity curves obtained with varying amount of acetate were of the Michaelis-~enten type with an apparent K~ of 0.135 M. With varying amounts of ATP sigmoidal kinetic was observed (S0.s = 1.64 raM), suggesting cooperative binding of this substrate. The enzyme had only moderate thermal stability with a temperature optimum of about 60 ~ C and exhibited a broken line in an Arrhenius graph. From gel filtration a molecular weight of about 60000 daltons was estimated for the enzyme~ The S~0w value was 6.0 S.