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Microbiology 143 (1997), 3279-3286; DOI  10.1099/00221287-143-10-3279
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Acetate kinase from Clostridium acetobutylicum: a highly specific enzyme that is actively transcribed during acidogenesis and solventogenesis

Klaus Winzer{dagger}, Karin Lorenz and Peter Dürre1

Angewandte Mikrobiologie und Mykoiogie, Universität Ulm, D-89069 Ulm, Germany

1 Author for correspondence: Peter Dürre. Tel: +49 731 502 2710. Fax: +49 731 502 2719. e-mail: peter.duerre@biologie.uni-ulm.de

ABSTRACT

Acetate kinase (ATP:phosphotransferase, EC 2.7.2.1) has been purified 294-fold from acid-producing cells of Clostridium acetobutylicum DSM 1731 to a specific activity of 1087 U mg-1 (ADP-forming direction). The dimeric enzyme consisted of subunits with a molecular mass of 43 kDa. The molecular mass of the native acetate kinase was in the range 87-94 kDa as judged by gel filtration and native gel electrophoresis. The enzyme showed high specificity for the substrates acetate and ATP, and maximal activity was obtained with Mn2+ as divalent cation. The presence of mercury compounds such as HgCl2 and p-hydroxymercuribenzoate resulted in an essential loss of activity. The apparent Km values for acetate, Mg-ATP, acetyl phosphate, and Mg-ADP were 73, 0.37, 0.58 and 0.71 mM. An activity-staining procedure for detection of acetate kinase in crude cell extracts after separation on native polyacrylamide gels was developed. A DNA fragment encoding 246 bp of the acetate kinase gene of C. acetobutylicum DSM 792 was cloned by a PCR-based approach. Northern blot analysis revealed transcription of the gene under acid- and solvent-producing conditions with no significant differences at the level of transcription.

Keywords: acetate kinase, ack gene, acidogenesis, butyrate kinase, Clostridium acetobutylicum

{ddagger} Present address: Department of Pharmaceutical Sciences, School of Pharmacy, University of Nottingham, University Park, Nottingham NG7 2RD, UK.




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