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Microbiology 145 (1999), 1839-1847; DOI  10.1099/13500872-145-8-1839
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The glyceraldehyde-3-phosphate dehydrogenase of Clostridium acetobutylicum: isolation and purification of the enzyme, and sequencing and localization of the gap gene within a cluster of other glycolytic genes

Wiebke Schreiber and Peter Dürre

Mikrobiologie und Biotechnologie, Universität Ulm, D-89069 Ulm, Germany

Author for correspondence: Peter Dürre. Tel: +49 731 50 22710. Fax: +49 731 50 22719. e-mail: peter.duerre@biologie.uni-ulm.de

ABSTRACT

Glyceraldehyde-3-phosphate dehydrogenase was purified from Clostridium acetobutylicum by sequential ammonium sulfate precipitation, gel filtration and anion-exchange chromatography (to a specific activity of 27 U mg-1). The enzyme had a molecular mass of 40 kDa as determined by SDS-PAGE and a native molecular mass of 160 kDa as determined by nondenaturing PAGE, indicating that it has a homotetrameric composition. Its pH optimum was between 8.5 and 9.3. The corresponding gene (gap) was cloned and sequenced from C. acetobutylicum DSM 792 and found to cluster with other genes of enzymes from the glycolytic pathway (pgk, phosphoglycerate kinase; tpi, triosephosphate isomerase; pgm(i), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase). No sequences resembling rho-independent transcription terminators were found in the intergenic regions. A plasmid carrying the clostridial gap gene complemented an Escherichia coli gap mutant.

Keywords: GAPDH, glycolytic gene cluster, Clostridium acetobutylicum

The GenBank accession number for the sequence reported in this paper is AF043386.

Abbreviations: GAPDH, glyceraldehyde-3-phosphate dehydrogenase; PGK, phosphoglycerate kinase; PGM, phosphoglycerate mutase; PGM(i), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase; TPI, triosephosphate isomerase.

Received 23 December 1998; revised 10 March 1999; accepted 9 April 1999.


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