Corpus ID: 10462938

Kinetics and properties of beta-ketothiolase from Clostridium pasteurianum.

  title={Kinetics and properties of beta-ketothiolase from Clostridium pasteurianum.},
  author={H. Berndt and H. Schlegel},
  journal={Archives of microbiology},
  volume={103 1},
1. Beta-Ketothiolase of Clostridium pasteurianum was purified 130-fold by ammonium sulphate fractionation and by column chromatography using DEAE-Sephadex A-50 and hydroxylapatite. Subjected to gel electrophoresis beta-ketothiolase revealed two distinct bands; by isoelectric focusing two enzymes with isoelectric points at pH 4.5 and 7.6 were separated. As established by sucrose density gradient centrifugation the molecular weight of both enzymes was found to be 158000. 2. The condensation… Expand
Purification and properties of β-ketothiolase from Zoogloea ramigera
Abstractβ-Ketothiolase from Zoogloea ramigera I-16-M was purified 140-fold to electrophoretic homogeneity. The bacterium appeared to contain a single isoenzyme of β-ketothiolase with a molecularExpand
A thermostable #x003B2;-ketothiolase of polyhydroxyalkanoates (PHAs) in Thermus thermophilus: Purification and biochemical properties
Polyhydroxyalkanoates (PHAs) are polyesters of hydroxyalkanoates (HAs) synthesised by numerous bacteria as intracellular carbon and energy storage compounds which accumulate as granules in theExpand
Acetyl coenzyme A and coenzyme A contents of growing Clostridium kluyveri as determined by isotope assays
While disulfides of coenzyme A were undetectable, 0.13 μmol CoASH and 1.17 μmol of total acyl-SCoA per g wet wt. Expand
α-Isopropylmalate synthase as a marker for the leucine biosynthetic pathway in several clostridia and in Bacteroides fragilis
  • J. Wiegel
  • Biology, Medicine
  • Archives of Microbiology
  • 2004
It is suggested that in these anaerobic bacteria the α-isopropylmalate pathway is present in addition to the pathway via the ferrodoxin-dependent, reductive carboxylation of branched chain fatty acids. Expand
Cloning, Expression and Characterization of a Thiolase Gene from Clostridium pasteurianum
A thl gene encoding the thiolase (EC of Clostridium pasteurianum was cloned by thermal asymmetric interlaced (TAIL) PCR and should be classified as a biosynthetic thiol enzyme with three conserved residues Cys89, Cys382 and His352. Expand
Production of medium-chain carboxylic acids by Megasphaera sp. MH with supplemental electron acceptors
This is the first report on the production of high-titer heptanoic Acid and octanoic acid using a pure anaerobic culture and further metabolic activities of Megaspahera sp. Expand