KM1, a Bacteriophage of Clostridium butyricum

The amylase of Clostridium butyricum.

Phosphatidylserine decarboxylase from Clostridium butyricum.

Phosphatidylserine decarboxylase activity has been characterized in membrane preparations from Clostridium butyricum ATCC 19398. A particulate fraction was shown to catalyze the formation of phosphatidylethanolamine and plasmenylethanolamine when vesicles containing phosphatidylserine and plasmenylserine were used as substrate. No plasmenylethanolamine was formed when phosphatidylserine alone w...

Biotechnological potential of Clostridium butyricum bacteria

In response to demand from industry for microorganisms with auspicious biotechnological potential, a worldwide interest has developed in bacteria and fungi isolation. Microorganisms of interesting metabolic properties include non-pathogenic bacteria of the genus Clostridium, particularly C. acetobutylicum, C. butyricum and C. pasteurianum. A well-known property of C. butyricum is their ability ...

Reversal of pyruvate oxidation in Clostridium butyricum.

The failure to detect an equilibrium between acetyl phosphate, a product of pyruvate cleavage, and pyruvate has been one of the poorly understood observations of the pyruvate cleavage reactions in Clostridium butyricum and in Escherichia coli (l-3), although pyruvate synthesis from acetyl phosphate was reported in the latter organism (4). In the preceding paper (5) a small incorporation of acet...

Cofactors of the phosphoroclastic reaction of Clostridium butyricum.

The degradation of pyruvate, in the presence of phosphate, to acetate, carbon dioxide, and hydrogen by cell-free extracts of Clostridium butylicum was described by Koepsell and Johnson (1). Later acetyl phosphate, the labile precursor of the acetate, was shown to be produced (2, 3), and phosphotransacetylase was shown to be present in the cell-free extracts (4). This reaction is, at least, supe...