Publications

• Mechanism of enzymic acetylation of des-acetyl citrate lyase.

  Schmellenkamp H., Eggerer H.

  A new enzyme, acetate:SH-[acyl-carrier-protein] enzyme ligase (AMP), has been purified about 30-fold from cell-free extracts of Klebsiella aerogenes. The enzyme, in the presence of acetate and ATP, catalyzes the acetylation of enzymically inactive des-acetyl citrate lyase to enzymically active cit ... >> More

  A new enzyme, acetate:SH-[acyl-carrier-protein] enzyme ligase (AMP), has been purified about 30-fold from cell-free extracts of Klebsiella aerogenes. The enzyme, in the presence of acetate and ATP, catalyzes the acetylation of enzymically inactive des-acetyl citrate lyase to enzymically active citrate lyase (EC 4.1.3.6). Acetate and ATP could be replaced by acetyl adenylate. Acetyl-CoA can act as acetyl donor in this activation only if trace amounts of adenine nucleotides and auxiliary enzymes are present. These allow formation of acetyl adenylate in acetate- and ATP-generating reactions. << Less

  Proc Natl Acad Sci U S A 71:1987-1991(1974) [PubMed] [EuropePMC]

• Covalent modification of citrate lyase ligase from Clostridium sphenoides by phosphorylation/dephosphorylation.

  Antranikian G., Herzberg C., Gottschalk G.

  Citrate lyase ligase was shown to be present in Clostridium sphenoides actively degrading citrate. In contrast to citrate lyase ligase from C. sporosphaeroides and Streptococcus lactis, the enzyme from C. sphenoides was under stringent regulatory control. The alteration of the kinetic properties o ... >> More

  Citrate lyase ligase was shown to be present in Clostridium sphenoides actively degrading citrate. In contrast to citrate lyase ligase from C. sporosphaeroides and Streptococcus lactis, the enzyme from C. sphenoides was under stringent regulatory control. The alteration of the kinetic properties of the enzyme after depletion of citrate suggested the presence of two different enzyme species in different phases of growth: active and partially active citrate lyase ligase. These enzymes were purified from in vivo 32P-labeled C. sphenoides cells, which were grown on low-phosphate medium containing 40 mM citrate and 1 mCi [32]orthophosphate. During enzyme purification only the active form of citrate lyase ligase was shown to be radioactively labeled. Growth experiments with 14C-labeled precursors of purines and pyrimidines and subsequent purification of active citrate lyase ligase indicated that the 32P labeling of the enzyme was not due to the incorporation of a nucleotide. Inactivation of the ligase after its treatment with acid phosphatase also suggested that the active form of the enzyme is phosphorylated. Citrate lyase ligase, therefore, is the first known enzyme in an anaerobic bacterium whose activity is modulated by phosphorylation/dephosphorylation. << Less

  Eur J Biochem 153:413-420(1985) [PubMed] [EuropePMC]

• Characterization of citrate lyase from Clostridium sporosphaeroides.

  Quentmeier A., Antranikian G.

  Cells of Clostridium sporosphaeroides which were grown on citrate contained citrate lyase and citrate lyase acetylating enzyme, but no detectable citrate synthase and citrate lyase deacetylase activities. Citrate lyase from C. sporosphaeroides was purified to homogeneity as judged by polyacrylamid ... >> More

  Cells of Clostridium sporosphaeroides which were grown on citrate contained citrate lyase and citrate lyase acetylating enzyme, but no detectable citrate synthase and citrate lyase deacetylase activities. Citrate lyase from C. sporosphaeroides was purified to homogeneity as judged by polyacrylamide gel electrophoresis and high performance liquid chromatography. In contrast to the enzyme from Clostridium sphenoides, the addition of L-glutamate was not necessary for activity and stabilization of the enzyme. The purified enzyme had a specific activity of 34 U/mg protein and was comparable to other citrate lyases with respect to its molecular weight and subunit composition. Electron microscopic investigations showed that similar to the lyase from C. sphenoides and in contrast to all other citrate lyases examined so far, the majority of the enzyme molecules was present in "star" form. << Less

  Arch Microbiol 141:85-90(1985) [PubMed] [EuropePMC]

• Copurification of citrate lyase and citrate lyase ligase from Rhodopseudomonas gelatinosa and subsequent separation of the two enzymes.

  Antranikian G., Gottschalk G.

  A procedure has been worked out which allowed the purification and crystallization of a citrate lyase/citrate lyase ligase complex from Rhodopseudomonas gelatinosa. The complex was subsequently separated to yield two homogeneous enzymes. Citrate lyase ligase was purified 365-fold with a yield of 3 ... >> More

  A procedure has been worked out which allowed the purification and crystallization of a citrate lyase/citrate lyase ligase complex from Rhodopseudomonas gelatinosa. The complex was subsequently separated to yield two homogeneous enzymes. Citrate lyase ligase was purified 365-fold with a yield of 3.23%. The molecular weight of the enzyme was estimated to be 39500, the enzyme consisted of one polypeptide chain. The reaction rates for ATP, acetate and citrate lyase (sulfhydryl form) followed Michaelis-Menten kinetics (Km values: 0.14 mM, 5 mM and 37 nM respectively). Citrate lyase ligase exhibited a high substrate specificity and could not react with citrate lyases from nonphototrophic microorganisms. In contrast to the ligase from Streptococcus diacetilactis, the enzyme from R. gelatinosa was extremely labile; however, it could be stabilized by nucleotides, the most potent stabilizing one being ADP. << Less

  Eur J Biochem 126:43-47(1982) [PubMed] [EuropePMC]