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W Babel

Publications and source records attributed to W Babel.

At least 73 records · Page 4Linked to original sources
PubMed1980

A critical analysis of kinetic data of 3-hexulosephosphate synthases. Michaelis-Menten or complex characteristics.

Investigations of the 3-hexulosephosphate synthase (HPS) from different methylotrophic bacteria have revealed apparent discrepancies in kinetic behaviour. In all methanol-utilizing species investigated by us the kinetic characteristics showed intermediary plateau regions. Therefore, this behaviour is assumed to be a general feature of the HPS from all non-methane-utilizing methylotrophic bacteria. However, this assumption is in contrast to the results of other authors. Both for Methylomonas M15 (SAHM et al. 1976) and Methylomonas aminofaciens 77a (KATO et al. 1977, 1978) MICHAELIS-MENTEN kinetics of the HPS were stated. To check the validity of our assumption we have analyzed the kinetic data given by others. Indications of the existence of intermediary plateau regions could be found with the enzyme from Arthrobacter globiformis (BYKOVSKAYA and VORONKOV 1977) and Methylomonas aminofaciens 77a (KATO et al. 1978). Furthermore, biphasic ARRHENIUS plots indicate a multiple character of the HPS from these species as could already be demonstrated with the enzyme from Bacterium MB 58 and Pseudomonas oleovorans. In addition, causes which may obscure the detection of intermediary plateau regions are demonstrated.

Aldehyde-Lyases↗
PubMed1980

Dihydroxyacetone kinase of methanol-assimilating yeast. I. Regulation of dihydroxyacetone kinase from Candida methylica in situ.

In order to investigate the control behaviour of dihydroxyacetone kinase of methanol-grown Candida methylica under nearly physiological conditions kinetic and regulatory studies were carried out in situ. Yeast cells were made permeable to substrate and reaction products by treatment with Triton X-100. Normal Michaelis-Menten kinetics resulted in dependence upon the dihydroxyacetone concentration, both at the pH optimum of 7.6 and near the physiological pH-value of 6.5. The Km obtained for dihydroxyacetone was 0.02 mM, independent of the pH-value. The plots of dihydroxyacetone kinase activity as a function of the ATP concentration revealed complex kinetic characteristics with plateau regions. The maximum reaction rate was reached only after a lag time both at pH 7.6 and concentrations of ATP higher than 5 mM and at pH 6.5 and concentrations of ATP higher than 1.25 mM. Among a great number of tested metabolites no inhibitors of dihydroxyacetone kinase were found. Dihydroxyacetone kinase activity depending upon energy charge according to Atkinson exhibited curves of the U-type. These results and further data concerning the regulation of other enzymes obtained with C. methylica and other yeasts were the basis to propose a preliminary overall model of fine control of the carbon and energy metabolism of methanol-utilizing yeasts.

Adenosine Triphosphate↗
PubMed1980

Regulation of NAD+- and NADP+-linked isocitrate dehydrogenase in the obligate methylotrophic bacterium Pseudomonas W6.

Cell-free extracts of the obligate methanol-utilizing bacterium Pseudomonas W6 catalyze the oxydation of isocitrate to alpha-ketoglutarate in the presence of NAD+ and NADP+. After electro-focusing of the crude extract of Pseudomonas W6 actually two distinct bands each of NAD+-linked isocitrate dehydrogenase (NAD+-IDH) and of NADP+-linked isocitrate dehydrogenase (NADP+-IDH) could be observed. The NAD+-IDH was completely separated from the NADP+-IDH by employing DEAE ion exchange chromatography and further purified by affinity chromatography using Cibacron blue F 3G-A. The NAD+-IDH was inhibited by a high energy charge, whereas the NADP+-IDH was found to be independent of energy charge. Consequently the NAD+-IDH showed the control behaviour of an enzyme of an energy-generating sequence which, however, equally fulfils a catabolic and an anabolic function. With respect to the inhibition by reduced pyridine nucleotides and alpha-ketoglutarate differences between NAD+-IDH and NADP+-IDH were also found. Only the NADP+-linked enzyme exhibited a feedback inhibition by its reaction products alpha-ketoglutarate and NADPH. This control behaviour gives evidence for the biosynthetic function of the NADP+-IDH. These results confer an amphibolic character to the sequence from citrate to alpha-ketoglutarate in the incomplete citric-acid cycle of Pseudomonas W6.

Cell-Free System↗
PubMed1978

Isolation of the ADP/ATP translocator from beef heart mitochondria as the bongkrekate-protein complex.

1. The isolation of the ADP/ATP translocator from beef heart mitochondria as the bongkrekateprotein complex is described, using hydroxyapatite chromatography and gel filtration in Triton X-100 solution. 2. The inhibitor is bound to the protein prior to solubilization with detergent for protection against denaturation. Only the intact bongkrekate-protein passes easily through the hydroxyapatite column. Bongkrekate shileds the protein in contrast to carboxyatractylate only partially against proteinases present in the crude extract. 3. The isolated bongkrekate protein shows the same molecular weights in dodecylsulfate and Triton X-100, the same amino acid composition and the same isoelectric point as the earlier isolated carboxyatractylate-protein complex. It differs by its higher sensitivity against trypsin and thermolysin. 4. The identity of both proteins is demonstrated by interconversion of the bongkrekate-protein into the carboxyatractylate-protein. The process requires the catalysis by ADP or ATP, the natural substrates of the protein. 5. The formation of the extractable [3H]bongkrekate-protein complex in mitochondria requires the presence of ADP or ATP. 6. These data, the immunological studies presented earlier, and the differences in the reactivity of -SH groups of the isolated bongkrekate and carboxyatractylate complexes (to be published) indicate that both proteins represent different conformational states of the translocator protein (m-state and c-state).

Adenosine Diphosphate↗