Existence and functions of two enzymes with beta-ketoadipate: succinyl-CoA transferase activity in Pseudomonas florescens.
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Biomedical subjects
Publications and source records attributed to R Y Stanier.
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Crystalline preparations of muconate lactonizing enzyme and muconolactone isomerase, two inducible enzymes that catalyze successive steps in the catechol branch of the beta-ketoadipate pathway, were used to prepare antisera. Both enzymes were isolated from a strain of Pseudomonas putida biotype A. The antisera did not cross-react with enzymes of the same bacterial strain that catalyze the chemically analogous steps in the protocatechuate branch of the beta-ketoadipate pathway, carboxymuconate lactonizing enzyme and carboxymuconolactone decarboxylase. The antisera gave heterologous cross-reactions of varying intensities with the muconate lactonizing enzymes and muconolactone isomerases of P. putida biotype B, P. aeruginosa, P. stutzeri, and all biotypes of P. fluorescens, but did not cross-react with the isofunctional enzymes of P. acidovorans, of P. multivorans, and of two bacterial species that belong to other genera. The evolutionary and taxonomic implications of the findings are discussed.
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The control of aspartokinase and homoserine dehydrogenase activities was compared in aerobic and fermentative pseudomonads (genera Pseudomonas and Aeromonas), and in coliform bacteria representative of the principal genera of the Enterobacteriaceae. Isofunctional aspartokinases subject to independent end-product control occur in the Enterobacteriaceae and in Aeromonas. In Pseudomonas, there appears to be a single aspartokinase, subject to concerted feedback inhibition by lysine and threonine. Within this genus, the sensitivity of aspartokinase to the single allosteric inhibitors varies considerably: the aspartokinase of the acidovorans group is little affected by the single inhibitors, whereas that of the fluorescent group is severely inhibited by either amino acid at high concentration. In all bacteria examined, homoserine dehydrogenase activity is inhibited by threonine; inhibition is more severe in aerobic pseudomonads than in the other groups. In most of the bacteria examined, either nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate can serve as a cofactor for this enzyme, though the relative activity with the two pyridine nucleotides varies widely. Aerobic pseudomonads of the acidovorans group contain a homoserine dehydrogenase that is absolutely specific for NAD. The taxonomic implications of these findings are discussed.
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A number of strains of oxidase-positive moraxellas and of neisserias related to Neisseria catarrhalis were characterized with respect to a number of nutritional and physiological properties and could be assigned to several species or species groups on the basis of their phenotypic traits. This grouping was consistent with that established by Bövre on the basis of transformation frequencies for streptomycin resistance. It is proposed to reserve the generic name Moraxella for the oxidase-positive rodshaped organisms, and a redescription of the genus is offered. Following the recent taxonomic proposals of Bövre and Henriksen, the specific name Moraxella osloensis is applied to the nutritionally unexacting strains that accumulate poly-beta-hydroxybutyrate as carbon reserve. The nutritionally exacting strains are assigned to three distinct groups which can be regarded as separate species or as varieties of M. lacunata. The epithets applicable to these groups appear to be lacunata, nonliquefaciens, and bovis. The "false neisserias" could be assigned to at least three subgroups, one of which constitutes the clearly defined entity, N. catarrhalis, which could be distinguished from N. caviae and N. ovis.
A number of nutritional and biochemical properties of more than 100 strains of the oxidase-negative moraxellas (the Mima-Herellea-Acinetobacter group of bacteria) were studied. These properties included the range of carbon sources that can support growth, the utilization of nitrate, the production of proteolytic and lipolytic enzymes, and the reactions involved in the oxidation of sugars and of aromatic compounds. No evidence could be obtained for the accumulation of either poly-beta-hydroxybutyrate or polysaccharide as intracellular reserve materials. Of 158 different compounds tested, the group as a whole could use 85 as sole carbon sources for growth. The nutritional spectra of the individual strains, however, differed widely, with a range of from 17 to 74 alternative substrates. On the basis of 56 selected nutritional and physiological characters used for a numerical analysis, the collection could be divided into two major groups of strains comprising at least seven less clearly defined clusters. Neither the hydrolysis of gelatin nor acid production from aldose sugars was found to be a reliable index of strain affinities indicated by the phenotypic analysis, although both properties were of some use in distinguishing between the subgroups. For reasons that are discussed, we propose that the oxidase-negative moraxellas be placed in the genus Acinetobacter Brisou and Prévot, for which a modified description is presented. A. calco-aceticus (Beijerinck) is proposed as the type species, of which anitratum is regarded as a synonym or variety. On the basis of the present studies and unpublished supporting evidence provided by M. Mandel on deoxyribonucleic acid (DNA) composition and by J. Johnson on DNA homologies, it is proposed that two other species in the genus, A. lwoffi (Audureau) and A. hemolysans (Henriksen), as well as one subspecies, A. hemolysans haemolyticus (Stenzel and Mannheim), be recognized provisionally.
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