22 results on '"Vander Wauven, C"'
Search Results
2. The Arginine Deiminase Pathway in Rhizobium etli: Functional Study of the arcABC Genes
- Author
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Lerouge, I., D’hooghe, I., Michiels, J., Vander Wauven, C., Stalon, V., Vanderleyden, J., Summerfield, R. J., editor, Elmerich, C., editor, Kondorosi, A., editor, and Newton, W. E., editor
- Published
- 1998
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3. Comparative degradation by micro-organisms of terephthalic acid, 2,6-naphthalene dicarboxylic acid, their esters and polyesters
- Author
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Lefèvre, C., Mathieu, C., Tidjani, A., Dupret, I., Vander Wauven, C., De Winter, W., and David, C.
- Published
- 1999
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4. The arginine deiminase pathway in Rhizobium etli: DNA sequence analysis and functional study of the arcABC genes
- Author
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D'Hooghe, I, primary, Vander Wauven, C, additional, Michiels, J, additional, Tricot, C, additional, de Wilde, P, additional, Vanderleyden, J, additional, and Stalon, V, additional
- Published
- 1997
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5. Biodegradation of polycaprolactone by micro-organisms from an industrial compost of household refuse
- Author
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Lefebvre, F., primary, David, C., additional, and Vander Wauven, C., additional
- Published
- 1994
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6. Regulation of enzyme synthesis in the arginine deiminase pathway of Pseudomonas aeruginosa
- Author
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Mercenier, A, Simon, J P, Vander Wauven, C, Haas, D, and Stalon, V
- Abstract
The three enzymes of the arginine deiminase pathway in Pseudomonas aeruginosa strain PAO were induced strongly (50- to 100-fold) by a shift from aerobic growth conditions to very low oxygen tension. Arginine in the culture medium was not essential for induction, but increased the maximum enzyme levels twofold. The induction of the three enzymes arginine deiminase (EC 3.5.3.6), catabolic ornithine carbamoyltransferase (EC 2.1.3.3), and carbamate kinase (EC 2.7.2.3) appeared to be coordinate. Catabolic ornithine carbamoyltransferase was studied in most detail. Nitrate and nitrite, which can replace oxygen as terminal electron acceptors in P. aeruginosa, partially prevented enzyme induction by low oxygen tension in the wild-type strain, but not in nar (nitrate reductase-negative) mutants. Glucose was found to exert catabolite repression of the deiminase pathway. Generally, conditions of stress, such as depletion of the carbon and energy source or the phosphate source, resulted in induced synthesis of catabolic ornithine carbamoyltransferase. The induction of the deiminase pathway is thought to mobilize intra- and extracellular reserves of arginine, which is used as a source of adenosine 5'-triphosphate in the absence of respiration.
- Published
- 1980
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7. Pseudomonas aeruginosa mutants affected in anaerobic growth on arginine: evidence for a four-gene cluster encoding the arginine deiminase pathway
- Author
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Vander Wauven, C, Piérard, A, Kley-Raymann, M, and Haas, D
- Abstract
Pseudomonas aeruginosa PAO was able to grow in the absence of exogenous terminal electron acceptors, provided that the medium contained 30 to 40 mM L-arginine and 0.4% yeast extract. Under strictly anaerobic conditions (O2 at less than 1 ppm), growth could be measured as an increase in protein and proceeded in a non-exponential way; arginine was largely converted to ornithine but not entirely consumed at the end of growth. In the GasPak anaerobic jar (Becton Dickinson and Co.), the wild-type strain PAO1 grew on arginine-yeast extract medium in 3 to 5 days; mutants could be isolated that were unable to grow under these conditions. All mutants (except one) were defective in at least one of the three enzymes of the arginine deiminase pathway (arcA, arcB, and arcC mutants) or in a novel function that might be involved in anaerobic arginine uptake (arcD mutants). The mutations arcA (arginine deiminase), arcB (catabolic ornithine carbamoyltransferase), arcC (carbamate kinase), and arcD were highly cotransducible and mapped in the 17-min chromosome region. Some mutations in the arc cluster led to low, noninducible levels of all three arginine deiminase pathway enzymes and thus may affect control elements required for induction of the postulated arc operon. Two fluorescent pseudomonads (P. putida and P. fluorescens) and P. mendocina, as well as one PAO mutant, possessed an inducible arginine deiminase pathway and yet were unable to grow fermentatively on arginine. The ability to use arginine-derived ATP for growth may provide P. aeruginosa with a selective advantage when oxygen and nitrate are scarce.
- Published
- 1984
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8. Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia
- Author
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Vander Wauven, C and Stalon, V
- Abstract
Pseudomonas cepacia NCTC 10743 utilizes arginine as the sole source of carbon and nitrogen for growth. Arginine is degraded to glutamate via succinyl derivatives. The catabolic sequence in this pathway is L-arginine----N2-succinylarginine----N2-succinylornithine--- -N2-succinylglutamate semialdehyde----N2-succinylglutamate----glutamate + succinate. The formation of the enzymes responsible for arginine degradation is regulated not only by induction but also by both carbon and nitrogen catabolite repression.
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- 1985
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9. Catabolism of Arginine, Citrulline and Ornithine by Pseudomonas and Related Bacteria
- Author
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STALON, V., primary, VANDER WAUVEN, C., additional, MOMIN, P., additional, and LEGRAIN, C., additional
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- 1987
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10. Production of a halotolerant endo-1,4-β-glucanase by a newly isolated Bacillus velezensis H1 on olive mill wastes without pretreatment: purification and characterization of the enzyme.
- Author
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Djelid H, Flahaut S, Vander Wauven C, Oudjama Y, Hiligsmann S, Cornu B, Cherfia R, Gares M, and Kacem Chaouche N
- Subjects
- Carboxymethylcellulose Sodium, Amino Acid Sequence, Hydrogen-Ion Concentration, Substrate Specificity, Cellulase metabolism, Olea, beta-Glucans
- Abstract
Facing the critical issue of high production costs for cellulase, numerous studies have focused on improving the efficiency of cellulase production by potential cellulolytic microorganisms using agricultural wastes as substrates, extremophilic cellulases, in particular, are crucial in the biorefinery process because they can maintain activity under harsh environmental conditions. This study aims to investigate the ability of a potential carboxymethylcellulose-hydrolyzing bacterial strain H1, isolated from an Algerian saline soil and identified as Bacillus velezensis, to use untreated olive mill wastes as a substrate for the production of an endo-1,4-β-glucanase. The enzyme was purified 44.9 fold using only two steps: ultrafiltration concentration and ion exchange chromatography, with final recovery of 80%. Its molecular mass was estimated to be 26 kDa by SDS-PAGE. Enzyme identification by LC-MS analysis showed 40% identity with an endo-1,3-1,4-β-glucanase of GH-16 family. The highest enzymatic activity was significantly measured on barley β-glucan (604.5 U/mL) followed by lichenan and carboxymethylcellulose as substrates, confirming that the studied enzyme is an endo-1,4-β-glucanase. Optimal enzymatic activity was at pH 6.0-6.5 and at 60-65 °C. It was fairly thermotolerant, retaining 76.9% of the activity at 70 °C, and halotolerant, retaining 70% of its activity in the presence of 4 M NaCl. The enzyme had a V
max of 625 U/min/mL and a high affinity with barley β-glucan resulting a Km of 0.69 mg/mL. It also showed a significant ability to release cello-oligosaccharides. Based on such data, the H1 endo-1,4-β-glucanase may have significant commercial values for industry, argo-waste treatment, and other biotechnological applications., (© 2022. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.)- Published
- 2022
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11. Highlighting the factors governing transglycosylation in the GH5_5 endo-1,4-β-glucanase RBcel1.
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Collet L, Vander Wauven C, Oudjama Y, Galleni M, and Dutoit R
- Subjects
- Bacterial Proteins chemistry, Cellobiose, Glycoside Hydrolases chemistry, Glycosylation, Hydrolysis, Substrate Specificity, Bacteria enzymology, Cellulase chemistry
- Abstract
Transglycosylating glycoside hydrolases (GHs) offer great potential for the enzymatic synthesis of oligosaccharides. Although knowledge is progressing, there is no unique strategy to improve the transglycosylation yield. Obtaining efficient enzymatic tools for glycan synthesis with GHs remains dependent on an improved understanding of the molecular factors governing the balance between hydrolysis and transglycosylation. This enzymatic and structural study of RBcel1, a transglycosylase from the GH5_5 subfamily isolated from an uncultured bacterium, aims to unravel such factors. The size of the acceptor and donor sugars was found to be critical since transglycosylation is efficient with oligosaccharides at least the size of cellotetraose as the donor and cellotriose as the acceptor. The reaction pH is important in driving the balance between hydrolysis and transglycosylation: hydrolysis is favored at pH values below 8, while transglycosylation becomes the major reaction at basic pH. Solving the structures of two RBcel1 variants, RBcel1_E135Q and RBcel1_Y201F, in complex with ligands has brought to light some of the molecular factors behind transglycosylation. The structure of RBcel1_E135Q in complex with cellotriose allowed a +3 subsite to be defined, in accordance with the requirement for cellotriose as a transglycosylation acceptor. The structure of RBcel1_Y201F has been obtained with several transglycosylation intermediates, providing crystallographic evidence of transglycosylation. The catalytic cleft is filled with (i) donors ranging from cellotriose to cellohexaose in the negative subsites and (ii) cellobiose and cellotriose in the positive subsites. Such a structure is particularly relevant since it is the first structure of a GH5 enzyme in complex with transglycosylation products that has been obtained with neither of the catalytic glutamate residues modified., (open access.)
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- 2022
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12. Glycoside hydrolase family 5: structural snapshots highlighting the involvement of two conserved residues in catalysis.
- Author
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Collet L, Vander Wauven C, Oudjama Y, Galleni M, and Dutoit R
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- Cellulase metabolism, Crystallography, X-Ray, Macromolecular Substances, Protein Binding, Cellulase chemistry, Oligosaccharides chemistry, Oligosaccharides metabolism
- Abstract
The ability of retaining glycoside hydrolases (GHs) to transglycosylate is inherent to the double-displacement mechanism. Studying reaction intermediates, such as the glycosyl-enzyme intermediate (GEI) and the Michaelis complex, could provide valuable information to better understand the molecular factors governing the catalytic mechanism. Here, the GEI structure of RBcel1, an endo-1,4-β-glucanase of the GH5 family endowed with transglycosylase activity, is reported. It is the first structure of a GH5 enzyme covalently bound to a natural oligosaccharide with the two catalytic glutamate residues present. The structure of the variant RBcel1_E135A in complex with cellotriose is also reported, allowing a description of the entire binding cleft of RBcel1. Taken together, the structures deliver different snapshots of the double-displacement mechanism. The structural analysis revealed a significant movement of the nucleophilic glutamate residue during the reaction. Enzymatic assays indicated that, as expected, the acid/base glutamate residue is crucial for the glycosylation step and partly contributes to deglycosylation. Moreover, a conserved tyrosine residue in the -1 subsite, Tyr201, plays a determinant role in both the glycosylation and deglycosylation steps, since the GEI was trapped in the RBcel1_Y201F variant. The approach used to obtain the GEI presented here could easily be transposed to other retaining GHs in clan GH-A.
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- 2021
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13. Crystal structure determination of Pseudomonas stutzeri A1501 endoglucanase Cel5A: the search for a molecular basis for glycosynthesis in GH5_5 enzymes.
- Author
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Dutoit R, Delsaute M, Collet L, Vander Wauven C, Van Elder D, Berlemont R, Richel A, Galleni M, and Bauvois C
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- Cellulose metabolism, Crystallization, Crystallography, X-Ray methods, Escherichia coli, Glycosylation, Substrate Specificity, Trioses metabolism, Bacterial Proteins chemistry, Cellulase chemistry, Cellulose chemistry, Pseudomonas stutzeri enzymology, Trioses chemistry
- Abstract
The discovery of new glycoside hydrolases that can be utilized in the chemoenzymatic synthesis of carbohydrates has emerged as a promising approach for various biotechnological processes. In this study, recombinant Ps_Cel5A from Pseudomonas stutzeri A1501, a novel member of the GH5_5 subfamily, was expressed, purified and crystallized. Preliminary experiments confirmed the ability of Ps_Cel5A to catalyze transglycosylation with cellotriose as a substrate. The crystal structure revealed several structural determinants in and around the positive subsites, providing a molecular basis for a better understanding of the mechanisms that promote and favour synthesis rather than hydrolysis. In the positive subsites, two nonconserved positively charged residues (Arg178 and Lys216) were found to interact with cellobiose. This adaptation has also been reported for transglycosylating β-mannanases of the GH5_7 subfamily.
- Published
- 2019
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14. Antimicrobial properties of Pseudomonas strains producing the antibiotic mupirocin.
- Author
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Matthijs S, Vander Wauven C, Cornu B, Ye L, Cornelis P, Thomas CM, and Ongena M
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- Anti-Bacterial Agents metabolism, Antibiosis, Cluster Analysis, DNA, Bacterial chemistry, DNA, Bacterial genetics, Genes, Bacterial, Lipopeptides metabolism, Lipopeptides pharmacology, Molecular Sequence Data, Mupirocin metabolism, Phylogeny, Pseudomonas genetics, Pseudomonas isolation & purification, Pseudomonas metabolism, Sequence Analysis, DNA, Sequence Homology, Staphylococcus aureus drug effects, Staphylococcus aureus growth & development, Anti-Bacterial Agents pharmacology, Mupirocin pharmacology, Pseudomonas physiology
- Abstract
Mupirocin is a polyketide antibiotic with broad antibacterial activity. It was isolated and characterized about 40 years ago from Pseudomonas fluorescens NCIMB 10586. To study the phylogenetic distribution of mupirocin producing strains in the genus Pseudomonas a large collection of Pseudomonas strains of worldwide origin, consisting of 117 Pseudomonas type strains and 461 strains isolated from different biological origins, was screened by PCR for the mmpD gene of the mupirocin gene cluster. Five mmpD(+) strains from different geographic and biological origin were identified. They all produced mupirocin and were strongly antagonistic against Staphylococcus aureus. Phylogenetic analysis showed that mupirocin production is limited to a single species. Inactivation of mupirocin production leads to complete loss of in vitro antagonism against S. aureus, except on certain iron-reduced media where the siderophore pyoverdine is responsible for the in vitro antagonism of a mupirocin-negative mutant. In addition to mupirocin some of the strains produced lipopeptides of the massetolide group. These lipopeptides do not play a role in the observed in vitro antagonism of the mupirocin producing strains against S. aureus., (Copyright © 2014 Institut Pasteur. Published by Elsevier Masson SAS. All rights reserved.)
- Published
- 2014
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15. The proteome of Salmonella Typhimurium grown under in vivo-mimicking conditions.
- Author
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Sonck KA, Kint G, Schoofs G, Vander Wauven C, Vanderleyden J, and De Keersmaecker SC
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- Electrophoresis, Gel, Two-Dimensional, Gene Expression Regulation, Bacterial drug effects, Osmolar Concentration, Oxygen pharmacology, Salmonella typhimurium drug effects, Proteome analysis, Salmonella typhimurium growth & development, Salmonella typhimurium metabolism
- Abstract
To successfully infect a host, it is a prerequisite for enteric pathogens such as Salmonella enterica serovar Typhimurium to adapt to their environment, in casu the gastrointestinal tract. The adoption of an appropriate lifestyle is triggered by environmental signals such as the low oxygen availability and high osmolarity prevalent in the gut. In order to gain more insight in the changes that are induced when S. Typhimurium is adapting to these particular conditions, we used 2-D DIGE technology to investigate the combined effect of low oxygen tension and high osmolarity on the proteome of S. Typhimurium SL1344 compared to standard laboratory conditions. As a validation of the 2-D DIGE technique, preferential protein labeling by the Cy-dyes was assessed and proved to be negligible. The differentially expressed proteins identified reflect very well the applied culture conditions. Furthermore, reported transcriptional changes and observed changes at the translational level show overlap. Among the metabolic processes that are upregulated under in vivo-mimicking conditions are anaerobic fumarate respiration and the utilization of 1,2-propanediol. We also provide evidence that S. Typhimurium expresses an arginine deiminase pathway for the catabolism of L-arginine. The increased activity of this pathway was biochemically validated. Finally, also proteins involved in quorum sensing and virulence are differentially expressed under in vivo-mimicking conditions. These conditions offer possibilities as a simplified model system for the host environment given the high overlap of identifications in our study and reported genuine in vivo studies, respectively.
- Published
- 2009
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16. Purification of ArcR, an oxidation-sensitive regulatory protein from Bacillus licheniformis.
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Wohlkönig A, Stalon V, and Vander Wauven C
- Subjects
- Amino Acid Sequence, Bacillus genetics, Bacillus metabolism, Bacterial Proteins genetics, Bacterial Proteins metabolism, Cloning, Molecular, Cysteine chemistry, DNA-Binding Proteins genetics, DNA-Binding Proteins metabolism, Disulfides chemistry, Molecular Sequence Data, Oxidation-Reduction, Recombinant Proteins genetics, Recombinant Proteins isolation & purification, Recombinant Proteins metabolism, Salts chemistry, Sequence Alignment, Bacillus chemistry, Bacterial Proteins isolation & purification, DNA-Binding Proteins isolation & purification
- Abstract
In Bacillus licheniformis, ArcR, a transcriptional activator of the Crp/Fnr family, is required for expression of the anaerobic pathway of arginine catabolism, the arginine deiminase pathway. The method described here allows the purification of milligram quantities of functional ArcR from a recombinant Escherichia coli strain. The solubility properties of ArcR were much exploited during the purification process. The protein appeared highly sensitive to oxidation. Oxidation-induced precipitation of the protein was attributed to the formation of intermolecular disulfide bridges. Alkylation of mutant proteins with single substitutions showed that both cysteine residues of the protein, C178 and C205, are involved in formation of the disulfide bridges. Substitution of both cysteines yielded a functional protein insensitive to oxidation and able to form a complex with its cognate target on the DNA.
- Published
- 2004
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17. Regulation of anaerobic arginine catabolism in Bacillus licheniformis by a protein of the Crp/Fnr family.
- Author
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Maghnouj A, Abu-Bakr AA, Baumberg S, Stalon V, and Vander Wauven C
- Subjects
- Amino Acid Sequence, Anaerobiosis, Bacillus metabolism, Bacterial Proteins chemistry, Base Sequence, Binding Sites, Carrier Proteins, Cyclic AMP Receptor Protein genetics, Cyclic AMP Receptor Protein metabolism, DNA, Bacterial chemistry, DNA, Bacterial metabolism, DNA-Binding Proteins chemistry, Genes, Bacterial, Iron-Sulfur Proteins genetics, Iron-Sulfur Proteins metabolism, Molecular Sequence Data, Multigene Family, Mutation, Sequence Analysis, DNA, Arginine metabolism, Bacillus genetics, Bacterial Proteins genetics, Bacterial Proteins metabolism, DNA-Binding Proteins genetics, DNA-Binding Proteins metabolism, Escherichia coli Proteins, Gene Expression Regulation, Bacterial
- Abstract
Arginine anaerobic catabolism occurs in Bacillus licheniformis through the arginine deiminase pathway, encoded by the gene cluster arcABDC. We report here the involvement of a new protein, ArcR, in the regulation of the pathway. ArcR is a protein of the Crp/Fnr family encoded by a gene located 109 bp downstream from arcC. It binds to a palindromic sequence, very similar to an Escherichia coli Crp binding site, located upstream from arcA. Residues in the C-terminal domain of Crp that form the DNA binding motif, in particular residues Arg-180 and Glu-181 that make specific bonds with DNA, are conserved in ArcR, suggesting that the complexes formed with DNA by Crp and ArcR are similar. Moreover, the pattern of DNase I hypersensitivity sites induced by the binding of ArcR suggests that ArcR bends the DNA in the same way as Crp. From the absence of anaerobic induction following inactivation of arcR and from the existence of a binding site upstream of the arcA transcription start point, it can be inferred that ArcR is an activator of the arginine deiminase pathway.
- Published
- 2000
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18. The arcABDC gene cluster, encoding the arginine deiminase pathway of Bacillus licheniformis, and its activation by the arginine repressor argR.
- Author
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Maghnouj A, de Sousa Cabral TF, Stalon V, and Vander Wauven C
- Subjects
- Amino Acid Sequence, Bacillus genetics, Bacterial Outer Membrane Proteins genetics, Base Sequence, Cloning, Molecular, DNA, Bacterial, Enzyme Induction, Escherichia coli Proteins, Gene Expression Regulation, Bacterial, Gene Expression Regulation, Enzymologic, Hydrolases metabolism, Molecular Sequence Data, Mutagenesis, Ornithine Carbamoyltransferase metabolism, Phosphotransferases (Carboxyl Group Acceptor) metabolism, Promoter Regions, Genetic, Repressor Proteins genetics, Amino Acid Transport Systems, Antiporters genetics, Bacillus enzymology, Bacterial Proteins genetics, Bacterial Proteins metabolism, Hydrolases genetics, Multigene Family, Ornithine Carbamoyltransferase genetics, Phosphotransferases (Carboxyl Group Acceptor) genetics, Repressor Proteins metabolism
- Abstract
The arginine deiminase pathway enables Bacillus licheniformis to grow anaerobically on arginine. Both the presence of arginine and anaerobiosis are needed to trigger induction of the pathway. In this study we have cloned and sequenced the arc genes encoding the pathway. They appear clustered in an operon-like structure in the order arcA (arginine deiminase), arcB (ornithine carbamoyltransferase), arcD (putative arginine-ornithine antiporter), arcC (carbamate kinase). It was found that B. licheniformis has an arginine repressor, ArgR, homologous to the B. subtilis arginine repressor AhrC. Mutants affected in argR were isolated. These mutants have lost both repression by arginine of the anabolic ornithine carbamoyltransferase and induction of the arginine deiminase pathway. Electrophoretic band shift experiments and DNase I footprinting revealed that in the presence of arginine, ArgR binds to a site upstream from the arc promoter. The binding site is centered 108 nucleotides upstream from the transcription start point and contains a single Arg box.
- Published
- 1998
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19. Purification and properties of a succinyltransferase from Pseudomonas aeruginosa specific for both arginine and ornithine.
- Author
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Tricot C, Vander Wauven C, Wattiez R, Falmagne P, and Stalon V
- Subjects
- Acyltransferases metabolism, Amino Acid Sequence, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Homoarginine metabolism, Hydrogen-Ion Concentration, Molecular Sequence Data, Mutation, Pseudomonas aeruginosa growth & development, Substrate Specificity, Acyltransferases isolation & purification, Arginine metabolism, Ornithine metabolism, Pseudomonas aeruginosa enzymology
- Abstract
The arginine and ornithine succinyltransferase from Pseudomonas aeruginosa, a bifunctional enzyme involved in the aerobic utilization of arginine and ornithine, has been purified to homogeneity. The apparent molecular mass of the native enzyme was 150 kDa by gel filtration and 140 kDa by polyacrylamide gel electrophoresis under non-denaturing conditions. After SDS/PAGE two subunits of 35 kDa and 37 kDa were evident, indicating that the enzyme is a heterotetramer. Microsequence analysis of the electroblotted protein bands gave two different but well-conserved N-terminal amino acid sequences. The L-arginine saturation curve followed Henri-Michaelis kinetics with an apparent Km value of 0.5 mM. The sigmoidal saturation curve for L-ornithine indicated allosteric behaviour. D-Arginine, a competitive inhibitor with respect to L-arginine, reduced L-ornithine cooperativity. In the presence of spermidine, the L-ornithine saturation curve became increasingly sigmoidal, the Hill coefficient shifting from 2.5 in the absence of the inhibitor, to 3.5 in the presence of 20 mM spermidine. The L-arginine analog, L-homoarginine, was also a substrate of the succinyltransferase, and the saturation of the enzyme by this substrate was also cooperative. All these data confirmed the allosteric nature of the enzyme. Moreover, a mutant growing faster on L-ornithine than the parent strain had a modified succinyltransferase with a reduced L-ornithine cooperativity. The fate of L-homoarginine was different depending on whether the succinyltransferase was induced or not; excreted succinylhomoarginine was found in cultures induced for the transferase activity whereas guanidinovalerate was excreted in non-induced cultures. The 'waste' of succinyl CoA, which could not be regenerated from the excreted succinylhomoarginine, explained the inhibition exerted by L-homoarginine on growth when ornithine or arginine was used as the growth medium.
- Published
- 1994
- Full Text
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20. Catabolism of arginine, citrulline and ornithine by Pseudomonas and related bacteria.
- Author
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Stalon V, Vander Wauven C, Momin P, and Legrain C
- Subjects
- Acyltransferases metabolism, Aeromonas enzymology, Ammonia-Lyases metabolism, Arginine analogs & derivatives, Klebsiella pneumoniae enzymology, Pseudomonas enzymology, Pseudomonas aeruginosa metabolism, Pseudomonas fluorescens metabolism, Succinates metabolism, Arginine metabolism, Citrulline metabolism, Ornithine metabolism, Pseudomonas metabolism
- Abstract
The distribution of the arginine succinyltransferase pathway was examined in representative strains of Pseudomonas and related bacteria able to use arginine as the sole carbon and nitrogen source for growth. The arginine succinyltransferase pathway was induced in arginine-grown cells. The accumulation of succinylornithine following in vivo inhibition of succinylornithine transaminase activity by aminooxyacetic acid showed that this pathway is responsible for the dissimilation of the carbon skeleton of arginine. Catabolism of citrulline as a carbon source was restricted to relatively few of the organisms tested. In P. putida, P. cepacia and P. indigofera, ornithine was the main product of citrulline degradation. In most strains which possessed the arginine succinyltransferase pathway, the first step of ornithine utilization as a carbon source was the conversion of ornithine into succinylornithine through an ornithine succinyltransferase. However P. cepacia and P. putida used ornithine by a pathway which proceeded via proline as an intermediate and involved an ornithine cyclase activity.
- Published
- 1987
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21. N2-succinylornithine in ornithine catabolism of Pseudomonas aeruginosa.
- Author
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Vander Wauven C, Jann A, Haas D, Leisinger T, and Stalon V
- Subjects
- Acyltransferases biosynthesis, Acyltransferases metabolism, Arginine metabolism, Enzyme Induction, Mutation, Pseudomonas aeruginosa enzymology, Pseudomonas aeruginosa genetics, Ornithine analogs & derivatives, Ornithine metabolism, Pseudomonas aeruginosa metabolism, Succinates metabolism
- Abstract
Most Pseudomonas aeruginosa PAO mutants which were unable to utilize L-arginine as the sole carbon and nitrogen source (aru mutants) under aerobic conditions were also affected in L-ornithine utilization. These aru mutants were impaired in one or several enzymes involved in the conversion of N2-succinylornithine to glutamate and succinate, indicating that the latter steps of the arginine succinyltransferase pathway can be used for ornithine catabolism. Addition of aminooxyacetate, an inhibitor of the N2-succinylornithine 5-aminotransferase, to resting cells of P. aeruginosa in ornithine medium led to the accumulation of N2-succinylornithine. In crude extracts of P. aeruginosa an ornithine succinyltransferase (L-ornithine:succinyl-CoA N2-succinyltransferase) activity could be detected. An aru mutant having reduced arginine succinyltransferase activity also had correspondingly low levels of ornithine succinyltransferase. Thus, in P. aeruginosa, these two activities might be due to the same enzyme, which initiates aerobic arginine and ornithine catabolism.
- Published
- 1988
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22. Control of enzyme synthesis in the oxalurate catabolic pathway of Streptococcus faecalis ATCC 11700: evidence for the existence of a third carbamate kinase.
- Author
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Vander Wauven C, Simon JP, Slos P, and Stalon V
- Subjects
- Agmatine metabolism, Agmatine pharmacology, Arginine metabolism, Arginine pharmacology, Enzyme Induction, Glucose metabolism, Glucose pharmacology, Kinetics, Ornithine Carbamoyltransferase metabolism, Oxamic Acid analogs & derivatives, Amino Acids metabolism, Carboxyl and Carbamoyl Transferases, Enterococcus faecalis enzymology, Oxamic Acid metabolism, Phosphotransferases metabolism, Phosphotransferases (Carboxyl Group Acceptor), Transferases metabolism
- Abstract
Streptococcus faecalis ATCC 11700 uses oxalurate as a sole energy source for growth. An oxamate carbamoyltransferase and a carbamate kinase, both induced by oxalurate, are involved in this process. The oxalurate-induced kinase is specific for the pathway. Its properties are different from those of the previously characterized agmatine and arginine-induced kinases. Glucose, but not arginine, nor agmatine, two other energy sources, represses the oxalurate pathway. In contrast, oxalurate was found to be at least as effective as glucose in repressing the arginine deiminase pathway in arginine grown cells, or the agmatine deiminase pathway during growth on agmatine.
- Published
- 1986
- Full Text
- View/download PDF
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