References of "Jacques, Philippe"
     in
Bookmark and Share    
See detailInfluence of lipopeptide production on oxygen transfer during fermentation of Bacillus subtilis
Hbid, Choukri; Jacques, Philippe; Razafindralambo, Hary ULg et al

Poster (1995, May 07)

Detailed reference viewed: 7 (1 ULg)
Full Text
Peer Reviewed
See detailLes mécanismes biochimiques développés par les Pseudomonas fluorescents dans la lutte biologique contre les maladies des plantes transmises par le sol
Jacques, Philippe; Delfosse, Philippe; Ongena, MARC ULg et al

in Cahiers Agricultures (1993), 2

Detailed reference viewed: 59 (4 ULg)
Full Text
Peer Reviewed
See detailIsopyoverdin Pp BTP1, a biogenetically interesting novel siderophore from Pseudomonas putida
Jacques, Philippe; Gwose, Inga; Seinsche, Dieter et al

in Natural Product Letters (1993), 3

From the cultures of Pseudomonas putida BTP 1 a siderophore could be isolated which contains the chromophore 2a rather than 1a typical for pyoverdins. Its structure was elucidated by MS, NHR and chemical ... [more ▼]

From the cultures of Pseudomonas putida BTP 1 a siderophore could be isolated which contains the chromophore 2a rather than 1a typical for pyoverdins. Its structure was elucidated by MS, NHR and chemical degradation. This new structural type is of great interest. The currently accepted biogenetic pathway leading to 1a starts from D-Tyr and L-Dab which condense to give the ferribactin chromophore 4. Subsequent ring closure via the -nitrogen of Dab leads to 1a while alternative ring closure via the -nitrogen would yield 2a. It is for the first time that this iso-chromophore has been detected in a Pseudomonas siderophore. Its discovery confirms the assumed intermediacy of ferribactine in the biogenesis of pyoverdins. [less ▲]

Detailed reference viewed: 22 (2 ULg)
Full Text
Peer Reviewed
See detailPurification Of Antifungal Lipopeptides By Reversed-Phase High-Performance Liquid-Chromatography
Razafindralambo, Hary ULg; Paquot, Michel ULg; Hbid, Choukri et al

in Journal of Chromatography. A (1993), 639(1), 81-85

A rapid procedure for the purification of antifungal lipopeptides from Bacillus subtilis, a potential agent for biocontrol of plant diseases, was tested. It consists of a solid-phase extraction on C18 gel ... [more ▼]

A rapid procedure for the purification of antifungal lipopeptides from Bacillus subtilis, a potential agent for biocontrol of plant diseases, was tested. It consists of a solid-phase extraction on C18 gel followed by reversed-phase chromatography using a biocompatible PepRPC HR 515 column with a pharmacia fast protein liquid chromatographic system. This is a very effective method for isolating and fractionating iturin A and surfactin, two lipopeptides of different nature, co-produced by Bacillus subtilis strain S499. The presence of homologous lipopeptides was easily detected. [less ▲]

Detailed reference viewed: 109 (37 ULg)
Full Text
Peer Reviewed
See detailThe Enterococcus Hirae R40 Penicillin-Binding Protein 5 and the Methicillin-Resistant Staphylococcus Aureus Penicillin-Binding Protein 2' Are Similar
el Kharroubi, Aboubaker; Jacques, Philippe; Piras, Graziella et al

in Biochemical Journal (1991), 280(Pt 2), 463-469

The penicillin-resistant Enterococcus hirae R40 has a typical profile of membrane-bound penicillin-binding proteins (PBPs) except that the 71 kDa PBP5 of low penicillin affinity represents about 50% of ... [more ▼]

The penicillin-resistant Enterococcus hirae R40 has a typical profile of membrane-bound penicillin-binding proteins (PBPs) except that the 71 kDa PBP5 of low penicillin affinity represents about 50% of all the PBPs present. Water-soluble tryptic-digest peptides were selectively produced from PBP5, their N-terminal regions were sequenced and synthetic oligonucleotides were used as primers to generate a 476 bp DNA fragment by polymerase chain reaction. On the basis of these data, the PBP5-encoding gene was cloned in Escherichia coli by using pBR322 as vector. The gene, included in a 7.1 kb insert, had the information for a 678-amino acid-residue protein. PBP5 shows similarity, in the primary structure, with the high-molecular-mass PBPs of class B. In particular, amino acid alignment of the enterococcal PBP5 and the methicillin-resistant staphylococcal PBP2' generates scores that are 30, for the N-terminal domains, and 53, for the C-terminal domains, standard deviations above that expected for a run of 20 randomized pairs of proteins having the same amino acid compositions as the two proteins under consideration. [less ▲]

Detailed reference viewed: 16 (4 ULg)
Full Text
Peer Reviewed
See detailMode of Membrane Insertion and Sequence of a 32-Amino Acid Peptide Stretch of the Penicillin-Binding Protein 4 of Enterococcus Hirae
Jacques, Philippe; el Kharroubi, Aboubaker; Van Beeumen, Jozef et al

in FEMS Microbiology Letters (1991), 66(2), 119-123

Analysis of water-soluble derivatives of the Enterococcus hirae 75-kDa membrane-bound penicillin-binding protein 4 (PBP4) has yielded the amino acid sequence of a 32-amino acid polypeptide stretch. This ... [more ▼]

Analysis of water-soluble derivatives of the Enterococcus hirae 75-kDa membrane-bound penicillin-binding protein 4 (PBP4) has yielded the amino acid sequence of a 32-amino acid polypeptide stretch. This peptide is similar to peptide segments known to occur in the N-terminal domain of high-Mr PBPs of class B. The E. hirae PBP4 probably belongs to the same class. It is anchored in the membrane at the N-terminus of the polypeptide chain. [less ▲]

Detailed reference viewed: 16 (0 ULg)
Full Text
Peer Reviewed
See detailBioconversion of a L-Carnitin Precursor in a One- or Two-Phase System
Bare, Ghislain; Jacques, Philippe; Hubert, Jean-Benoit et al

in Applied Biochemistry and Biotechnology (1991), 28-29(Spring), 445-56

The ability of the yeast Saccharomyces cerevisiae to bioconvert stereo-selectively octyl-4-chloroacetoacetate (OCA) into the corresponding chiral alcohol, precursor of L-carnitin, an important ... [more ▼]

The ability of the yeast Saccharomyces cerevisiae to bioconvert stereo-selectively octyl-4-chloroacetoacetate (OCA) into the corresponding chiral alcohol, precursor of L-carnitin, an important physiological agent, was investigated. In a monophasic system with free cells, more than 90% of OCA (0.018 M) bioconversion have been reached after 6 h (enantiomeric excess for the R form, eeR:97%). Immobilized cells in alginate beads were less efficient in conversion of OCA than free cells. In a two-phase system with free cells, the level of reduction of OCA (0.018 M) reached 85% after 48 h. With a medium containing a higher OCA concentration (0.270 M), 41% of this product were bioconverted after the same period. On the other hand, immobilized cells did not show any significant bioconversion of OCA in two-phase reactors. The limiting factor of these reactors in the regeneration of the cofactors involved in the OCA reduction. [less ▲]

Detailed reference viewed: 21 (2 ULg)
Full Text
Peer Reviewed
See detailActive-Site and Membrane Topology of the Dd-Peptidase/Penicillin-Binding Protein No. 6 of Enterococcus Hirae (Streptococcus Faecium) A.T.C.C. 9790
El Kharroubi, Aboubaker; Piras, Graziella; Jacques, Philippe et al

in Biochemical Journal (1989), 262(2), 457-462

The membrane-bound 43,000-Mr penicillin-binding protein no. 6 (PBP6) of Enterococcus hirae consists of a 30,000-Mr DD-peptidase/penicillin-binding domain and a approximately 130-residue C-terminal ... [more ▼]

The membrane-bound 43,000-Mr penicillin-binding protein no. 6 (PBP6) of Enterococcus hirae consists of a 30,000-Mr DD-peptidase/penicillin-binding domain and a approximately 130-residue C-terminal appendage. Removal of this appendage by trypsin proteolysis has no marked effect on the catalytic activity and penicillin-binding capacity of the PBP. Anchorage of the PBP in the membrane appears to be mediated by a short 15-20-residue stretch at the C-terminal end of the appendage. The sequence of the 50-residue N-terminal region of the PBP shows high degree of homology with the sequences of the corresponding regions of the PBPs5 of Escherichia coli and Bacillus subtilis. On this basis the active-site serine residue occurs at position 35 in the enterococcal PBP. [less ▲]

Detailed reference viewed: 8 (0 ULg)
Full Text
See detailCharacterization of the Trypsin-Solubilized Penicillin-Binding Proteins of Enterococcus hirae (Streptococcus faecium)
El Kharroubi, Aboubaker; Jacques, Philippe; Piras, Graziella et al

in Actor, Paul; Daneo-Moore, Lolita; Higgins, Michael L. (Eds.) et al Antibiotic Inhibition of Bacterial Cell Surface Assembly and Function (1988)

Detailed reference viewed: 13 (2 ULg)
Full Text
See detailPurification and Characterization of a β-lactam-Resistant Penicillin-Binding Protein from Enterococcus hirae (Streptococcus faecium)
Jacques, Philippe; El Kharroubi, Aboubaker; Joris, Bernard ULg et al

in Actor, Paul; Daneo-Moore, Lolita; Higgins, Michael L. (Eds.) et al Antibiotic Inhibition of Bacterial Cell Surface Assembly and Function (1988)

Detailed reference viewed: 15 (3 ULg)
Full Text
Peer Reviewed
See detailPrimary structure of the Streptomyces R61 extracellular DD-peptidase. 2. Amino acid sequence data
Joris, Bernard ULg; Jacques, Philippe; Frère, Jean-Marie ULg et al

in European Journal of Biochemistry (1987), 162(3), 519-524

In order to confirm the Streptomyces codon usage, the Streptomyces R61 DD-peptidase was fragmented by cyanogen bromide cleavage of the carboxymethylated protein, trypsin digestion of the carboxymethylated ... [more ▼]

In order to confirm the Streptomyces codon usage, the Streptomyces R61 DD-peptidase was fragmented by cyanogen bromide cleavage of the carboxymethylated protein, trypsin digestion of the carboxymethylated protein and trypsin digestion of the protein treated with beta-iodopenicillinate and endoxo-delta 4-tetrahydrophthalic acid. The isolated peptides, which altogether represented more than 50% of the polypeptide chain, were sequenced. The data thus obtained were in excellent agreement with the primary structure of the protein as deduced from the nucleotide sequence of the cloned gene. Though a weak acylating agent, beta-iodopenicillanate reacted selectively with the active site of the DD-peptidase and formed an adduct which mas much more stable than that formed with benzylpenicillin, thus facilitating the isolation and characterization of the active-site peptide. [less ▲]

Detailed reference viewed: 4 (0 ULg)