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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 ▲]

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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 ▲]

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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)

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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)

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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 ▲]

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