References of "Vacheron, Marie-Jeanne"
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See detailOverproduction and properties of the mannuronate alginate lyase AlxMB
Malissard, Martine; Chavagnat, Frédéric; Duez, Colette ULg et al

in FEMS Microbiology Letters (1995), 126(2), 105-111

In previous studies (Malissard et al., FEMS Microbiol. Lett. (1993) 110, 101-106), the alginate lyase AlxM of the marine bacterium ATCC 433367 was produced in Escherichia coli TC4/pAL-A3 with a yield of ... [more ▼]

In previous studies (Malissard et al., FEMS Microbiol. Lett. (1993) 110, 101-106), the alginate lyase AlxM of the marine bacterium ATCC 433367 was produced in Escherichia coli TC4/pAL-A3 with a yield of 50 mu g per litre of culture. The polypeptide chain was cleaved between two cysteine residues, C169 and C183, themselves linked by a disulphide bridge. AlxM has now been overproduced in E. coli BL21(DE3)/pAL-Sur/pLysS. Under conditions in which formation of inclusion bodies can be avoided, the enzyme is synthesized as a catalytically active, water-soluble, unnicked polypeptide with a yield of 32 mg per litre of culture. It has been purified to protein homogeneity using a one-step procedure. The nicked ALxM(A) and unnicked ALxM(B) alginate lyases have identical alginate-degrading activities at high salt concentrations. [less ▲]

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See detailCharacterization of the Sporulation-Related Gamma-D-Glutamyl-(L)Meso-Diaminopimelic-Acid-Hydrolysing Peptidase I of Bacillus Sphaericus NCTC 9602 as a Member of the Metallo(Zinc) Carboxypeptidase A Family. Modular Design of the Protein
Hourdou, Marie-Laure; Guinand, Micheline; Vacheron, Marie-Jeanne et al

in Biochemical Journal (1993), 292(Pt 2), 563-570

The sporulation-related gamma-D-glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 has been analysed by proton-induced X-ray emission. It contains 1 equivalent ... [more ▼]

The sporulation-related gamma-D-glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 has been analysed by proton-induced X-ray emission. It contains 1 equivalent Zn2+ per mol of protein. As derived from gene cloning and sequencing, the B. sphaericus Zn peptidase I is a two-module protein. A 100-amino-acid-residue N-terminal domain consisting of two tandem segments of similar sequences, is fused to a 296-amino-acid-residue C-terminal catalytic domain. The catalytic domain belongs to the Zn carboxypeptidase A family, the closest match being observed with the Streptomyces griseus carboxypeptidase [Narahashi (1990) J. Biochem. 107, 879-886] and with the family prototype, bovine carboxypeptidase A. The catalytic domain of the B. sphaericus peptidase I possesses, distributed along the amino-acid sequence, peptide segments, a triad His162-Glu165-His307 and a dyad Tyr347-Glu366 that are equivalent to secondary structures, the zinc-binding triad His69-Glu72-His196 and the catalytic dyad Tyr248-Glu270 of bovine carboxypeptidase A respectively. The N-terminal repeats of the B. sphaericus peptidase I have similarity with the C-terminal repeats of the Enterococcus hirae muramidase 2, the Streptococcus (now Enterococcus) faecalis autolysin and the Bacillus phi PZA and phi 29 lysozymes, to which a role in the recognition of a particular moiety of the bacterial cell envelope has been tentatively assigned. Detergents enhance considerably the specific activity of the B. sphaericus peptidase I. [less ▲]

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See detailSequence of a gene encoding a (poly ManA) alginate lyase active on Pseudomonas aeruginosa alginate
Malissard, Martine; Duez, Colette ULg; Guinand, Micheline et al

in FEMS Microbiology Letters (1993), 110(1), 101-106

The recombinant plasmid pAL-A3 bears a (poly ManA) alginate lyase-encoding gene that originates from the marine bacterium ATCC 433367 (Brown et al., Appl. Environ. Microbiol. (1991) 57, 1870-1872). The ... [more ▼]

The recombinant plasmid pAL-A3 bears a (poly ManA) alginate lyase-encoding gene that originates from the marine bacterium ATCC 433367 (Brown et al., Appl. Environ. Microbiol. (1991) 57, 1870-1872). The alginate lyase produced by Escherichia coli TC4 harbouring pAL-A3 was purified to protein homogeneity and the corresponding gene sequenced, giving access to the first known primary structure of an alginate lyase. The 265-amino acid residue alginate lyase showed lytic activity on a Pseudomonas aeruginosa alginate isolated from a cystic fibrosis patient. Unexpectedly, the alginate lyase thus characterized differed from that isolated from the culture medium of the bacterium ATCC 433367 (Romeo and Preston, Biochemistry (1986) 25, 8385-8391). [less ▲]

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See detailCloning and nucleotide sequence of the gene encoding the γ-D-glutamyl-L-diamino acid endopeptidase II of Bacillus sphaericus
Hourdou, Marie-Laure; Duez, Colette ULg; Joris, Bernard ULg et al

in FEMS Microbiology Letters (1992), 91(2), 165-170

The gene encoding the Bacillus sphaericus gamma-D-glutamyl-L-diamino acid endopeptidase II, a cytoplasmic enzyme involved in cell sporulation [1], contains the information for a 271-amino acid protein ... [more ▼]

The gene encoding the Bacillus sphaericus gamma-D-glutamyl-L-diamino acid endopeptidase II, a cytoplasmic enzyme involved in cell sporulation [1], contains the information for a 271-amino acid protein devoid of a signal peptide. The endopeptidase lacks sequence relatedness with other proteins of known primary structure except that its C-terminal region has significant similarity with the C-terminal region of the 54-kDa P54 protein of Enterococcus faecium, of unknown function [2]. [less ▲]

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See detailStructural investigations on cell walls of Nocardia sp. The wall lipid and peptidoglycan moieties of Nocardia kirovani
Vacheron, Marie-Jeanne; Guinand, Micheline; Michel, Georges et al

in European Journal of Biochemistry (1972), 29(1), 156-166

The walls of Nocardia kirovani are composed of three main constituents: the peptidoglycan matrix, a polysaccharide polymer and a variety of free and bound lipids. The free lipids represent 17.5% (dry ... [more ▼]

The walls of Nocardia kirovani are composed of three main constituents: the peptidoglycan matrix, a polysaccharide polymer and a variety of free and bound lipids. The free lipids represent 17.5% (dry weight) of the walls and consist for the major part of C16–18 fatty acids and nocardic acids, and for the minor part, of nocardones, triglycerides and carotenoid pigments. The nocardic acids were identified as tri- and tetra-unsaturated, α-branched, β-hydroxylated compounds C58H110O3—C66H124O3 the nocardones as tri-and tetra-unsaturated ketones C57H106O—C63H1180O, and the main carotenoid pigment as phlei-xantophylle palmitate. Esters of glycerol with C14, C16, C18 fatty acids and, for some of them, with odd numbered poly-unsaturated acids containing 35 to 45 carbon atoms, were also identified. Bound lipids represent about 20% (dry weight) of the walls and consist mainly of nocardic acids probably ester-linked to an arabinogalactan polymer. The peptidoglycan (about 40% dry weight) is composed of β-1,4-N-acetylglucosaminyl-N-glycolylmuramic acid disaccharide units that are substituted by diamidated L-Ala-D-αGln-(L)-A2pm-(D)-NH2 tripeptides and diamidated l-Ala-d-αGln-(L)-A2pm-(D)-NH2-(L)-d-Ala tetrapeptides, where A2pm is meso-diaminopimelic acid. Crosslinking between some of the peptide units is mediated through D-Ala-(D)-A2pm linkages (peptidoglycan of chemotype I). [less ▲]

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