References of "Ghuysen, Jean-Marie"
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See detailStructure of the cell wall of Micrococcus lysodeikticus. I. Study of the structure of the glycan
Leyh-Bouille, Mélina; Ghuysen, Jean-Marie ULg; Tipper, Donald J. et al

in Biochemistry (1966), 5(10), 3079-3090

The glycan portion of the cell wall of Micrococcus lysodeikticus, or at least the greatest part of it, consists of linear chains of alternating N-acetyl-glucosamine and N-acetylmuramic acid residues, both ... [more ▼]

The glycan portion of the cell wall of Micrococcus lysodeikticus, or at least the greatest part of it, consists of linear chains of alternating N-acetyl-glucosamine and N-acetylmuramic acid residues, both in the pyranose ring form. Both glycosidic links are 1,4. The links from N-acetylglucosamine to N-acetyl-muramic acid and probably the links from N-acetyl-muramic acid to N-acetylglucosamine are in the β configuration. At least 40% of the N-acetylmuramic residues are not substituted by peptide. This structure is based on the quantitative isolation of the disaccharides N-acetylglucosaminyl-β-1,4-N-acetylmuramic acid and N-acetylmuramyl-(β?)-l,4-N-acetylglucosamine, of the trisaccharides N-acetylglucosaminyl-β-l,4-N-acetyl-muramyl-(β?)-1,4-N-acetylglucosamine and N-acetyl-muramyl-(β?)-1,4-N-acetylglucosaminyl-β-1,4-N-acetyl-muramic acid, and of the tetrasaccharide N-acetylglucos-aminyl-β-1,4-N-acetylmuramyl-(β?)-l,4-N-acetylglucos-aminyl-β-l,4-N-acetylmuramic acid. An octasaccharide the structure of which has not been fully elucidated has also been isolated. [less ▲]

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See detailStructural variations in bacterial cell wall peptidoglycans studied with Streptomyces F1 endo-N-acetylmuramidase
Munoz, Emilio; Ghuysen, Jean-Marie ULg; Leyh-Bouille, Mélina et al

in Biochemistry (1966), 5(10), 30913098

An improved procedure for the purification of the Streptomyces FI [beta]-l,4 endo-N-acetylmuramidase is described. FI enzymes digests cell walls from bacteria of the most important grampositive genera ... [more ▼]

An improved procedure for the purification of the Streptomyces FI [beta]-l,4 endo-N-acetylmuramidase is described. FI enzymes digests cell walls from bacteria of the most important grampositive genera. Its mechanism of action upon cell walls of Staphylococcus aureus, Micrococcus roseus, and Micrococcus lysodeikticus has been studied. To all appearances, the affinity of the F1 enzyme for the glycosidic linkages of N-acetylmuramic add in the polysaccharide chains is greatly enhanced by the peptide substitution of these residues. From an integration of the properties of the FI enzyme digests of various cell walls, it appears that tight network peptidoglycans, typified by a high degree of cross-linkings of the polysaccharide chains through peptide unites, as they occur in cell wals of S. aureus and M. roseus, are not encountered in many cell walls from gram-positive bacteria. [less ▲]

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See detailPeptide cross-links in bacterial cell wall peptidoglycans studied with specific endopeptidases from Streptomyces albus G
Petit, Jean-François; Munoz, Emilio; Ghuysen, Jean-Marie ULg

in Biochemistry (1966), 5(8), 2764-2776

Evidence is given for the existence of at least four types of peptide cross-linkages in lysine-containing peptidoglycans of cell walls from Gram-positive bacteria. Three kinds of such cross-linkages, by ... [more ▼]

Evidence is given for the existence of at least four types of peptide cross-linkages in lysine-containing peptidoglycans of cell walls from Gram-positive bacteria. Three kinds of such cross-linkages, by which the є-amino group of the lysine residue of one peptide subunit is joined to the carboxyl group of the terminal D-alanine of a second, have been demonstrated, namely: bridging by tri-L-alanine (Micrococcus roseus Thr(-)), by tri-L-alanine-L-threonine (M. roseus R 27), and by pentaglycine (Staphylococcus aureus Copenhagen) residues. The lytic Streptomyces SA endopeptidase hydrolyzes D-alanylglycyl linkages in S. aureus and D-alanyl-L-alanine linkages in M. roseus, i.e., at the amino terminus of the peptide bridges and at the carboxyl terminus of the peptide subunits. The lytic Streptomyces MR endopeptidase hydrolyzes L-alanyl-L-threonine linkages within the peptide bridges in M. roseus R 27 and, with a much smaller rate, L-alanyl-L-alanine linkages within the peptide bridges in M. roseus Thr(-)). A fourth kind of cross-linkage, in which no additional amino acid is involved, can also occur in the form of a direct bonding between the C-terminal alanine residue of one peptide subunit and the є-amino group of the lysine residue of a second (Micrococcus lysodeikticus). This latter alanyl-є-lysine bond is sensitive to a third lytic Streptomyces enzyme, the ML endopeptidase. A structure for the peptide moiety of the peptidoglycan of M. roseus is proposed and compared to the peptidoglycan structure in S. aureus. The present studies lend support to recent proposals dealing with the mechanism of action of penicillin. [less ▲]

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See detailAction des enzymes bactériolytiques, autres que le lysozyme, sur le peptidoglycane des parois cellulaires bactériennes
Ghuysen, Jean-Marie ULg; Petit, Jean-François; Munoz, Emilio et al

in Exposés Annuels de Biochimie Médicale (1966)

La structure réticulaire proposée pour le peptidoglycane des parois cellulaires bactériennes permet de comprendre les propriétés apparemment contradictoires de résistance mécanique et d'extensibilité qui ... [more ▼]

La structure réticulaire proposée pour le peptidoglycane des parois cellulaires bactériennes permet de comprendre les propriétés apparemment contradictoires de résistance mécanique et d'extensibilité qui caractérisent cette structure anatomique, unique dans le monde vivant, destinée à protéger contre l'éclatement osmotique des êtres unicellulaires dont le temps de génération est parfois de quelques dizaines de minutes. Ces études de structure basées sur des dégradations enzymatiques contrôlées, jointes aux recherches sur la biosynthèse du peptidoglycane, ont également permis d'interpréter le mécanisme d'action d'un certain nombre d'antibiotiques. La pénicilline, en particulier, a pour effet d'induire chez S. aureus la formation d'un peptidoglycane fragile dont beaucoup de chaînes polyglycine ont leurs extrémités NH² libres [31, 37]. Chez ces cellules intoxiquées, la réaction de transpeptidisation qui assure normalement la fermeture des ponts, est inhibée. Il est frappant de constater que l'inhibition de la biosynthèse de la liaison D-alanylglycine par la pénicilline provoque la lyse d'une culture de staphylocoques en voie de multiplication et que l'ouverture de cette même liaison par la SA. endopeptidase a pour effet de dissoudre les parois staphylococciques isolées. [less ▲]

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See detailEnzymes that degrade bacterial cell walls
Ghuysen, Jean-Marie ULg; Tipper, Donald J.; Strominger, Jack L.

in Methods in Enzymology (1966), 8

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See detailStructure of the Cell Wall of Staphylococcus Aureus, Strain Copenhagen. IV. The Teichoic Acid-Glycopeptide Complex
Ghuysen, Jean-Marie ULg; Tipper, Donald J.; Strominger, Jack L.

in Biochemistry (1965), 4

A teichoic acid-glycopeptide complex has been obtained from the cell wall of Staphylococcus aureus after enzymatic lysis of the walls with either of two acetylmuramidases. This complex was fractionated ... [more ▼]

A teichoic acid-glycopeptide complex has been obtained from the cell wall of Staphylococcus aureus after enzymatic lysis of the walls with either of two acetylmuramidases. This complex was fractionated into materials containing a glycopeptide component of varying size linked to teichoic acid. Most of the glycopeptide was removed by hydrolysis of the complexes with an acetylmuramyl-L-alanine amidase. After this treatment, a native teichoic acid with a weight-average molecular weight of about 20,000 and a number-average molecular weight of 12,000-16,000 was obtained. These data suggest that the largest molecules of the teichoic acid contain forty to fifty repeating units and that some smaller molecules also exist in the preparation. Chemical and physical analyses of native teichoic acid and various teichoic acid-glycopeptide complexes are presented. [less ▲]

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See detailStructure of the cell wall of Staphylococcus aureus, strain Copenhagen. III. Further studies of the disaccharides
Tipper, Donald J.; Ghuysen, Jean-Marie ULg; Strominger, Jack L.

in Biochemistry (1965), 4(3), 468-473

Two disaccharides have previously been obtained in high yield from the cell wall of S. aureus by the use of hydrolytic enzymes. Disaccharide 1 is N-acetylglucosaminyl-N-acetylmuramic acid and disaccharide ... [more ▼]

Two disaccharides have previously been obtained in high yield from the cell wall of S. aureus by the use of hydrolytic enzymes. Disaccharide 1 is N-acetylglucosaminyl-N-acetylmuramic acid and disaccharide 2 is N-acetylglucosaminyl-N,Ogr;-diacetylmuramic acid. After hydrolysis of disaccharide 2 with β-acetylglucosaminidase, N,O-diacetylmuramic acid was prepd. Data obtained from periodate oxidn. of these compds. coupled with their susceptibility to β-acetylglucosaminidase indicate that both disaccharides are β-1,4-linked and that the O-acetyl group of disaccharide 2 is on the 6-position of N-acetylmuramic acid. The high reducing power and pos. Morgan-Elson reaction of the disaccharides are due to their unusual susceptibility to hydrolysis at alk. pH. These and other anomalous properties of the compds. are discussed. [on SciFinder(R)] [less ▲]

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See detailStaphylolytic Enzyme from Chalaropsis: Mechanism of Action
Tipper, Donald J.; Strominger, Jack L.; Ghuysen, Jean-Marie ULg

in Science (1964), 146

The staphylolytic enzyme recently isolated from cultures of a Chalaropsis species by Hash is shown to be an acetylmurainidase that cleaves all the glycosidic linkages of N-acetylmuramic acid and N,O ... [more ▼]

The staphylolytic enzyme recently isolated from cultures of a Chalaropsis species by Hash is shown to be an acetylmurainidase that cleaves all the glycosidic linkages of N-acetylmuramic acid and N,O-diacetylmuramic acid in the cell wall of Staphylococcus aureus strain Copenhagen. It is similar in specificity to the "32 enzyme" from Streptomyces albus but it differs from egg-white lysozyme whose activity is inhibited by the presence of O-acetyl groups. [less ▲]

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See detailAlkaline degradation of the phosphomucopolysaccharide from cell walls of Bacillus megaterium KM
Ghuysen, Jean-Marie ULg

in Biochimica et Biophysica Acta (1964), 83(1), 132-134

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See detailStructure of the Cell Wall of Staphylococcus Aureus, Strain Copenhagen. II. Separation and Structure of Disaccharides
Ghuysen, Jean-Marie ULg; Strominger, Jack L.

in Biochemistry (1963), 2

The disaccharides, β-1,6-N-acetylglucosamimyl-N-acetylmuramic acid and β-1,6-N-acetyl-glucosaminyl-N,4-O-diacetylmuramic acid, have been identified as products of hydrolysis of the cell wall of S. aureus ... [more ▼]

The disaccharides, β-1,6-N-acetylglucosamimyl-N-acetylmuramic acid and β-1,6-N-acetyl-glucosaminyl-N,4-O-diacetylmuramic acid, have been identified as products of hydrolysis of the cell wall of S. aureus by an acetylmuramidase and an amidase from Streptomyces albus G. N-acetylmuramic acid and N,4-O-diacetylmuramic acid were formed from these compounds after hydrolysis with a β-acetylglucosarninidase. The data obtained do not exclude the presence of a small percentage of disaccharides with other linkages, however. Several bases for the resistance of cell walls of S. aureus to hydrolysis by egg white lysozyme have been discussed. [less ▲]

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See detailStructure of the Cell Wall of Staphylococcus Aureus, Strain Copenhagen. I. Preparation of Fragments by Enzymatic Hydrolysis
Ghuysen, Jean-Marie ULg; Strominger, Jack L.

in Biochemistry (1963), 2(5), 1110-1119

The cell wall of S. aureus strain Copenhagen, has been solubilized through the action of the 32 enzyme" isolated from Streptomyces albus G. This solubilization was the consequence of hydrolysis of ... [more ▼]

The cell wall of S. aureus strain Copenhagen, has been solubilized through the action of the 32 enzyme" isolated from Streptomyces albus G. This solubilization was the consequence of hydrolysis of acetylamino sugar linkages in the cell wall [less ▲]

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See detailOn the Linkage between Teichoic Acid and the Glycopeptide in the Cell Wall of Staphylococcus Aureus
Strominger, Jack L.; Ghuysen, Jean-Marie ULg

in Biochemical & Biophysical Research Communications (1963), 12(5), 418-424

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See detailStructure des parois de Bacillus megaterium KM II. étude des complexes mucopeptidique et phosphomucopolysaccharidique
Ghuysen, Jean-Marie ULg; Leyh-Bouille, Mélina; Dierickx, L.

in Biochimica et Biophysica Acta (1962), 63

Bacillus megaterium KM cell walls are composed of two distinct heteropolymers. The first, referred as to X-teichoic acid, presents a molecular weight of about 11000. It consists of about 10 subunits ... [more ▼]

Bacillus megaterium KM cell walls are composed of two distinct heteropolymers. The first, referred as to X-teichoic acid, presents a molecular weight of about 11000. It consists of about 10 subunits containing P, glucose and GlcNHAc in the molar ratio 1/2/1.3 as well as a polyol compound. It does not play any role in maintaining the rigidity of the wall. The second can be visualized as a three-dimensional network of structural subunits consisting of four mucopeptide residues with an average composition GlcNHAc1- (N-acetylmuramic acid)1-Ala2.20-Glu1- ([alpha],[epsilon]-diaminopimelic acid)1. They also contain glucose. This mucopeptide is the basal structure of the wall. The two heteropolymers are present in equimolar proportions. They are covalently bound through glucosido-muraminyl bridges branched on some of the alanine residues of the basal mucopeptide thanks to amidic linkages. [less ▲]

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See detailPurification de la [beta]-(1-4)-N-acétylhexosaminidase sécrétée par Streptomyces albus G et active sur les parois de Micrococus lysodeikticus
Dierickx, L.; Ghuysen, Jean-Marie ULg

in Biochimica et Biophysica Acta (1962), 58

The N-acetylhexosaminidase (referred as Str) secreted by Streptomyces albus G. has been purified by zone electrophoresis. It is slightly less basic than egg-white lysozyme. Its isoelectric point is close ... [more ▼]

The N-acetylhexosaminidase (referred as Str) secreted by Streptomyces albus G. has been purified by zone electrophoresis. It is slightly less basic than egg-white lysozyme. Its isoelectric point is close to pH 10.3. It has no action on the [alpha]- and [beta]-phenylglycosides of N-acetylglucosamine and on the disaccharides [beta]-(1-4)-di-N-acetylglucosamine (di-N-acetylchitobiose) and [beta]-(1-6)-N-acetylglucosaminyl-N-acetylmuramic acid but it splits the tetrasaccharide [beta]-(1-4)-tetra-N-acetylglucosamine(tetra-N-acetylchitotetraose) in di-N-acetylchitobiose. Contrary to lysozyme, it does not split the tetrasaccharide O-[beta]-N-acetylglucosaminyl-(1-6)-O-[beta]-N-acetylmuraminyl-(1-4)-O-[beta]-N-acetylglucosaminyl-(1-6)-[beta]-N-acetylmuramic acid in disaccharide by hydrolyzing the [beta](1-4) linkage. In those conditions the disaccharide liberated, as well as the tetrasaccharide, from Microccus lysodeikticus cell walls after incubation with the N-acetylhexosaminidase Str, can not be put down to a further digestion of some tetrasaccharidic fragments. A chitobiase only active on the [beta]-phenyl-glycoside of N-acetylglucosamine and on the di-N-acetylchitobiose is also present in contentrated culture filtrates. It is a protein acid at pH 6.6. [less ▲]

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See detailStructure des parois de Bacillus megaterium KM I. Isolement de l'amidase et d'un enzyme nouveau sécrétés par Streptomyces albus G et actifs sur les parois de Bacillus megaterium KM et de Micrococcus lysodeikticus
Ghuysen, Jean-Marie ULg; Leyh-Bouille, Melina; Dierickx, L.

in Biochimica et Biophysica Acta (1962), 63(2), 286-296

The Streptomyces albus G enzymic complex of the F2B preparation has been fractionated by zone electrophoresis in sucrose gradient. Five enzymes have been shown to be present and three of them have been ... [more ▼]

The Streptomyces albus G enzymic complex of the F2B preparation has been fractionated by zone electrophoresis in sucrose gradient. Five enzymes have been shown to be present and three of them have been fully separated. Three distinct enzymes make the casein no further precipitable by the trichloroacetic acid. They are likely not to have any action on Bacillus megaterium KM and on Micrococcus lysodeikticus cell walls. A fourth enzyme is the amidase previously studied which splits the muraminyl-alanine linkages present in the bacterial walls. The amidase does not clarify by itself the wall suspensions so far examined but enhances the lytic activity of a fifth enzyme also present in the F2B preparation. As lysozyme and Streptomyces N-acetylhexosaminidase, this fifth enzyme seems to act at the level of the polysaccharide residues of the walls basal mucopeptide but, contrary to those enzymes, its hydrolyzing action does not induce the liberation of free oligosaccharides from Micrococcus lysodeikticus walls. This enzyme will be referred to as Enzyme “32”. [less ▲]

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See detailComplexe acide téichoique-mucopeptide des parois cellulaires de Bacillus megaterium KM
Ghuysen, Jean-Marie ULg

in Biochimica et Biophysica Acta (1961), 50(3), 413-429

Walls of a batch of Bacillus megalerium KM contain a polyol phosphate compound which, in contrast with BADDILEY'S teichoic acids, is not extracted by cold tri-chloroacetic acid. It has been isolated by ... [more ▼]

Walls of a batch of Bacillus megalerium KM contain a polyol phosphate compound which, in contrast with BADDILEY'S teichoic acids, is not extracted by cold tri-chloroacetic acid. It has been isolated by paper electrorheophoresis from the non-dialysable fraction obtained after incubation of the walls by lysozyme. Owing to the chemical analysis, it is associated with mucopeptide residues and the whole complex represents 40%, dry weight, of the walls. The degradation of this complex by two Streptomyces enzymes enables the identi-fication of three fragments: a teichoic fragment of polyol phosphate, glucose and N-acetylglucosamine; a mucopeptide fragment of amino acids and N-acetylmuramic acid; a disaccharide fragment 6-O-fl-N-acetylglucosaminyl-N-acetyl-muramic acid. It is believed that the latter represents an unit of a poly-N-acetylhexosamine back-bone of the basal mucopeptide of the wall. The teichoic fragment is liberated from the whole colnplex under the action of both Streptomyces enzymic preparations FI or F2B. It can also be obtained by in-cubating directly the walls with each of those preparations. The disaccharide fragment is liberated under the action of the F2B amidase. Approx. 6 %, dry weight, of the walls consist of glucose (probably a polyglucose) non associated with the teichoic acid-mucopeptide complex. N-acetylmuramic acid and various oligosaccharides consisting of N-acetyl- glucosamine alone or of both N-acetylglucosamine and N-acetylmuramic acid, give, on paper, a pink coloration with the diphenylamine-trichloroacetic reagent which allows them to be distinguished from N-acetylglucosamine. [less ▲]

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See detailPrécisions sur la structure des complexes disaccharide-peptide libérés des parois de Micrococcus lysodeikticus sous l'action des β (I → 4) N-acetylhexosaminidases
Ghuysen, Jean-Marie ULg

in Biochimica et Biophysica Acta (1961), 47(3), 561-568

Two types of disaccaride-peptide complexes have been studied. In a first type of complex, the fragment 6-O-[beta]-N-acetylglucosaminyl-N-acetyl-muraminyl is joined to a peptide moiety consisting of 2 ... [more ▼]

Two types of disaccaride-peptide complexes have been studied. In a first type of complex, the fragment 6-O-[beta]-N-acetylglucosaminyl-N-acetyl-muraminyl is joined to a peptide moiety consisting of 2 alanines, 1 glycine, 1 glutamic acid and 1 lysine, by an amide bond between the COOH of N-acetylmuramic acid and the NH2 of one of the alanine residues of the peptide. The reaction with 1-fluoro-2,4 dinitrobenzene shows that the [epsilon]-NH2 group of lysine is free. The electroheophoretic properties suggest that the [gamma]-COOH group of glutamic acid and an unspecified [alpha]-COOH group are free too. The second type of complex is a dimer of the former, joined by a peptide linkage between an [epsilon]-NH2 group of lysine and, very probably, an [alpha]-COOH group. THe F2B amidase splits the amidic acetylmuraminyl-alanine linkage. Consequently, the disaccharide is liberated and a new free [alpha]-NH2 group of alanine appears in the peptide moiety. [less ▲]

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