Výsledky vyhledávání - "J M, Ghuysen"

Point mutations of two arginine residues in the Streptomyces R61 dd-peptidase

Autor: C Bourguignon-Bellefroid, J M Ghuysen, Jean-Marie Frère, J. Van Beeumen, Bernard Joris

Publikováno v: Biochemical Journal. 283:123-128

Incubation of the exocellular DD-carboxypeptidase/transpeptidase of Streptomyces R61 with phenylglyoxal resulted in a time-dependent decrease in the enzyme activity. This inactivation was demonstrated to be due to modification of the Arg-99 side chai

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c6750d84bbe0fbbbbfc75afe74e7409
https://doi.org/10.1042/bj2830123

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Primary and predicted secondary structures of the Actinomadura R39 extracellular dd-peptidase, a penicillin-binding protein (PBP) related to the Escherichia coli PBP4

Autor: B. Granier, Jean-Marie Frère, Colette Duez, J. Van Beeumen, Jean Dusart, Sophie Lepage, J M Ghuysen, Otto Dideberg, Serge Englebert

Publikováno v: Biochemical Journal. 282:781-788

As derived from gene cloning and sequencing, the 489-amino-acid DD-peptidase/penicillin-binding protein (PBP) produced by Actinomadura R39 has a primary structure very similar to that of the Escherichia coli PBP4 [Mottl, Terpstra & Keck (1991) FEMS M

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f25b6b2e013d57ce52cddbf49a13ed3b
https://doi.org/10.1042/bj2820781

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Amino acid sequence of the penicillin-binding protein/dd-peptidase of Streptomyces K15. Predicted secondary structures of the low Mr penicillin-binding proteins of class A

Autor: J M Ghuysen, P Palomeque-Messia, Mélina Leyh-Bouille, J. Van Beeumen, Serge Englebert, Colette Duez, Otto Dideberg, Martine Nguyen-Distèche, Simone Houba

Publikováno v: Biochemical Journal. 279:223-230

The low-Mr penicillin-binding protein (PBP)/DD-transpeptidase of Streptomyces K15 is synthesized in the form of a 291-amino acid-residue precursor possessing a cleavable 29-amino acid-residue signal peptide. Sequence-similarity searches and hydrophob

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f48502b410661beca693a2d77595bd54
https://doi.org/10.1042/bj2790223

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Penicillin‐Binding Proteins

Autor: J. M. Ghuysen

Publikováno v: Encyclopedia of Molecular Biology

Maggy ADAM,* Christian DAMBLON,* Marc JAMIN,* Willy ZORZI,* Vincent DUSART,* Moreno GALLENI,* Aboubaker EL KHARROUBI,* Graziella PIRAS,* Brian G. SPRATT,t Wolfgang KECK,t Jacques COYETTE,* Jean-Marie GHUYSEN,* Martine NGUYEN-DISTECHE* and Jean-Marie

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::780c1387a9c8be5a298e56f3f4389bcd
https://doi.org/10.1002/047120918x.emb1092

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[Bacterial resistance to antibiotics, an exemplary model of directed molecular evolution]

Autor: J M, Ghuysen

Publikováno v: Revue medicale de Liege. 53(9)

The simplest conceivable event that can occur at the gene level can result in the development of efficacious resistance tot antibiotics. The bacterial world behaves as an enormous organism whose cells can exchange their genes very easily. Accordingly

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::291c2cf0b14325c2f163187c282a246c
https://pubmed.ncbi.nlm.nih.gov/9834675

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Characterization 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

Autor: Bernard Joris, J M Ghuysen, Colette Duez, Marie-Jeanne Vacheron, L Denoroy, Georges Michel, Micheline Guinand, M L Hourdou, Serge Englebert, G. Weber

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 c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb56ee4055da63436686b48b901c47ec
https://europepmc.org/articles/PMC1134247/

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Secretion by overexpression and purification of the water-soluble Streptomyces K15 DD-transpeptidase/penicillin-binding protein

Autor: J M Ghuysen, I K Dacey, Mélina Leyh-Bouille, J. Van Beeumen, Martine Nguyen-Distèche, V Quittre, Jean Dusart, P Palomeque-Messia, C J L Gershater

Though synthesized with a cleavable signal peptide and devoid of membrane anchors, the 262-amino-acid-residue Streptomyces K15 DD-transpeptidase/penicillin-binding protein is membrane-bound. Overexpression in Streptomyces lividans resulted in the exp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c694114ba7f77662cf644157f53f0a9
https://europepmc.org/articles/PMC1132083/

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Modular design of the Enterococcus hirae muramidase-2 and Streptococcus faecalis autolysin

Autor: B, Joris, S, Englebert, C P, Chu, R, Kariyama, L, Daneo-Moore, G D, Shockman, J M, Ghuysen

Publikováno v: FEMS microbiology letters. 70(3)

The mature forms of the extracellular muramidase-2 of Enterococcus hirae and Streptococcus faecalis autolysin have very similar primary structures. Each consists of an active-site-containing N-terminal domain fused to a multiple-repeat C-terminal dom

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::190d652802f01fe4f883403431d11ca7
https://pubmed.ncbi.nlm.nih.gov/1352512

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