Zobrazeno 1 - 10
of 328
pro vyhledávání: '"Frere, JM"'
Deacetoxycephalosporin C synthase is an iron(II) 2-oxoglutaratedependent oxygenase that catalyzes the oxidative ring-expansion of penicillin N to deacetoxycephalosporin C. The wild-type enzyme is only able to efficiently utilize 2-oxoglutarate and 2-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::3eb88c2d306417aa943ebc49127aa406
https://ora.ox.ac.uk/objects/uuid:f8904bd0-8b4b-46c2-b65a-75e8eecaa764
https://ora.ox.ac.uk/objects/uuid:f8904bd0-8b4b-46c2-b65a-75e8eecaa764
Autor:
ADAM, M, DAMBLON, C, JAMIN, M, ZORZI, W, DUSART, [No Value], GALLENI, M, ELKHARROUBI, A, PIRAS, G, SPRATT, BG, Keck, W, COYETTE, J, GHUYSEN, JM, NGUYENDISTECHE, M, FRERE, JM
Publikováno v:
Biochemical Journal, 279(2), 601-604. PORTLAND PRESS LTD
The high-molecular-mass penicillin-binding proteins (HMM-PBPs), present in the cytoplasmic membranes of all eubacteria, are involved in important physiological events such as cell elongation, septation or shape determination. Up to now it has, howeve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca8a02a326be4ac25dbc7b9915f4a55f
https://hdl.handle.net/11370/93485313-8265-4c9f-a1b9-250c0f42afce
https://hdl.handle.net/11370/93485313-8265-4c9f-a1b9-250c0f42afce
Autor:
Moali, C., Anne, C., Lamotte-Brasseur, J., Groslambert, S., Devreese, B., Vanbeeumen, J., Galleni, M., Frere, Jm
The role of the mobile loop comprising residues 60-66 in metallo-beta-lactamases has been studied by site-directed mutagenesis, determination of kinetic parameters for six substrates and two inhibitors, pre-steady-state characterization of the intera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______166::e564eb955bd8fb3b577011fcb7f8057f
https://hal.archives-ouvertes.fr/hal-00314476
https://hal.archives-ouvertes.fr/hal-00314476
Autor:
Bebrone, C., Moali, C., Mahy, F., Rival, S., Docquier, Jd, Rossolini, Gm, Fastrez, J., Pratt, Rf, Frere, Jm, Galleni, M.
CENTA, a chromogenic cephalosporin, is readily hydrolyzed by beta-lactamases of all classes except for the Aeromonas hydrophila metalloenzyme. Although it cannot practically be used for the detection of beta-lactamase-producing strains on agar plates
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______166::43ae06d890cd9e9137f5f2f66cdb4b2d
https://hal.archives-ouvertes.fr/hal-00313147
https://hal.archives-ouvertes.fr/hal-00313147
Publikováno v:
Biochemical Journal, 292, 555-562. PORTLAND PRESS LTD
Three class-D beta-lactamases (OXA2, OXA1 and PSE2) were produced and purified to protein homogeneity. 6beta-lodopenicillanate inactivated the OXA2 enzyme without detectable turnover. Labelling of the same beta-lactamase with 6beta-iodo[H-3]penicilla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::d779c50bfccbc236fa41b45c188046fc
https://research.rug.nl/en/publications/d6fa4be4-f485-4fa4-a142-9fdffea3c149
https://research.rug.nl/en/publications/d6fa4be4-f485-4fa4-a142-9fdffea3c149