Reference : Penicillin-sensitive DD-carboxypeptidases from Streptomyces strains R39 and K11
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/87288
Penicillin-sensitive DD-carboxypeptidases from Streptomyces strains R39 and K11
English
Leyh-Bouille, Mélina [Université de Liège - ULg > Institut de Botanique > Service de Microbiologie]
Nakel, Marlies [Ludwig-Maximilians-Universität München - LMU > Botanisches Institut]
Frère, Jean-Marie mailto [Université de Liège - ULg > Institut de Botanique > Service de Microbiologie]
Johnson, Kenneth [Université de Liège - ULg > Institut de Botanique > Service de Microbiologie]
Ghuysen, Jean-Marie [Université de Liège - ULg > Institut de Chimie]
Nieto, Manuel [National Institute for Medical Research - London]
Perkins, Harold R. [National Institute for Medical Research - London]
28-Mar-1972
Biochemistry
American Chemical Society
11
7
1290-1298
Yes (verified by ORBi)
International
0006-2960
1520-4995
Washington
DC
[en] ammonium sulfate ; carboxypeptidases antagonists & inhibitors isolation & purification ; chromatography gel ; electrophoresis ; filtration ; hydrogen-ion concentration ; hydrolysis ; kinetics ; osmolar concentration ; penicillin g ; penicillinase ; species specificity ; streptomyces enzymology ; structure-activity relationship
[en] The two penicillin-sensitive DD-carboxypeptidases from Streptomyces R39 and K11 are anionic at pH 8. They specifically recognize a C-terminal L-R3-D-alanyl-D sequence with a long side chain at the R3 position. The two enzymes differ from each other with respect to: (1) the effects of ionic strength on activity, (2) the influence exerted on activity by the presence of a free amino group at the end of the L-R3 side chain, (3) the K3 and Vmax values. Enzyme K11 has Km values which are high for both good and poor substrates. The enzyme efficiency reflects itself in Vmax values which are high for good substrates and low for poor substrates. Enzyme R39 has Km values which are low for good substrates. The enzyme efficiency toward various substrates reflects itself in the Km and, to a lesser extent, in the Vmax values, (4) the effects of penicillin. Kinetically, inhibition of enzyme K11 by penicillin is competitive. On the contrary, inhibition of enzyme R39 by penicillin is noncompetitive and increasing penicillin concentrations cause disproportionate decreases in the catalytic rate. Noncompetitiveness cannot be attributed to an irreversible inactivation of the enzyme by penicillin.
Researchers ; Professionals
http://hdl.handle.net/2268/87288

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