Article (Scientific journals)
Crystallographic data for the DD-carboxypeptidase-endopeptidase of low penicillin sensitivity excreted by Streptomyces albus g
Dideberg, Otto; Frère, Jean-Marie; Ghuysen, Jean-Marie
1979In Journal of Molecular Biology, 129 (4), p. 677-679
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Keywords :
alanine; crystallization; dipeptides; endopeptidases/isolation & purification; kinetics; streptomyces/*enzymology; x-ray diffraction
Abstract :
[en] The DD-carboxypeptidase-endopeptidase of low penicillin sensitivity that is excreted by Streptomyces albus G has been crystallized from a polyethylene glycol (Mr 6000 to 7500) solution at pH 8.0. X-ray examination of the prismatic crystals shows that the space group is P21 with unit cell dimensions a = 51.1 Å, B = 49.7 Å, C = 38.7 Å, β = 100.6 ° and one molecule in the asymmetric unit. A crystal suspension made in 50 mM -Tris • HCl buffer (pH 8.0) supplemented with 5 mM-MgCl2 and 16% (w/v) polyethylene glycol exhibits enzyme activity on the substrate Ac2-L-Lys-D-Ala-D-Ala.
Disciplines :
Microbiology
Biochemistry, biophysics & molecular biology
Author, co-author :
Dideberg, Otto;  Université de Liège - ULiège > Insitut de Chimie > Laboratoire de Cristallographie
Frère, Jean-Marie  ;  Université de Liège - ULiège > Faculté de Médecine, Institut de Botanique > Service de Microbiologie
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Faculté de Médecine, Institut de Botanique > Service de Microbiologie
Language :
English
Title :
Crystallographic data for the DD-carboxypeptidase-endopeptidase of low penicillin sensitivity excreted by Streptomyces albus g
Publication date :
25 April 1979
Journal title :
Journal of Molecular Biology
ISSN :
0022-2836
eISSN :
1089-8638
Publisher :
Academic Press, London, United Kingdom
Volume :
129
Issue :
4
Pages :
677-679
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
NIH - National Institutes of Health
F.R.S.-FNRS - Fonds de la Recherche Scientifique
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