On the origin of bacterial resistance to penicillin: comparison of a beta-lactamase and a penicillin target.
Science
; 231(4744): 1429-31, 1986 Mar 21.
Article
em En
| MEDLINE
| ID: mdl-3082007
ABSTRACT
Structural data are now available for comparing a penicillin target enzyme, the D-alanyl-D-alanine-peptidase from Streptomyces R61, with a penicillin-hydrolyzing enzyme, the beta-lactamase from Bacillus licheniformis 749/C. Although the two enzymes have distinct catalytic properties and lack relatedness in their overall amino acid sequences except near the active-site serine, the significant similarity found by x-ray crystallography in the spatial arrangement of the elements of secondary structure provides strong support for earlier hypotheses that beta-lactamases arose from penicillin-sensitive D-alanyl-D-alanine-peptidases involved in bacterial wall peptidoglycan metabolism.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Beta-Lactamases
/
Resistência às Penicilinas
/
Carboxipeptidases
/
D-Ala-D-Ala Carboxipeptidase Tipo Serina
Idioma:
En
Revista:
Science
Ano de publicação:
1986
Tipo de documento:
Article