title: On the origin of bacterial resistance to penicillin: comparison of a beta-lactamase and a penicillin target.
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.
authors.forename: J A
authors.initials: JA
authors.lastname: Kelly
authors.forename: O
authors.initials: O
authors.lastname: Dideberg
authors.forename: P
authors.initials: P
authors.lastname: Charlier
authors.forename: J P
authors.initials: JP
authors.lastname: Wery
authors.forename: M
authors.initials: M
authors.lastname: Libert
authors.forename: P C
authors.initials: PC
authors.lastname: Moews
authors.forename: J R
authors.initials: JR
authors.lastname: Knox
authors.forename: C
authors.initials: C
authors.lastname: Duez
authors.forename: C
authors.initials: C
authors.lastname: Fraipont
authors.forename: B
authors.initials: B
authors.lastname: Joris
mesh_terms: D000595:Amino Acid Sequence; D001409:Bacillus cereus / Q000201:enzymology; D001665:Binding Sites; D002268:Carboxypeptidases / Q000235:genetics / Q000378:metabolism*; D008970:Molecular Weight; D010403:Penicillin Resistance; D011487:Protein Conformation; D046929:Serine-Type D-Ala-D-Ala Carboxypeptidase; D013302:Streptomyces / Q000201:enzymology; D014961:X-Ray Diffraction; D001618:beta-Lactamases / Q000235:genetics / Q000378:metabolism*
chemical_list: D002268:Carboxypeptidases; D046929:Serine-Type D-Ala-D-Ala Carboxypeptidase; D001618:beta-Lactamases