On the origin of bacterial resistance to penicillin: comparison of a beta-lactamase and a penicillin target.
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.
Kelly
J A
JA
Dideberg
O
O
Charlier
P
P
Wery
J P
JP
Libert
M
M
Moews
P C
PC
Knox
J R
JR
Duez
C
C
Fraipont
C
C
Joris
B
B
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*
D002268:Carboxypeptidases; D046929:Serine-Type D-Ala-D-Ala Carboxypeptidase; D001618:beta-Lactamases