The relationship between the structures of four beta-lactamases obtained from Bacillus cereus.
Bacillus cereus has proved to be one of the most interesting microorganisms in the study of beta-lactamases. It secrets these enzymes very efficiently and, frequently, in multiple forms. Three different forms are produced by strain 569/H; mutant 5/B of the same microorganism is constitutive for the secretion of beta-lactamases I and II. The present study, based on secondary structure prediction by two independent methods, states the relationship among the structures of beta-lactamases I, II and III produced by B. cereus 569/H and beta-lactamase I from the strain 5/B of this microorganism. A strong similarity is also established for the enzyme type III of B. cereus and the enzyme type I produced by B. licheniformis which could have an evolutionary explanation. A structural analysis of the leader peptide regions of these enzymes by the method of Mohana and Argos is also reported.
Cid
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Depto. de Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Chile.
Carrillo
O
O
Bunster
M
M
Martínez
J
J
Vargas
V
V
D001409:Bacillus cereus / Q000201:enzymology*; D015394:Molecular Structure; D011487:Protein Conformation; D001618:beta-Lactamases / Q000737:chemistry / Q000378:metabolism*
D001618:beta-Lactamases