SUMMARY: Two β-lactamases, A and B, have been shown to be present in a strain of Yersinia enterocolitica (W222). β-Lactamase A hydrolyses a variety of penicillins and cephalosporins. This enzyme is sensitive to thiol reagents, is only partially inhibited 0·1 mm-cloxacillin and has a molecular weight of approximately 20000. β-Lactamase B shows strong cephalosporinase activity but does not hydrolyse some of the penicillins. It is more resistant than β-lactamase A to thiol reagents, is completely inhibited 0·1 mm-cloxacillin and has a molecular weight of about 34000. With cephaloridine as a substrate, which is readily hydrolysed both enzymes, about 85% of the total activity of a cell extract is due to β-lactamase A and 15% to B. Addition of 6-aminopenicillanic acid to the culture during growth results in a 2- to 4-fold selective increase in the amount of β-lactamase B. Two β-lactamases similar to enzymes A and B have been found in five other strains of Y. enterocolitica. In contrast, only one β-lactamase, similar to enzyme B, has been detected in a different strain of Y. enterocolitica (H66), which is abnormal in that it is sensitive to ampicillin. Addition of 6-aminopenicillanic acid to cultures of this strain results in an 8- to 10-fold increase in β-lactamase production.
CornelisG.,
WautersG.,
BruynogheG.1973a; Resistances transferables chez des souches sauvages de Yersinia enterocolitica. Annales de Microbiologie (Institut Pasteur) 124A:299–309
CornelisG.,
WautersG.,
VanderhaegheH.1973b; Presence de β-lactamase chez Yersinia entero-colitica. Annales de Microbiologie {Institut Pasteur) 124B:139–152
CromptonB.,
JagoM.,
CrawfordK.,
NewtonG. G. F.,
AbrahamE. P.1962; Behaviour of some derivatives of 7-aminocephalosporanic acid and 6-aminopenicilIanic acid as substrates, inhibitors and inducers of penicillinases. Biochemical Journal 83:52–63
EykynS.,
JenkinsC.,
KingA.,
PhillipsI.1973; Antibacterial activity of cefamandole, a new cephalosporin antibiotic, compared with that of cephaloridine, cephalothin, and cephalexin. Antimicrobial Agents and Chemotherapy 3:657–661
HouJ. P.,
PooleJ. W.1972; Measurement of β-lactamase activity and rate of inactivation of penicillins by a pH-stat alkalimetric titration method. Journal of Pharmaceutical Sciences 61:1594–1598
JackG. W.,
RichmondM. H.1970; A comparative study of eight distinct β-lactamases synthesized by Gram-negative bacteria. Journal of General Microbiology 61:43–61
McphailM.,
FurthA.1973; Purification and properties of an inducible β-lactamase from Pseudomonas aeruginosan.c.t.c. 8203. Biochemical Society Transactions 1:1260–1263
MishankinB. N.,
RyzhkoI. V.,
GrigorianE. G.1973; Study of penicillinase activity of Pasteurella pseudotuberculosis and Pasteurella X. Antibiotiki 18:621–624
NewsomS. W. B.,
SykesR. B.,
RichmondM. H.1970; Detection of a β-lactamase markedly active against carbenicillin in a strain of Pseudomonas aeruginosa. Journal of Bacteriology 101:1079–1080
NiléhnB.1969; Studies on Yersinia enterocolitica: with special reference to bacterial diagnosis and occurrence in human acute enteric disease. Acta pathologica et microbiologica scandinavica 206:1–48
O’CallaghanC. H.,
MorrisA.,
KirbyS. M.,
ShinglerA. H.1972; Novel method for detection of β-lactamases by using a chromogenic cephalosporin substrate. Antimicrobial Agents and Chemotherapy 1:283–288
RichmondM. H.,
JackG. W.,
SykesR. B.1971; The β-lactamases of Gram-negative bacteria including pseudomonads. Annals of the New York Academy of Sciences 182:243–257
SabathL. D.,
JagoM.,
AbrahamE. P.1965; Cephalosporinase and pencillinase activities of a β-lactamase from Pseudomonas pyocyanae. Biochemical Journal 96:739–752
WautersG.,
Le MinorL.,
ChalonA. M.,
LassenJ.1972; Supplement au schema antigenique de Yersinia enterocolitica. Annales de l’Institut Pasteur 122:951–956
WinbladS.1968; Studies on O antigen factors of Y. enterocolitica. In International Symposium on Pseudotuberculosis1968 Symposia Series in Immunobiological Standardization 9 pp. 337–342 Basle: Karger;
YaginumaS.,
SawaiT.,
OnoH.,
YamagishiS.,
MitsuhashiS.1973; Biochemical properties of a cephalosporin β-lactamase from Pseudomonas aeruginosa. Japanese Journal of Microbiology 17:141–149