The interaction of penicillinase with penicillins III. Comparison of exopenicillinase preparations of various origins

N. Citri, N. Garber, A. Kalkstein
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引用次数: 15

Abstract

  • 1.

    1. The interaction of various penicillinases (penicillin amidohydrolase, EC 3.5.2.6) with methicillin and oxacillin has been studied.

  • 2.

    2. The Km values have been compared and found to reflect the phylogenetic and serological relationship of the penicillinases.

  • 3.

    3. Methicillin and oxacillin accelerate the inactivation of penicillinases by heat and by urea, and expose groups sensitive to iodine and to p-chloromercuribenzoate (p-hydroxymercuribenzoate).

  • 4.

    4. The response of penicillinases from different sources to various concentrations of these analogs has been compared.

  • 5.

    5. The patterns of response are characteristic of the source of penicillinase, and essentially independent of the structure of the analog.

  • 6.

    6. A comparison of these patterns brings out subtle differences in the tertiary structure of the active sites of closely related enzymes.

  • 7.

    7. The sensitivity of such analysis is illustrated by the difference in reponse patterns of enzymically and serologically indistinguishable induced and constitutive enzyme preparations.

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青霉酶与青霉素的相互作用III。不同产地外霉素酶制剂的比较
1.1. 研究了各种青霉素酶(青霉素酰胺水解酶,EC 3.5.2.6)与甲氧西林和恶西林的相互作用。比较了Km值,发现它反映了青霉菌病的系统发育和血清学关系。甲氧西林和苯氧西林可通过加热和尿素加速青霉素酶的失活,并使对碘和对氯汞苯甲酸盐(对羟基汞苯甲酸盐)敏感的基团暴露。比较了不同来源的青霉酶对不同浓度的这些类似物的反应。反应模式是青霉酶来源的特征,基本上与类似物的结构无关。这些模式的比较显示出密切相关的酶的活性位点的三级结构的细微差别。这种分析的敏感性是由酶和血清学上难以区分的诱导酶和组成酶制剂的反应模式的差异所说明的。
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