B类和C类β-内酰胺酶的pH依赖性
The pH-dependence of class B and class C beta-lactamases.
作者信息
Bicknell R, Knott-Hunziker V, Waley S G
出版信息
Biochem J. 1983 Jul 1;213(1):61-6. doi: 10.1042/bj2130061.
Abstract
The classification by structure allots beta-lactamases to (at present) three classes, A, B and C. The pH-dependence of the kinetic parameters for class B and class C have been determined. They differ from each other and from class A beta-lactamases. The class B enzyme was beta-lactamase II from Bacillus cereus 569/H/9. The plots of kcat against pH for the hydrolysis of benzylpenicillin by Zn(II)-requiring beta-lactamase II and Co(II)-requiring beta-lactamase II were not symmetrical, but those of kcat/Km were. A similar feature was observed for the hydrolysis of both benzylpenicillin and cephalosporin C by a class C beta-lactamase from Pseudomonas aeruginosa. The results have been interpreted by a scheme in which two ionic forms of an intermediate can give product, but do so at differing rates.
摘要
根据结构分类，（目前）β-内酰胺酶可分为A、B和C三类。已确定了B类和C类动力学参数的pH依赖性。它们彼此不同，也与A类β-内酰胺酶不同。B类酶是蜡样芽孢杆菌569/H/9的β-内酰胺酶II。锌（II）依赖性β-内酰胺酶II和钴（II）依赖性β-内酰胺酶II水解苄青霉素时，kcat对pH的曲线不对称，但kcat/Km的曲线对称。铜绿假单胞菌的C类β-内酰胺酶水解苄青霉素和头孢菌素C时也观察到类似特征。结果通过一种机制进行了解释，即中间体的两种离子形式都能产生产物，但速率不同。
相似文献
1
The pH-dependence of class B and class C beta-lactamases.B类和C类β-内酰胺酶的pH依赖性
Biochem J. 1983 Jul 1;213(1):61-6. doi: 10.1042/bj2130061.
2
The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent beta-lactamase.蜡样芽孢杆菌锌依赖性β-内酰胺酶的催化机制及抑制作用
Biochem J. 1998 May 1;331 ( Pt 3)(Pt 3):703-11. doi: 10.1042/bj3310703.
3
Changes in the coordination geometry of the active-site metal during catalysis of benzylpenicillin hydrolysis by Bacillus cereus beta-lactamase II.蜡样芽孢杆菌β-内酰胺酶II催化苄青霉素水解过程中活性位点金属配位几何结构的变化。
Biochemistry. 1986 Nov 4;25(22):7208-15. doi: 10.1021/bi00370a066.
4
Cryoenzymology of Bacillus cereus beta-lactamase II.蜡样芽孢杆菌β-内酰胺酶II的低温酶学
Biochemistry. 1985 Nov 19;24(24):6876-87. doi: 10.1021/bi00345a021.
5
A thiono-beta-lactam substrate for the beta-lactamase II of Bacillus cereus. Evidence for direct interaction between the essential metal ion and substrate.蜡样芽孢杆菌β-内酰胺酶II的硫代-β-内酰胺底物。必需金属离子与底物之间直接相互作用的证据。
Biochem J. 1989 Mar 15;258(3):765-8. doi: 10.1042/bj2580765.
6
Enzyme deactivation due to metal-ion dissociation during turnover of the cobalt-beta-lactamase catalyzed hydrolysis of beta-lactams.在钴β-内酰胺酶催化β-内酰胺水解的周转过程中，由于金属离子解离导致酶失活。
Biochemistry. 2006 Sep 12;45(36):11012-20. doi: 10.1021/bi0610146.
7
Kinetic parameters from progress curves of competing substrates. Application to beta-lactamases.来自竞争性底物进程曲线的动力学参数。在β-内酰胺酶中的应用。
Biochem J. 1983 May 1;211(2):511-3. doi: 10.1042/bj2110511.
8
The acyl-enzyme mechanism of beta-lactamase action. The evidence for class C Beta-lactamases.β-内酰胺酶作用的酰基-酶机制。C类β-内酰胺酶的证据。
Biochem J. 1982 Nov 1;207(2):315-22. doi: 10.1042/bj2070315.
9
The mutation Lys234His yields a class A beta-lactamase with a novel pH-dependence.赖氨酸234突变为组氨酸产生了一种具有新型pH依赖性的A类β-内酰胺酶。
Biochem J. 1991 Sep 15;278 ( Pt 3)(Pt 3):673-8. doi: 10.1042/bj2780673.
10
Mechanism of acyl transfer by the class A serine beta-lactamase of Streptomyces albus G.白色链霉菌G的A类丝氨酸β-内酰胺酶的酰基转移机制
Biochem J. 1991 Oct 1;279 ( Pt 1)(Pt 1):213-21. doi: 10.1042/bj2790213.
引用本文的文献
1
Substrate-promoted formation of a catalytically competent binuclear center and regulation of reactivity in a glycerophosphodiesterase from Enterobacter aerogenes.产气肠杆菌甘油磷酸二酯酶中底物促进催化活性双核中心的形成及反应性调控
J Am Chem Soc. 2008 Oct 29;130(43):14129-38. doi: 10.1021/ja803346w. Epub 2008 Oct 3.
2
The activity of the dinuclear cobalt-beta-lactamase from Bacillus cereus in catalysing the hydrolysis of beta-lactams.蜡样芽孢杆菌双核β-内酰胺酶催化β-内酰胺水解的活性。
Biochem J. 2007 Jan 1;401(1):197-203. doi: 10.1042/BJ20061002.
3
Site-selective binding of Zn(II) to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia.锌（II）与嗜麦芽窄食单胞菌金属β-内酰胺酶L1的位点选择性结合。
J Biol Inorg Chem. 2006 Apr;11(3):351-8. doi: 10.1007/s00775-006-0083-z. Epub 2006 Feb 18.
4
The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent beta-lactamase.蜡样芽孢杆菌锌依赖性β-内酰胺酶的催化机制及抑制作用
Biochem J. 1998 May 1;331 ( Pt 3)(Pt 3):703-11. doi: 10.1042/bj3310703.
5
The production and molecular properties of the zinc beta-lactamase of Pseudomonas maltophilia IID 1275.嗜麦芽窄食单胞菌IID 1275锌β-内酰胺酶的产生及分子特性
Biochem J. 1985 Aug 1;229(3):791-7. doi: 10.1042/bj2290791.
6
Properties of a class C beta-lactamase from Serratia marcescens.粘质沙雷氏菌C类β-内酰胺酶的特性
Biochem J. 1986 Nov 1;239(3):581-6. doi: 10.1042/bj2390581.
7
A survey of the kinetic parameters of class C beta-lactamases. Penicillins.C类β-内酰胺酶动力学参数的研究。青霉素类。
Biochem J. 1988 Oct 1;255(1):119-22. doi: 10.1042/bj2550119.
8
The beta-lactamase of Enterobacter cloacae P99. Chemical properties, N-terminal sequence and interaction with 6 beta-halogenopenicillanates.阴沟肠杆菌P99的β-内酰胺酶。化学性质、N端序列以及与6种β-卤代青霉素酸的相互作用。
Biochem J. 1985 May 15;228(1):241-8. doi: 10.1042/bj2280241.
9
Inhibition of class C beta-lactamases by (1'R,6R)-6-(1'-hydroxy)benzylpenicillanic acid SS-dioxide.(1'R,6R)-6-(1'-羟基)苄基青霉烷酸SS-二氧化物对C类β-内酰胺酶的抑制作用
Biochem J. 1985 Jan 15;225(2):435-9. doi: 10.1042/bj2250435.
10
A thiono-beta-lactam substrate for the beta-lactamase II of Bacillus cereus. Evidence for direct interaction between the essential metal ion and substrate.蜡样芽孢杆菌β-内酰胺酶II的硫代-β-内酰胺底物。必需金属离子与底物之间直接相互作用的证据。
Biochem J. 1989 Mar 15;258(3):765-8. doi: 10.1042/bj2580765.
本文引用的文献
1
Use of the pH-stat in kinetic studies of reactions whose products are capable of functioning as buffers.pH稳态在产物可作为缓冲剂的反应动力学研究中的应用。
Biochemistry. 1962 Mar;1:238-43. doi: 10.1021/bi00908a007.
2
An easy method for the determination of initial rates.一种测定初始速率的简便方法。
Biochem J. 1981 Mar 1;193(3):1009-12. doi: 10.1042/bj1931009.
3
Half-time analysis of the integrated Michaelis equation. Simulation and use of the half-time plot and its direct linear variant in the analysis of some alpha-chymotrypsin, papain- and fumarase-catalysed reactions.米氏积分方程的半衰期分析。半衰期图及其直接线性变体在某些α-糜蛋白酶、木瓜蛋白酶和延胡索酸酶催化反应分析中的模拟与应用。
Biochem J. 1982 May 1;203(2):351-60. doi: 10.1042/bj2030351.
4
Purification and properties of inducible penicillin beta-lactamase isolated from Pseudomonas maltophilia.从嗜麦芽窄食单胞菌中分离出的诱导型青霉素β-内酰胺酶的纯化及特性
Antimicrob Agents Chemother. 1982 Oct;22(4):564-70. doi: 10.1128/AAC.22.4.564.
5
A spectroscopic study of metal ion and ligand binding to beta-lactamase II.金属离子与配体结合β-内酰胺酶II的光谱研究。
J Inorg Biochem. 1980 Nov;13(3):189-204. doi: 10.1016/s0162-0134(00)80068-9.
6
The 1H nuclear-magnetic-resonance spectroscopy of cobalt(II)-beta-lactamase II.钴（II）-β-内酰胺酶II的氢核磁共振光谱
Biochem J. 1980 Jun 1;187(3):789-95. doi: 10.1042/bj1870789.
7
The acyl-enzyme mechanism of beta-lactamase action. The evidence for class C Beta-lactamases.β-内酰胺酶作用的酰基-酶机制。C类β-内酰胺酶的证据。
Biochem J. 1982 Nov 1;207(2):315-22. doi: 10.1042/bj2070315.
8
Active sites of beta-lactamases. The chromosomal beta-lactamases of Pseudomonas aeruginosa and Escherichia coli.β-内酰胺酶的活性位点。铜绿假单胞菌和大肠杆菌的染色体β-内酰胺酶。
Biochem J. 1982 Mar 1;201(3):621-7. doi: 10.1042/bj2010621.
9
Isolation and properties of an inducible and a constitutive beta-lactamase from Pseudomonas aeruginosa.铜绿假单胞菌中一种诱导型和一种组成型β-内酰胺酶的分离与特性
J Gen Microbiol. 1982 Jan;128(1):155-9. doi: 10.1099/00221287-128-1-155.
10
ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type.大肠杆菌K-12的AmpC头孢菌素酶与青霉素酶型β-内酰胺酶有着不同的进化起源。
Proc Natl Acad Sci U S A. 1981 Aug;78(8):4897-901. doi: 10.1073/pnas.78.8.4897.
Zotero 插件