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羧基作为β-内酰胺酶中的必需残基。

Carboxy groups as essential residues in beta-lactamases.

作者信息

Little C, Emanuel E L, Gagnon J, Waley S G

出版信息

Biochem J. 1986 Nov 15;240(1):215-9. doi: 10.1042/bj2400215.

DOI:10.1042/bj2400215
PMID:3493768
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1147395/
Abstract

Beta-lactamases are divided into classes A, B and C on the basis of their amino acid sequences. Beta-Lactamases were incubated at pH 4.0 with the carboxy-group reagent 1-(3-dimethylaminopropyl)-3-ethylcarbodi-imide plus a coloured nucleophile and the extents of inactivation and nucleophile incorporation were monitored. Two class A enzymes (from Bacillus cereus and Bacillus licheniformis) and two class C enzymes (from Enterobacter cloacae P99 and Pseudomonas aeruginosa) were examined. All four enzymes were inactivated, with total inactivation corresponding to the incorporation of approx. 2-3 mol of nucleophile/mol of enzyme. In the case of beta-lactamase I from Bacillus cereus, some 53% of the incorporated nucleophile was located on glutamic acid-168 in the amino acid sequence.

摘要

β-内酰胺酶根据其氨基酸序列分为A、B和C类。将β-内酰胺酶在pH 4.0条件下与羧基试剂1-(3-二甲基氨基丙基)-3-乙基碳二亚胺以及一种带色亲核试剂一起温育,并监测失活程度和亲核试剂掺入情况。检测了两种A类酶(来自蜡样芽孢杆菌和地衣芽孢杆菌)和两种C类酶(来自阴沟肠杆菌P99和铜绿假单胞菌)。所有四种酶均被失活,完全失活对应于每摩尔酶掺入约2 - 3摩尔亲核试剂。就蜡样芽孢杆菌的β-内酰胺酶I而言,掺入的亲核试剂约53%位于氨基酸序列中的谷氨酸-168上。

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2
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引用本文的文献

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本文引用的文献

1
Relation between modification of functional groups of proteins and their biological activity. I.A graphical method for the determination of the number and type of essential groups.蛋白质官能团修饰与其生物活性之间的关系。I. 一种确定必需基团数量和类型的图解方法。
Sci Sin. 1962 Nov;11:1535-58.
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A method for characterizing the type and numbers of groups involved in enzyme action.一种表征参与酶作用的基团类型和数量的方法。
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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.
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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.
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Chemical modification of proteins: plotting of the remaining activity against the number of residues modified.蛋白质的化学修饰:将剩余活性相对于修饰残基数量作图。
J Biochem. 1984 Mar;95(3):605-9. doi: 10.1093/oxfordjournals.jbchem.a134648.
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The active site of the P99 beta-lactamase from Enterobacter cloacae.阴沟肠杆菌P99β-内酰胺酶的活性位点。
Biochem J. 1984 Oct 1;223(1):271-4. doi: 10.1042/bj2230271.
7
Purification of beta-lactamases by affinity chromatography on phenylboronic acid-agarose.通过苯基硼酸 - 琼脂糖亲和层析法纯化β - 内酰胺酶。
Biochem J. 1984 Jul 15;221(2):505-12. doi: 10.1042/bj2210505.
8
Rat brain Thy-1 glycoprotein. The amino acid sequence, disulphide bonds and an unusual hydrophobic region.大鼠脑甲状腺素-1糖蛋白。氨基酸序列、二硫键及一个不同寻常的疏水区域。
Biochem J. 1981 Apr 1;195(1):15-30. doi: 10.1042/bj1950015.
9
The structure of beta-lactamases.β-内酰胺酶的结构
Philos Trans R Soc Lond B Biol Sci. 1980 May 16;289(1036):321-31. doi: 10.1098/rstb.1980.0049.
10
Cephalosporinase and penicillinase activities of a beta-lactamase from Pseudomonas pyocyanea.铜绿假单胞菌β-内酰胺酶的头孢菌素酶和青霉素酶活性
Biochem J. 1965 Sep;96(3):739-52. doi: 10.1042/bj0960739.