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Literature DB >> 6409097

Kinetic parameters from progress curves of competing substrates. Application to beta-lactamases.

Abstract

The use of two substrates, one of them a reporter substrate, is often convenient. The time course of an enzymic reaction with competing substrates is given explicitly in the present paper. Kinetic parameters can be readily obtained. The method is applied to the hydrolysis of benzylpenicillin, with cephalosporin C as the reporter substrate, catalysed by a Pseudomonas beta-lactamase.

Entities: Chemical

Mesh：

Substances：

Year: 1983 PMID： 6409097 PMCID： PMC1154387 DOI： 10.1042/bj2110511

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

9 in total

1. A competition time-course method for following enzymic reactions applied to the hydrolysis of acetamide catalysed by an aliphatic amidase.

Authors: M R Hollaway; T Ticho
Journal: FEBS Lett Date: 1979-10-01 Impact factor: 4.124

2. A spectrophotometric assay of beta-lactamase action on penicillins.

Authors: S G Waley
Journal: Biochem J Date: 1974-06 Impact factor: 3.857

3. Characterization of an ammonium transport system in filamentous fungi with methylammonium-14C as the substrate.

Authors: S L Hackette; G E Skye; C Burton; I H Segel
Journal: J Biol Chem Date: 1970-09-10 Impact factor: 5.157

4. Mutant of Pseudomonas aeruginosa 18S that synthesizes type Id beta-lactamase constitutively.

Authors: F Flett; N A Curtis; M H Richmond
Journal: J Bacteriol Date: 1976-09 Impact factor: 3.490

5. Isolation and properties of an inducible and a constitutive beta-lactamase from Pseudomonas aeruginosa.

Authors: M Berks; K Redhead; E P Abraham
Journal: J Gen Microbiol Date: 1982-01

6. A quick method for the determination of inhibition constants.

Authors: S G Waley
Journal: Biochem J Date: 1982-09-01 Impact factor: 3.857

7. Use of alternative substrates to probe multisubstrate enzyme mechanisms.

Authors: C Y Huang
Journal: Methods Enzymol Date: 1979 Impact factor: 1.600

8. Cephalosporinase and penicillinase activities of a beta-lactamase from Pseudomonas pyocyanea.

Authors: L D Sabath; M Jago; E P Abraham
Journal: Biochem J Date: 1965-09 Impact factor: 3.857

9. The acyl-enzyme mechanism of beta-lactamase action. The evidence for class C Beta-lactamases.

Authors: V Knott-Hunziker; S Petursson; S G Waley; B Jaurin; T Grundström
Journal: Biochem J Date: 1982-11-01 Impact factor: 3.857

9 in total

5 in total

Kinetic parameters from progress curves of competing substrates. Application to beta-lactamases.

1. A competition time-course method for following enzymic reactions applied to the hydrolysis of acetamide catalysed by an aliphatic amidase.

2. A spectrophotometric assay of beta-lactamase action on penicillins.

3. Characterization of an ammonium transport system in filamentous fungi with methylammonium-14C as the substrate.

4. Mutant of Pseudomonas aeruginosa 18S that synthesizes type Id beta-lactamase constitutively.

5. Isolation and properties of an inducible and a constitutive beta-lactamase from Pseudomonas aeruginosa.

6. A quick method for the determination of inhibition constants.

7. Use of alternative substrates to probe multisubstrate enzyme mechanisms.

8. Cephalosporinase and penicillinase activities of a beta-lactamase from Pseudomonas pyocyanea.

9. The acyl-enzyme mechanism of beta-lactamase action. The evidence for class C Beta-lactamases.

1. Site-directed mutagenesis and substrate-induced inactivation of beta-lactamase I.

2. Site-directed mutagenesis of beta-lactamase I: role of Glu-166.

3. The pH-dependence of class B and class C beta-lactamases.

4. Imipenem as substrate and inhibitor of beta-lactamases.

5. Site-directed mutagenesis of beta-lactamase I. Single and double mutants of Glu-166 and Lys-73.