Literature DB >> 1747132

Allosteric regulation of phosphonoacetaldehyde hydrolase by n-butylphosphonic acid.

C Dumora1, A M Lacoste, A Cassaigne, J P Mazat.   

Abstract

The effect of n-butylphosphonic acid on the activity of phosphonoacetaldehyde hydrolase from Pseudomonas aeruginosa was investigated: at low concentrations this compound appeared as an activator of the enzyme activity, whereas at higher concentrations it exhibited inhibitory properties. The experimental results were modelled according to an allosteric model involving two different classes of sites for n-butylphosphonic acid.

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Year:  1991        PMID： 1747132      PMCID： PMC1130586          DOI： 10.1042/bj2800557

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


  13 in total

1.  ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.

Authors:  J MONOD; J WYMAN; J P CHANGEUX
Journal:  J Mol Biol       Date:  1965-05       Impact factor: 5.469

2.  Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase.

Authors:  J M La Nauze; J R Coggins; H B Dixon
Journal:  Biochem J       Date:  1977-08-01       Impact factor: 3.857

3.  Role of effector binding in allosteric control of ribonucleoside diphosphate reductase.

Authors:  N C Brown; P Reichard
Journal:  J Mol Biol       Date:  1969-11-28       Impact factor: 5.469

4.  Ribonucleoside diphosphate reductase. Purification of the two subunits, proteins B1 and B2.

Authors:  N C Brown; Z N Canellakis; B Lundin; P Reichard; L Thelander
Journal:  Eur J Biochem       Date:  1969-07

5.  The enzymic cleavage of the carbon-phosphorus bond: purification and properties of phosphonatase.

Authors:  J M La Nauze; H Rosenberg; D C Shaw
Journal:  Biochim Biophys Acta       Date:  1970-08-15

6.  Comparison of experimental binding data and theoretical models in proteins containing subunits.

Authors:  D E Koshland; G Némethy; D Filmer
Journal:  Biochemistry       Date:  1966-01       Impact factor: 3.162

7.  Phosphonoacetaldehyde hydrolase from Pseudomonas aeruginosa: purification properties and comparison with Bacillus cereus enzyme.

Authors:  C Dumora; A M Lacoste; A Cassaigne
Journal:  Biochim Biophys Acta       Date:  1989-08-31

8.  Investigation of the Bacillus cereus phosphonoacetaldehyde hydrolase. Evidence for a Schiff base mechanism and sequence analysis of an active-site peptide containing the catalytic lysine residue.

Authors:  D B Olsen; T W Hepburn; M Moos; P S Mariano; D Dunaway-Mariano
Journal:  Biochemistry       Date:  1988-03-22       Impact factor: 3.162

9.  Lysine-sensitive aspartokinase of Escherichia coli K12. Synergy and autosynergy in an allosteric V system.

Authors:  J P Mazat; J C Patte
Journal:  Biochemistry       Date:  1976-09-07       Impact factor: 3.162

10.  Purification and properties of 2-aminoethylphosphonate:pyruvate aminotransferase from Pseudomonas aeruginosa.

Authors:  C Dumora; A M Lacoste; A Cassaigne
Journal:  Eur J Biochem       Date:  1983-06-01
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