Allosteric regulation in Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase revisited: association of concerted homotropic cooperative interactions and local heterotropic effects

1998 ◽  
Vol 283 (3) ◽  
pp. 695-704 ◽  
Author(s):  
C Tricot ◽  
V Villeret ◽  
G Sainz ◽  
O Dideberg ◽  
V Stalon
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Allosteric Regulation ◽  
Ornithine Carbamoyltransferase ◽  
Cooperative Interactions

scholarly journals The Global Arginine Regulator ArgR Controls Expression of argF in Pseudomonas syringae pv. phaseolicola but Is Not Required for the Synthesis of Phaseolotoxin or for the Regulated Expression of argK

2004 ◽  
Vol 186 (11) ◽  
pp. 3653-3655 ◽  
Author(s):  
José Luis Hernández-Flores ◽  
Karina López-López ◽  
Rogelio Garcidueñas-Piña ◽  
Alba E. Jofre-Garfias ◽  
Ariel Alvarez-Morales
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Pseudomonas Syringae ◽  
Ornithine Carbamoyltransferase ◽  
Regulated Expression

ABSTRACT In Pseudomonas syringae pv. phaseolicola the enzyme ornithine carbamoyltransferase (OCTase), encoded by argF, is negatively regulated by argR, similar to what has been reported for Pseudomonas aeruginosa. However, production of the phaseolotoxin-resistant OCTase encoded by argK, synthesis of phaseolotoxin, and infectivity for bean pods occur independently of the ArgR protein.

scholarly journals Allosteric regulation of phosphonoacetaldehyde hydrolase by n-butylphosphonic acid

1991 ◽  
Vol 280 (2) ◽  
pp. 557-559
Author(s):  
C Dumora ◽  
A M Lacoste ◽  
A Cassaigne ◽  
J P Mazat
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Enzyme Activity ◽  
Allosteric Regulation ◽  
Experimental Results ◽  
Low Concentrations ◽  
Allosteric Model

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.

scholarly journals Kinetic studies of allosteric catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa

1998 ◽  
Vol 251 (1-2) ◽  
pp. 528-533 ◽  
Author(s):  
Germaine Sainz ◽  
Catherine Tricot ◽  
Marie-Francoise Foray ◽  
Dominique Marion ◽  
Otto Dideberg ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Kinetic Studies ◽  
Ornithine Carbamoyltransferase

Purification, crystallization and preliminary X-ray analysis of catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa

1999 ◽  
Vol 55 (9) ◽  
pp. 1591-1593 ◽  
Author(s):  
G. Sainz ◽  
J. Vicat ◽  
R. Kahn ◽  
C. Tricot ◽  
V. Stalon ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Point Group ◽  
Unit Cell ◽  
Group Symmetry ◽  
Ornithine Carbamoyltransferase ◽  
Unit Cell Parameters ◽  
Crystal Forms ◽  
Space Group ◽  
Cell Parameters ◽  
Hexagonal Crystals

The catabolic ornithine carbamoyltransferase (OTCase) from Pseudomonas aeruginosa exhibits allosteric behaviour, with two conformational states of the molecule: an active R form and an inactive T form. The enzyme is a dodecamer with a molecular mass of 455700 Da. Three crystal forms have been obtained. Crystals of allosteric state T are rhombohedral, belonging to the R3 space group, with hexagonal unit-cell parameters a = b = 180.6, c = 122.0 Å. They diffract to a resolution of 4.5 Å. Two crystal forms for allosteric state R have been obtained, with hexagonal and cubic symmetries. Hexagonal crystals, which diffract to a resolution of 3.4 Å, belong to the space group P63 with unit-cell parameters a = b = 140.8, c = 145.6 Å. The cubic crystals belong to space group I23, with unit-cell parameter a = 134.32 Å and diffract to a resolution better than 2.5 Å. In all crystal forms, the dodecamer exhibits a 23 point-group symmetry.

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