L'existence chez Pseudomonas de deux ornithine carbamoyltransférases et le mécanisme de leur spécialisation physiologique

Doctorat en Sciencesinfo:eu-repo/semantics/nonPublishe

L'existence chez Pseudomonas de deux ornithine carbamoyltransférases et le mécanisme de leur spécialisation physiologique

Doctorat en Sciencesinfo:eu-repo/semantics/nonPublishe

L'existence chez Pseudomonas de deux ornithine carbamoyltransférases et le mécanisme de leur spécialisation physiologique

Doctorat en Sciencesinfo:eu-repo/semantics/nonPublishe

Ornithine carbamoyltransferase from Escherichia coli W. Purification, structure and steady state kinetic analysis

Ornithine carbamoyltransferase from E. coli W was purified to homogeneity. The enzyme has a molecular weight of 105000. It is composed of three apparently identical subunits with molecular weights of 35000. The mechanism of the ornithine carbamoyltransferase enzyme system from E. coli W was investigated kinetically by using the approach of product inhibition and dead end inhibition of both forward and reverse reactions. On the basis of the kinetic data and binding studies it appears that the mechanism of the reaction involves a compulsory sequence of substrate binding to the enzyme, in which carbamoylphosphate is the first substrate to bind to the enzyme and phosphate the last product to be released. The same studies also indicate that the mechanism involves dead end complexes. The reaction mechanism appears consistent with that proposed by Theorell and Chance. Values have been determined for the Michaelis and dissociation constants involved in the combination of each reactant with the enzyme. Comparison of the values for the kinetic constants which are common to both forward and reverse reaction have shown that they are always of a comparable magnitude.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

L-arginine utilization by Pseudomonas species

SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Study of the relationship among ornithine carbamoyltransferases by an immunological comparison of anabolic and catabolic enzymes

SCOPUS: NotDefined.jinfo:eu-repo/semantics/publishe

Structural and regulatory mutations allowing utilization of citrulline or carbamoylaspartate as a source of carbamoylphosphate in Escherichia coli K-12

SCOPUS: ar.jinfo:eu-repo/semantics/publishe

L Ornithine carbamoyltransferase from Saccharomyces cerevisiae: steady state kinetic analysis

SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Epiarginasic regulation in Saccharomyces cerevisiae. Citrulline, the third effector, acts as a specific binding site on the ornithine carbamoyltransferase

SCOPUS: ar.jinfo:eu-repo/semantics/publishe