par Stalon, Victor 
;Legrain, Christiane ;Wiame, Jean-Marie
Référence European journal of biochemistry / FEBS, 74, 2, page (319-327)
Publication Publié, 1977
;Legrain, Christiane ;Wiame, Jean-Marie Référence European journal of biochemistry / FEBS, 74, 2, page (319-327)
Publication Publié, 1977
Article révisé par les pairs
| Résumé : | The anabolic ornithine carbamoyltransferase of Pseudomonas appears to be extremely specialized. Unlike the other carbamoyltransferases studied, this enzyme catalyzes the phosphorolytic cleavage of citrulline with a very poor efficiency. The main goal of this paper is to understand what, in the catalytic process, causes this directed functional specialization. On the basis of kinetic data and thermodynamic properties of the reaction, it appears that the reaction mechanism is the same as for ornithine carbamoyltransferases from other sources, that is, of the sequential ordered type, where carbamoylphosphate is the first substrate to be bound and phosphate the last product to be released. In addition to this, and here lies the difference with other ornithine carbamoyltransferases, the anabolic transferase of Pseudomonas forms a binary dead‐end complex with citrulline, leading to inefficient binding of phosphate and citrul‐line to the enzyme. Therefore the phosphorolytic cleavage of citrulline is equally inefficient. It should be mentioned that the affinity of the enzyme for citrulline at its catalytic site is low as compared to other transferases. Copyright © 1977, Wiley Blackwell. All rights reserved |
