Iron: a possible heterotropic effector of prolyl hydroxylase.
The mechanism of ferrous ion binding to prolyl hydroxylase (prolyl-glycyl-peptide,2-oxoglutarate:oxygen oxidoreductase, EC 1.14.11.2) was studied according to Koshland's curve-fitting procedure (Cornish-Bowden, A. and Koshland, Jr., D.E. (1970) Biochemistry 9, 3325--3336). The calculated data obtained by means of the unrestricted Adair equation were found to provide an adequate fit with experimentally obtained values, whereas those obtained on the basis of Michaelis-Menten kinetics did not. This suggests that prolyl hydroxylase could be an allosteric enzyme under positive heterotropic control.
D003201:Computers; D007501:Iron / Q000494:pharmacology*; D007700:Kinetics; D008433:Mathematics; D011393:Procollagen-Proline Dioxygenase / Q000378:metabolism*; D011485:Protein Binding
D007501:Iron; D011393:Procollagen-Proline Dioxygenase