Regulation of AMP deaminase from chicken erythrocytes. A kinetic study of the allosteric interactions.

Abstract:

:The allosteric properties of AMP deaminase [EC 3.5.4.6] from chicken erythrocytes have been qualitatively and quantitatively accounted for by the concerted transition theory of Monod et al., on the assumption that this enzyme has different numbers of binding sites for each ligand. Theoretical curves yield a satisfactory fit for all experimental saturation functions with respect to activation by alkali metals and inhibition by Pi, assuming that the numbers of binding sites for AMP, alkali metals, and Pi are 4, 2, and 4, respectively. The enzyme was inhibited by concentrations of ATP and GTP below 0.1 and 0.25 mM, respectively, whereas activation of the enzyme was observed at ATP and GTP concentrations above 0.4 and 1.5 mM, respectively. These unusual kinetics with respect to ATP and GTP could be also accounted for by assuming 2 inhibitory and 4 activating sites for each ligand.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Yoshino M,Kawamura Y,Ogasawara N

doi

10.1093/oxfordjournals.jbchem.a131277

keywords:

subject

Has Abstract

pub_date

1976-08-01 00:00:00

pages

299-308

issue

2

eissn

0021-924X

issn

1756-2651

journal_volume

80

pub_type

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