Influence of phosphoenolpyruvate and magnesium ions on the quaternary structure of enzyme I of the phosphotransferase system from gram-positive bacteria.

Abstract:

:Solution X-ray scattering patterns of enzyme I of the phosphotransferase system from Staphylococcus carnosus indicate an increase in radius of gyration and molecular mass in the presence of Mg2+ or both Mg2+ and phosphoenolpyruvate, indicating a partial dimerization of enzyme I. Mg2+ ions are essential for both the dimerization and the activation, whereas the substrate phosphoenolpyruvate shifts the monomer--dimer equilibrium to the enzymatically active dimer by decreasing the dissociation rate of the phosphorylated dimer.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Hübner G,König S,Koch MH,Hengstenberg W

doi

10.1021/bi00048a014

subject

Has Abstract

pub_date

1995-12-05 00:00:00

pages

15700-3

issue

48

eissn

0006-2960

issn

1520-4995

journal_volume

34

pub_type

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