Mutations in the hinge of a dynamic loop broadly influence functional properties of fructose-1,6-bisphosphatase.

Abstract excerpt

Loop 52-72 of porcine fructose-1,6-bisphosphatase may play a central role in the mechanism of catalysis and allosteric inhibition by AMP. The loop pivots between different conformational states about a hinge located at residues 50 and 51. The insertion of proline separately at positions 50 and 51 reduces k(cat) by up to 3-fold, with no effect on the K(m) for fructose 1,6-bisphosphate. The K(a) for Mg(2+) in the...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Adenosine Monophosphate
• Share to Alanine
• Share to Allosteric Regulation