Open AccessMuscle Pyruvate Kinase: Interaction with Substrates and Analogues Studied by Difference Spectroscopy
Author(s) -
BREVET Annie,
ROUSTAN Claude,
PRADEL LouiseAnne,
THOAI Nguyen
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb04002.x
Subject(s) - nucleotide , pyruvate kinase , phosphotransferases , substrate (aquarium) , binding site , chemistry , enzyme , biochemistry , stereochemistry , biology , glycolysis , gene , ecology
The substrate binding sites of pyruvate kinase have been studied by means of spectrophotometric investigations. Two binding sites, one for the nucleotide substrate and one for the acceptor, have been characterized. The interaction of nucleotide substrates with the enzyme, which is metal‐dependent, results in a perturbation of the spectrum of the nucleotide chromophore characterized by hypochromic and red shift effects; the hydrophobicity of the nucleotide site was estimated by using a reporter group reagent, 2‐(dansylamino)ethyl monophosphate. The interaction of pyruvate or phospho enol pyruvate with pyruvate kinase induces perturbation of a tyrosyl chromophore. The comparison between the binding sites of several ATP phosphotransferases is discussed and some common features are reported.