INTERACTION OF PHOSPHONOMETHYL ANALOG OF DIHYDROXYACETONE PHOSPHATE WITH RABBIT MUSCLE ALDOLASE

Authors
PAGE P BLONSKI C PERIE J
Citation
P. Page et al., INTERACTION OF PHOSPHONOMETHYL ANALOG OF DIHYDROXYACETONE PHOSPHATE WITH RABBIT MUSCLE ALDOLASE, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1386(1), 1998, pp. 59-64
Citations number
32
Categorie Soggetti
Biology,Biophysics
Journal title
Biochimica et biophysica acta. Protein structure and molecular enzymology → ACNP
ISSN journal
01674838
Volume
1386
Issue
1
Year of publication
1998
Pages
59 - 64
Database
ISI
SICI code
0167-4838(1998)1386:1<59:IOPAOD>2.0.ZU;2-Y
Abstract
Aldolase presents the same binding affinity for dihydroxyacetone phosp hate and its phosphonomethyl analog, but the partition coefficient bet ween the intermediates from the Michaelis complex to the eneamine is d ifferent. The effects of the structural modification of the triose pho sphate substrate on the interaction with rabbit muscle aldolase are di scussed in connection with the mechanistic pathway and the three-dimen sional structure of the enzyme. (C) 1998 Elsevier Science B.V. All rig hts reserved.