Premium
Inhibition of glyoxalase I by thermal copolyamino acids
Author(s) -
Syren Robert M.,
Windsor Charles R.,
Fox Sidney W.
Publication year - 2009
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.560160717
Subject(s) - chemistry , tryptophan , cysteine , amino acid , lactoylglutathione lyase , inhibitory postsynaptic potential , biochemistry , composition (language) , glutathione , stereochemistry , enzyme , biology , neuroscience , linguistics , philosophy
Variations in the composition of thermal copolyamino acids inhibitory for glyoxalase I have been studied. Those produced from both tryptophan and cysteine are the most active. The activity requires the polymeric state since the free amino acids are devoid of activity. On the basis of these studies and others elsewhere, hydrophobicily appears to be a significant physical property contributing to the activity of some of the inhibitors.