W. Rathbun
Oct 1, 1967
Citations
0
Influential Citations
27
Citations
Quality indicators
Journal
Archives of biochemistry and biophysics
Abstract
Abstract Seventy-one compounds have been tested for their ability to couple with l -glutamic acid to form a γ-glutamyl peptide bond through the action of a purified preparation of γ-glutamyl-cysteine synthetase from bovine lens. The most active amino acids in the system were l -cysteine, l -α-aminobutyrate, and their esters, β-chloro- l -alanine, S -methyl- l -cysteine, l -cycloserine, l -norvaline, allothreonine, allylglycine, β-aminoisobutyrate, and l -homocysteine. The specificity pattern displayed by the enzyme allowed certain conclusions to be drawn concerning its requirements for the cysteine moiety. Several of the isolated enzymic products were hydrolyzed, and formed glutamic acid and the original cysteine analogue. The values for the apparent K m and maximal velocity were determined for many of the reactions.