TRIPEPTIDE (GLUTATHIONE) SYNTHETASE . PURIFICATION PROPERTIES AND MECHANISM OF ACTION
TRIPEPTIDE (GLUTATHIONE) SYNTHETASE . PURIFICATION PROPERTIES AND MECHANISM OF ACTION
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DOI：
10.1021/bi00858a022
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发表时间：
1967-01-01
期刊：
影响因子：
2.9
通讯作者：
MEISTER, A
中科院分区：
文献类型：
--
作者：
MOOZ, ED;MEISTER, A
Tripeptide (glutathione [gamma] -glutamyl-[alpha]-aminobutyrylglycine) synthetase has been purified about 5000-fold from baker''s yeast; the enzyme is homogeneous by electrophoretic and ultracentrifugal criteria (sedimentation coefficient 6.1 S, mol wt 123,000). Various properties of the enzyme including its amino acid composition, kinetic behavior, and specificity have been studied. The ability of the enzyme to catalyze adenosine triphosphate-adenosine diphosphate (ATP-ADP) exchange decreases greatly during purification. Evidence has been obtained that the rate of formation of the enzyme-bound dipeptide intermediate ([gamma] -glutamyl-[alpha]-aminobutyryl phosphate) in the absence of acceptor is of the same order as that of the over-all reaction, and that the ADP formed in this reaction dissociates relatively slowly from the enzyme. It is tentatively concluded there are about 4 active sites per molecule of enzyme.
