Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.3.2.3 (glutathione synthetase)
 678 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Six factors were analyzed which may be involved in the decline of glutathione synthesis in the aging lens and cataract, with special emphasis placed upon the human lens. The factors included: 1) lability of gamma-glutamylcysteine synthetase, 2) paucity of gamma-glutamylcysteine synthetase in primate lenses as compared to other mammalian lenses, 3) enzyme activity reduction with age in the human lens, 4) rate control by reactant scarcity, especially of cysteine and magnesium ion, 5) rate control by inhibition using 5'-AMP, 5'-ADP and glutathione, and 6) possible dissociation of the multi-enzyme complex. It was concluded that decline of the glutathione synthetic capacity in vivo would be most likely caused by reduction of gamma-glutamylcysteine synthetase activity rather than of glutathione synthetase activity.
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PMID:Lenticular glutathione synthesis: rate-limiting factors in its regulation and decline. 614 Jan 27

The activity of glutathione synthetase from bovine lens was examined as a functions of the concentration of L-gamma-glutamyl-L-alpha-aminobutyrate, the dipeptide substrate required in the formation of ophthalmic acid. Several significant anomalies of the glutathione synthetase-catalyzed formation of ophthalmic acid were found. Curvilinearity of double reciprocal plots occurred with this substrate; this curvilinearity shows substrate activation of the reaction which is likely a result of negative cooperativity. Both ATP4- and, to a lesser extent Mg2+ inhibited the reaction, whereas MgATP2- is the substrate; maximum activity occurred with 2 mM Mg2+ in excess of the concentration of added ATP. This investigation shows that it is necessary to establish a defined set of conditions for reporting enzyme activity and that the usual practice of using very large concentrations of Mg2+ relative to ATP, and 5- to 20-fold excess of the dipeptide will give less than optimum activity. The unit of enzyme activity is suggested to be that activity in ml using 2 mM ATP, 4 mM Mg2+, 30 mM glycine and 15 mM L-gamma-glutamyl-alpha-aminobutyrate, which results in the formation of 1 nmole/minute of ADP or P(i). In this study, 5'-AMP was for the first time, shown to be an inhibitor of the reaction with a K(i) of 0.9 mM.
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PMID:Glutathathione synthetase of bovine lens: anomalies of the enzyme-catalyzed formation of ophthalmic acid. 654 96