Sandbox Reserved 771: Difference between revisions

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'''Glutathione Synthetase''' is the key enzyme involved in the ATP-dependent condensation of γ-Glutamylcysteine and glycine to form Glutathione during the second step of the glutathione biosynthesis pathway <ref>http://www.ncbi.nlm.nih.gov/protein/NP_000169.1</ref>. <ref>21771585</~~red~~>). The condensation begins by binding of ATP to GSS in the presence of γ-Glutamylcysteine, to form an enzyme-bound acyl-phosphate that binds glycine and generates the enzyme-product complex. Dissociation of GSS from the E::P complex results in release of GSH, ADP, and inorganic phosphate (Pi) <ref>PMID:20800579</ref>. The ATP-dependence of the catalysis qualifies GSS for inclusion into the ligase enzyme superfamily. Further, a Hill constant of ~0.67 indicates that GSS exhibits negative cooperativity towards the substrate γ-Glutamylcysteine <ref>PMID:21771585</ref>.

'''Glutathione Synthetase''' is the key enzyme involved in the ATP-dependent condensation of γ-Glutamylcysteine and glycine to form Glutathione during the second step of the glutathione biosynthesis pathway <ref>http://www.ncbi.nlm.nih.gov/protein/NP_000169.1</ref>. <ref>21771585</ref>. The condensation begins by binding of ATP to GSS in the presence of γ-Glutamylcysteine, to form an enzyme-bound acyl-phosphate that binds glycine and generates the enzyme-product complex. Dissociation of GSS from the E::P complex results in release of GSH, ADP, and inorganic phosphate (Pi) <ref>PMID:20800579</ref>. The ATP-dependence of the catalysis qualifies GSS for inclusion into the ligase enzyme superfamily. Further, a Hill constant of ~0.67 indicates that GSS exhibits negative cooperativity towards the substrate γ-Glutamylcysteine <ref>PMID:21771585</ref>.

Sandbox Reserved 771: Difference between revisions

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Revision as of 03:49, 7 December 2013 view source Elliott Wyatt (talk \| contribs) 42 edits No edit summary ← Older edit		Revision as of 04:01, 7 December 2013 view source Elliott Wyatt (talk \| contribs) 42 edits No edit summary Newer edit →
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	'''Glutathione Synthetase''' is the key enzyme involved in the ATP-dependent condensation of γ-Glutamylcysteine and glycine to form Glutathione during the second step of the glutathione biosynthesis pathway <ref>http://www.ncbi.nlm.nih.gov/protein/NP_000169.1</ref>. <ref>21771585</~~red~~>). The condensation begins by binding of ATP to GSS in the presence of γ-Glutamylcysteine, to form an enzyme-bound acyl-phosphate that binds glycine and generates the enzyme-product complex. Dissociation of GSS from the E::P complex results in release of GSH, ADP, and inorganic phosphate (Pi) <ref>PMID:20800579</ref>. The ATP-dependence of the catalysis qualifies GSS for inclusion into the ligase enzyme superfamily. Further, a Hill constant of ~0.67 indicates that GSS exhibits negative cooperativity towards the substrate γ-Glutamylcysteine <ref>PMID:21771585</ref>.		'''Glutathione Synthetase''' is the key enzyme involved in the ATP-dependent condensation of γ-Glutamylcysteine and glycine to form Glutathione during the second step of the glutathione biosynthesis pathway <ref>http://www.ncbi.nlm.nih.gov/protein/NP_000169.1</ref>. <ref>21771585</ref>. The condensation begins by binding of ATP to GSS in the presence of γ-Glutamylcysteine, to form an enzyme-bound acyl-phosphate that binds glycine and generates the enzyme-product complex. Dissociation of GSS from the E::P complex results in release of GSH, ADP, and inorganic phosphate (Pi) <ref>PMID:20800579</ref>. The ATP-dependence of the catalysis qualifies GSS for inclusion into the ligase enzyme superfamily. Further, a Hill constant of ~0.67 indicates that GSS exhibits negative cooperativity towards the substrate γ-Glutamylcysteine <ref>PMID:21771585</ref>.