Research graph
References from Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. Local targets link to admitted publications; unresolved targets remain external evidence.
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Aspartate 458 of human glutathione synthetase is important for cooperativity and active site structure
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Function of conserved residues of human glutathione synthetase: implications for the ATP-grasp enzymes
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Valine 44 and valine 45 of human glutathione synthetase are key for subunit stability and negative cooperativity
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Evolution of negative Cooperativity in Glutathione Transferase Enabled Preservation of Enzyme Function
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The physiological significance of negative cooperativity revisited
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Modeling the Role of negative Cooperativity in Metabolic Regulation and Homeostasis
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Ubereinen in biologischen Beziehung wiechtigen Einfluss den die kohlensauresparnung de bluter auf dessen sauerstoff binduing üft
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Unresolved reference
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Unresolved reference
External reference
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Human hereditary glutathione synthetase deficiency: kinetic properties of mutant enzymes
10.1042/bj20040114 · 2004 · External reference
Kinetic properties of missense mutations in patients with glutathione synthetase deficiency
10.1042/bj3490275 · 2000 · External reference
