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Literature summary for 6.3.2.17 extracted from

  • Tomsho, J.W.; Moran, R.G.; Coward, J.K.
    Concentration-dependent processivity of multiple glutamate ligations catalyzed by folylpoly-gamma-glutamate synthetase (2008), Biochemistry, 47, 9040-9050.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens folylpoly-gamma-glutamate synthetase can catalyze the processive addition of approximately four glutamate residues to (6R)-5,10-dideaza-5,6,7,8-tetrahydropteroylglutamic acid. The degree of processivity is dependent on the concentration of the folate substrate, thus suggesting a mechanism for the regulation of folate polyglutamate synthesis in cells ?
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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Reaction

Reaction Comment Organism Reaction ID
ATP + tetrahydropteroyl-[gamma-Glu]n + L-glutamate = ADP + phosphate + tetrahydropteroyl-[gamma-Glu]n+1 processive mechanism, in which the folate is the first substrate to bind and the folate-Glu product is the last to be released Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information folylpoly-gamma-glutamate synthetase can catalyze the processive addition of approximately four glutamate residues to (6R)-5,10-dideaza-5,6,7,8-tetrahydropteroylglutamic acid. The degree of processivity is dependent on the concentration of the folate substrate, thus suggesting a mechanism for the regulation of folate polyglutamate synthesis in cells Homo sapiens ?
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?