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Literature summary for 6.3.2.17 extracted from

  • Sun, X.; Cross, J.A.; Bognar, A.L.; Baker, E.N.; Smith, C.A.
    Folate-binding triggers the activation of folylpolyglutamate synthetase (2001), J. Mol. Biol., 310, 1067-1078.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Lacticaseibacillus casei

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme-MgAMPPCP complex is produced by soaking apoFPGS crystals, grown overnight in a solution containing 20% PEG4000, 10 mM AMPPCP, 20 mM MgCl2, 100 mM KCl and 50 mM CAPSO, pH 9.0. The enzyme has a ATP-binding pocket in deep cleft formed between the N and C-domains, the folate-binding site is located in the interdomain cleft, His316, Ser412 and Lys346 are involved in the L-glutamate binding site Lacticaseibacillus casei

Organism

Organism UniProt Comment Textmining
Lacticaseibacillus casei P15925
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-

Purification (Commentary)

Purification (Comment) Organism
chromatography on a chitin column Lacticaseibacillus casei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 5,10-methylene-5,6,7,8-tetrahydrofolic acid + L-glutamate
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Lacticaseibacillus casei ADP + phosphate + 5,10-methylene-5,6,7,8-tetrahydrofolyl-Glu
-
?
ATP + 5,6,7,8-tetrahydrofolic acid + L-glutamate
-
Lacticaseibacillus casei ADP + phosphate + 5,6,7,8-tetrahydrofolyl-Glu
-
?