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Literature summary extracted from

  • Sheng, Y.; Cross, J.A.; Shen, Y.; Smith, C.A.; Bognar, A.L.
    Mutation of an essential glutamate residue in folylpolyglutamate synthetase and activation of the enzyme by pteroate binding (2002), Arch. Biochem. Biophys., 402, 94-103.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.2.17 expression in Escherichia coli strain BL21 Escherichia coli
6.3.2.17 expression in Escherichia coli strain BL21 Lacticaseibacillus casei

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.2.17 microseeding, E143A mutant Lacticaseibacillus casei

Protein Variants

EC Number Protein Variants Comment Organism
6.3.2.17 E143A almost inactive Lacticaseibacillus casei
6.3.2.17 E143D almost inactive Lacticaseibacillus casei
6.3.2.17 E143Q almost inactive Lacticaseibacillus casei
6.3.2.17 E146Q completely inactive, no ATP binding is observed with this mutant Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.2.17 5,6,7,8-tetrahydrofolyl-Glu2 60% inhibition of ATP binding at 0.1 mM Escherichia coli
6.3.2.17 Dihydropteroic acid 5% inhibition of ATP binding at 0.1 mM Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.2.17 0.07
-
 ATP pH 9.75, temperature conditions not mentioned Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.2.17 additional information Escherichia coli the enzyme catalyzes the MgATP-dependent ligation of L-glutamate to tetrahydrofolate coenzymes or to antifolates at the gamma-carboxyl of the terminal glutamate to form polyglutamate derivatives ?
-
 ?
6.3.2.17 additional information Lacticaseibacillus casei the enzyme catalyzes the MgATP-dependent ligation of L-glutamate to tetrahydrofolate coenzymes or to antifolates at the gamma-carboxyl of the terminal glutamate to form polyglutamate derivatives ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.17 Escherichia coli
-
-
-
6.3.2.17 Lacticaseibacillus casei
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.2.17 0.0003
-
 mutant E143A, pH 9.75 Lacticaseibacillus casei
6.3.2.17 0.0005
-
 mutant E143Q, pH 9.75 Lacticaseibacillus casei
6.3.2.17 0.00055
-
 mutant E143D, pH 9.75 Lacticaseibacillus casei
6.3.2.17 0.2
-
 wild type enzyme, pH 9.75 Escherichia coli
6.3.2.17 0.2
-
 wild type enzyme, pH 9.75 Lacticaseibacillus casei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.17 ATP + 5,10-methylene-5,6,7,8-tetrahydrofolate-Glu2 + L-glutamate
-
 Escherichia coli ADP + phosphate + 5,10-methylene-5,6,7,8-tetrahydrofolyl-Glu3
-
 ?
6.3.2.17 ATP + 5,10-methylene-tetrahydrofolate-Glu2 + L-glutamate
-
 Lacticaseibacillus casei ADP + phosphate + 5,10-methylene-tetrahydrofolyl-Glu3
-
 ?
6.3.2.17 ATP + 5,6,7,8-tetrahydrofolate-Glu2 + L-glutamate
-
 Escherichia coli ADP + phosphate + 5,6,7,8-tetrahydrofolyl-Glu3
-
 ?
6.3.2.17 ATP + dihydropteroic acid + L-glutamate enhancement of ATP binding is observed in the presence of this substrate. The substrate causes a conformational change in the inactive fraction of the enzyme which allows it to bind ATP Escherichia coli ADP + dihydropteroyl-Glu
-
 ?
6.3.2.17 additional information the enzyme catalyzes the MgATP-dependent ligation of L-glutamate to tetrahydrofolate coenzymes or to antifolates at the gamma-carboxyl of the terminal glutamate to form polyglutamate derivatives Escherichia coli ?
-
 ?
6.3.2.17 additional information the enzyme catalyzes the MgATP-dependent ligation of L-glutamate to tetrahydrofolate coenzymes or to antifolates at the gamma-carboxyl of the terminal glutamate to form polyglutamate derivatives Lacticaseibacillus casei ?
-
 ?