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Literature summary extracted from

  • Bognar, A.L.; Shane, B.
    Purification and properties of Lactobacillus casei folylpoly-gamma-glutamate synthetase (1983), J. Biol. Chem., 258, 12574-12581.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.2.17 ADP noncompetitive with respect to MgATP2- Lacticaseibacillus casei
6.3.2.17 beta,gamma-methylene-ATP
-
Lacticaseibacillus casei
6.3.2.17 phosphate competitive with respect to MgATP2- Lacticaseibacillus casei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.2.17 0.0023
-
5,10-methylene-5,6,7,8-tetrahydropteroyl-Glu2
-
Lacticaseibacillus casei
6.3.2.17 0.423
-
L-Glu
-
Lacticaseibacillus casei
6.3.2.17 5.6
-
ATP
-
Lacticaseibacillus casei

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.2.17 K+ absolutely dependent on monovalent cation, K+ is most effective Lacticaseibacillus casei
6.3.2.17 K+ maximal activity at 200 mM Lacticaseibacillus casei
6.3.2.17 Mg2+ MgATP2- is an effective substrate Lacticaseibacillus casei
6.3.2.17 Mn2+ MnATP2- is an effective substrate Lacticaseibacillus casei

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.2.17 43000
-
1 * 43000, SDS-PAGE Lacticaseibacillus casei

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.2.17
-
Lacticaseibacillus casei

Reaction

EC Number Reaction Comment Organism Reaction ID
6.3.2.17 ATP + tetrahydropteroyl-[gamma-Glu]n + L-glutamate = ADP + phosphate + tetrahydropteroyl-[gamma-Glu]n+1 ordered ter ter mechanism with MgATP binding first to the enzyme, folate second, and glutamate last 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 0.23
-
-
Lacticaseibacillus casei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.17 ATP + (6R)-5,10-methylene-5,6,7,8-tetrahydropteroyl-Glu + L-glutamate ATP in form of MgATP2- Lacticaseibacillus casei ADP + phosphate + (6R)-5,10-methylene-5,6,7,8-tetrahydropteroyl-Glu2
-
?
6.3.2.17 ATP + 5,10-methylene-5,6,7,8-tetrahydrofolic acid + L-glutamate
-
Lacticaseibacillus casei ADP + phosphate + 5,10-methylene-5,6,7,8-tetrahydrofolyl-Glu
-
?
6.3.2.17 ATP + 5,10-methylene-5,6,7,8-tetrahydropteroyl-gamma-Glun + Glu n: 3 Lacticaseibacillus casei ADP + phosphate + 5,10-methylene-5,6,7,8-tetrahydropteroyl-gamma-Glun+1
-
?
6.3.2.17 ATP + 5,10-methylene-5,6,7,8-tetrahydropteroyl-gamma-Glun + Glu n: 2 Lacticaseibacillus casei ADP + phosphate + 5,10-methylene-5,6,7,8-tetrahydropteroyl-gamma-Glun+1
-
?
6.3.2.17 dATP + 5,10-methylene-5,6,7,8-tetrahydropteroyl-Glu + Glu
-
Lacticaseibacillus casei dADP + phosphate + 5,10-methylene-5,6,7,8-tetrahydropteroyl-gamma-Glu2
-
?
6.3.2.17 GTP + 5,10-methylene-5,6,7,8-tetrahydropteroyl-gamma-Glu + Glu
-
Lacticaseibacillus casei GDP + phosphate + 5,10-methylene-5,6,7,8-tetrahydropteroyl-gamma-Glu2
-
?
6.3.2.17 ITP + 5,10-methylene-5,6,7,8-tetrahydropteroyl-Glu + Glu
-
Lacticaseibacillus casei IDP + phosphate + 5,10-methylene-5,6,7,8-tetrahydropteroyl-gamma-Glu2
-
?
6.3.2.17 UTP + 5,10-methylene-5,6,7,8-tetrahydropteroyl-Glu + Glu
-
Lacticaseibacillus casei UDP + phosphate + 5,10-methylene-5,6,7,8-tetrahydropteroyl-gamma-Glu2
-
?

Subunits

EC Number Subunits Comment Organism
6.3.2.17 monomer 1 * 43000, SDS-PAGE Lacticaseibacillus casei

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.2.17 additional information
-
additional information
-
Lacticaseibacillus casei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.2.17 10
-
-
Lacticaseibacillus casei