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Literature summary extracted from

  • Shane, B.
    Pteroylpoly(gamma-glutamate) synthesis by Corynebacterium species. Studies on the mechanism of folylpoly(gamma-glutamate) synthetase (1980), J. Biol. Chem., 255, 5663-5667.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.2.17 ADP
-
 Corynebacterium sp.
6.3.2.17 beta,gamma-methylene-ATP
-
 Corynebacterium sp.
6.3.2.17 phosphate
-
 Corynebacterium sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.2.17 0.0021
-
 5,6,7,8-tetrahydropteroyl-Glu
-
 Corynebacterium sp.
6.3.2.17 0.018
-
 ATP
-
 Corynebacterium sp.
6.3.2.17 0.16
-
 5,6,7,8-tetrahydropteroyl-beta-Ala-Glu L-Glu Corynebacterium sp.

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.17 Corynebacterium sp.
-
-
-

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 Corynebacterium sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.17 ATP + 5,6,7,8-tetrahydropteroyl-beta-Ala-Glu + L-glutamate
-
 Corynebacterium sp. ADP + phosphate + 5,6,7,8-tetrahydropteroyl-beta-Ala-Glu2
-
 ?
6.3.2.17 ATP + 5,6,7,8-tetrahydropteroyl-beta-Ala-Glu + L-glutamate ATP in form of MgATP2- Corynebacterium sp. ADP + phosphate + 5,6,7,8-tetrahydropteroyl-beta-Ala-Glu2
-
 ?