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Literature summary for 6.3.2.17 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

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Corynebacterium sp.
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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.

Substrates and Products (Substrate)

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