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Literature summary for 6.3.2.12 extracted from

  • Shane, B.
    Properties of Corynebacterium species dihydrofolate synthetase-folylpolyglutamate synthetase (1983), Chem. Biol. Pteridines, Proc. Int. Symp. Pteridines Folic Acid Deriv. Chem. Biol. Clin. Aspects, , 621-626.
No PubMed abstract available

General Stability

General Stability Organism
relatively stable to trypsin pretreatment and relatively large amounts of protease and a temperature of 37°C are required for digestion Corynebacterium sp.

Inhibitors

Inhibitors Comment Organism Structure
pABA
-
Corynebacterium sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0012
-
7,8-dihydropteroate
-
Corynebacterium sp.

Metals/Ions

Metals/Ions Comment Organism Structure
K+ monovalent cation required, 200 mM K+ is most effective Corynebacterium sp.

Organism

Organism UniProt Comment Textmining
Corynebacterium sp.
-
enzyme posseses both dihydrofolate synthetase activity and folylpolyglutamate synthetase activity
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 7,8-dihydropteroate + L-Glu
-
Corynebacterium sp. ADP + phosphate + 7,8-dihydrofolate
-
?
dATP + 7,8-dihydropteroate + L-Glu 40.5% of the activity relative to ATP Corynebacterium sp. dADP + phosphate + 7,8-dihydrofolate
-
?
GTP + 7,8-dihydropteroate + L-Glu 11.0% of the activity relative to ATP Corynebacterium sp. GDP + phosphate + 7,8-dihydrofolate
-
?
ITP + 7,8-dihydropteroate + L-Glu 7.8% of the activity relative to ATP Corynebacterium sp. IDP + phosphate + 7,8-dihydrofolate
-
?
UTP + 7,8-dihydropteroate + L-Glu 79.8% of the activity relative to ATP Corynebacterium sp. UDP + phosphate + 7,8-dihydrofolate
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
-
Corynebacterium sp.