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Literature summary extracted from

  • Imeson, H.C.; Cossins, E.A.
    Higher plant folylpolyglutamate synthetase. II. Some major catalytic properties of the enzyme from Pisum sativum (1991), J. Plant Physiol., 138, 483-488.
No PubMed abstract available

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.2.17 0.0035
-
5,6,7,8-tetrahydropteroyl-Glu
-
Pisum sativum
6.3.2.17 0.61
-
L-Glu
-
Pisum sativum
6.3.2.17 2.3
-
ATP
-
Pisum sativum

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.17 Pisum sativum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.2.17
-
Pisum sativum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.2.17 cotyledon
-
Pisum sativum
-

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-Glu + L-glutamate
-
Pisum sativum ADP + phosphate + 5,6,7,8-tetrahydropteroyl-Glu2
-
?
6.3.2.17 ATP + 5,6,7,8-tetrahydropteroyl-Glun + Glu n: 1 Pisum sativum ADP + phosphate + 5,6,7,8-tetrahydropteroyl-gamma-Glun+1
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.2.17 8.5
-
-
Pisum sativum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
6.3.2.17 7 10 7.4: about 50% of maximal activity Pisum sativum
6.3.2.17 7 10 7: about 20% of maximal activity, 10: about 50% of maximal activity Pisum sativum