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Literature summary for 6.3.2.17 extracted from

  • Shane, B.
    Corynebacterium species folylpoly-gamma-glutamate synthetase (1982), Pept. Antibiot. Biosynth. Funct. (Kleinkauf H. et al. eds. ), , 353-368.
No PubMed abstract available
Search for more literature for 6.3.2.17

General Stability

General Stability Organism
MgATP2-, ATP or sulfhydryl compounds increase the lability of the enzyme Corynebacterium sp.

Inhibitors

Inhibitors Comment Organism Structure
ADP
-
 Corynebacterium sp.
ATP4-
-
 Corynebacterium sp.
beta,gamma-methylene-ATP
-
 Corynebacterium sp.
Borate
-
 Corynebacterium sp.
L-Glu-gamma-methylester
-
 Corynebacterium sp.
phosphate competitive with respect to MgATP2- Corynebacterium sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.018
-
 MgATP2- ATP Corynebacterium sp.
0.16
-
 5,6,7,8-tetrahydrofolyl-beta-L-Ala-L-Glu L-Glu Corynebacterium sp.

Metals/Ions

Metals/Ions Comment Organism Structure
K+ required form maximal activity Corynebacterium sp.
K+ maximal activity at 200 mM Corynebacterium sp.
Mg2+ required Corynebacterium sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
51000
-
 gel filtration Corynebacterium sp.
53000
-
 1 * 53000, SDS-PAGE 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.
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.57
-
-
 Corynebacterium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 10-formyl-5,6,7,8-tetrahydropteroyl-Glu + Glu
-
 Corynebacterium sp. ADP + phosphate + 10-formyl-5,6,7,8-tetrahydropteroyl-Glu2
-
 ?
ATP + 5,10-methylene-5,6,7,8-tetrahydropteroyl-gamma-Glun + Glu n:1 Corynebacterium sp. ADP + phosphate + 5,10-methylene-5,6,7,8-tetrahydropteroyl-gamma-Glun+1
-
 ?
ATP + 5,6,7,8-tetrahydrofolyl-beta-L-Ala-L-Glu + L-glutamate
-
 Corynebacterium sp. ADP + phosphate + 5,6,7,8-tetrahydrofolyl-beta-L-Ala-L-Glu2
-
 ?
ATP + 5,6,7,8-tetrahydropteroate + Glu
-
 Corynebacterium sp. ADP + phosphate + 5,6,7,8-terahydropteroyl-Glu
-
 ?
ATP + 5-methyl-5,6,7,8-tetrahydropteroyl-gamma-Glun + Glu n: 1 Corynebacterium sp. ADP + phosphate + 5-methyl-5,6,7,8-tetrahydropteroyl-gamma-Glun+1
-
 ?
ATP + 7,8-dihydropteroate + Glu
-
 Corynebacterium sp. ADP + phosphate + 7,8-dihydropteroyl-Glu
-
 ?
ATP + aminopterin + Glu
-
 Corynebacterium sp. ADP + phosphate + aminopteryl-Glu
-
 ?
ATP + methotrexate + Glu weak Corynebacterium sp. ADP + phosphate + methotrexyl-Glu
-
 ?
additional information dATP and UTP can act as substrate Corynebacterium sp. ?
-
 ?

Subunits

Subunits Comment Organism
? some anomalous behaviour in Sephadex G-150 suggests that the native or active form of the enzyme may be a multimer Corynebacterium sp.
monomer 1 * 53000, SDS-PAGE Corynebacterium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.5 10
-
 Corynebacterium sp.