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Literature summary for 1.5.1.3 extracted from

  • Nare, B.; Hardy, L.W.; Beverley, S.M.
    The roles of pteridine reductase 1 and dihydrofolate reductase-thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major (1997), J. Biol. Chem., 272, 13883-13891.
    View publication on PubMed
Search for more literature for 1.5.1.3

Cloned(Commentary)

Cloned (Comment) Organism
expression of dhfr gene in Escherichia coli Leishmania major

Protein Variants

Protein Variants Comment Organism
additional information knockout mutant dhfr-ts- Leishmania major

Inhibitors

Inhibitors Comment Organism Structure
methotrexate
-
 Leishmania major

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0041
-
 folate bifunctional enzyme DHFR-thymidylate synthase Leishmania major

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7,8-dihydrofolate + NADPH Leishmania major
-
 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
additional information Leishmania major dihydrofolate reductase deficient mutant needs thymidine for growth, pathway overview ?
-
 ?
additional information Leishmania major knockout mutants with either no pteridine reductase or dihydrofolate reductase activity revealed in comparison to wild-type that 90% of the cellular dihydrofolate reduction activity belongs to DHFR and 10% of the cellular dihydrofolate reductase activity belongs to pteridine reductase ?
-
 ?

Organism

Organism UniProt Comment Textmining
Leishmania major
-
 bifunctional enzyme dihydrofolate reductase-thymidylate synthase
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli Leishmania major

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0025
-
 bifunctional enzyme DHFR-thymidylate synthase, substrate folate Leishmania major
6.4
-
 bifunctional enzyme DHFR-thymidylate synthase, substrate 7,8-dihydrofolate Leishmania major

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7,8-dihydrofolate + NADPH
-
 Leishmania major 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
7,8-dihydrofolate + NADPH bifunctional enzyme DHFR-thymidylate synthase Leishmania major 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
folate + NADPH slow rate Leishmania major 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
folate + NADPH bifunctional enzyme DHFR-thymidylate synthase Leishmania major 5,6,7,8-tetrahydrofolate + NADP+
-
 ?
additional information no activity with pterins Leishmania major ?
-
 ?
additional information dihydrofolate reductase deficient mutant needs thymidine for growth, pathway overview Leishmania major ?
-
 ?
additional information knockout mutants with either no pteridine reductase or dihydrofolate reductase activity revealed in comparison to wild-type that 90% of the cellular dihydrofolate reduction activity belongs to DHFR and 10% of the cellular dihydrofolate reductase activity belongs to pteridine reductase Leishmania major ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 bifunctional enzyme DHFR-thymidylate synthase, substrate folate, sodium acetate buffer Leishmania major
7
-
 bifunctional enzyme DHFR-thymidylate synthase, substrate 7,8-dihydrofolate, sodium phosphate buffer Leishmania major

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Leishmania major

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0000001
-
 methotrexate recombinant enzyme Leishmania major