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Literature summary for 1.5.1.33 extracted from

  • Luba, J.; Nare, B.; Liang, P.H.; Anderson, K.S.; Beverley, S.M.; Hardy, L.W.
    Leishmania major pteridine reductase 1 belongs to the short chain dehydrogenase family: stereochemical and kinetic evidence (1998), Biochemistry, 37, 4093-4104.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
5-Deaza-5,6,7,8-tetrahydrofolate
-
Leishmania major
additional information relatively insensitive to methorexate Leishmania major
NADP+
-
Leishmania major

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.001
-
folate
-
Leishmania major
0.0014
-
NADPH with folate as cosubstrate Leishmania major

Organism

Organism UniProt Comment Textmining
Leishmania major
-
-
-

Reaction

Reaction Comment Organism Reaction ID
5,6,7,8-tetrahydrobiopterin + 2 NADP+ = biopterin + 2 NADPH + 2 H+ ordered ternary complex mechanism with NADPH binding first and NADP+ dissociating after the reduced pteridine. The enzyme transfers the pro-S hydride of NADPH to carbon 6 on the si face of dihydrofolate Leishmania major

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Biopterin + NADPH
-
Leishmania major 5,6,7,8-Tetrahydrobiopterin + NADP+
-
?
folate + NADPH
-
Leishmania major 5,6,7,8-tetrahydrofolate + NADP+
-
?

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Leishmania major