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Literature summary for 1.5.1.33 extracted from

  • Herrmann, F.C.; Sivakumar, N.; Jose, J.; Costi, M.P.; Pozzi, C.; Schmidt, T.J.
    In silico identification and in vitro evaluation of natural inhibitors of Leishmania major pteridine reductase I (2017), Molecules, 22, 2166 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.5.1.33

Inhibitors

Inhibitors Comment Organism Structure
(-)-epicatechin-3-gallate
-
 Leishmania major
2,3-dehydrosilybin A
-
 Leishmania major
apigenin-7-glucoside
-
 Leishmania major
eleutheroside B
-
 Leishmania major
garcinone C
-
 Leishmania major
icariside II
-
 Leishmania major
isosilybin B
-
 Leishmania major
isoxanthohumol
-
 Leishmania major
additional information in silico identification and in vitro evaluation of natural inhibitors of Leishmania major pteridine reductase I. No inhibition by phillyrin, magnolin, and isosakuranetin. Docking study of inhibitors using the structure of LmPTR1 (PDB ID 2BFM), co-crystallized with NADP+, structure modeling, overview. Apart from salvianolic acid A (5), the most active inhibitors share structural features with certain similarities, such as engaging in Pi-Pi interactions with the nicotinamide moiety, namely, a flavone, a flavonol, a flavanone, or a four-chromanone system Leishmania major
myricetin
-
 Leishmania major
rosmarinic acid
-
 Leishmania major
salvianolic acid A
-
 Leishmania major
silybin A
-
 Leishmania major
silybin B
-
 Leishmania major
silychristin
-
 Leishmania major
sophoraflavanone G
-
 Leishmania major

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7,8-dihydrobiopterin + NADPH + H+ Leishmania major
-
 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Leishmania major Q01782
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7,8-dihydrobiopterin + NADPH + H+
-
 Leishmania major 5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
LmPTR1
-
 Leishmania major
pteridine reductase I
-
 Leishmania major
PTR1
-
 Leishmania major

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Leishmania major

General Information

General Information Comment Organism
additional information the substrate-binding domain of LmPTR1 is characterized by a considerable degree of lipophilicity, especially in a part mainly made up by hydrophobic amino acids like Tyr, Phe, Leu, or Val. The NADPH/NADP+-binding part of the catalytic site, on the other hand, is characterized by more hydrophilic amino acids and more polar properties overall. Due to the close vicinity of the co-substrate and substrate binding sites, the co-substrate NADPH/NADP+ may also contribute to the properties of the substrate cavity, introducing the possibility of polar interactions with a ligand bound in the folic acid binding site Leishmania major