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Literature summary for 1.5.1.33 extracted from

  • Shamshad, H.; Hafiz, A.; Althagafi, I.I.; Saeed, M.; Mirza, A.Z.
    Characterization of the Trypanosoma brucei pteridine reductase active-site using computational docking and virtual screening techniques (2020), Curr. Comput. aided Drug Des., 16, 583-598 .
    View publication on PubMed
Search for more literature for 1.5.1.33

Inhibitors

Inhibitors Comment Organism Structure
6,7-dihydroxyflavone
-
 Trypanosoma brucei brucei
baicalein
-
 Trypanosoma brucei brucei
additional information docking study, structure-function analysis, and drug design. The effects of several factors on docking accuracy, including ligand and protein flexibility, are analyzed Leishmania major
additional information docking study, structure-function analysis, and drug design. The effects of several factors on docking accuracy, including ligand and protein flexibility, are analyzed Trypanosoma brucei brucei
pelargonidin
-
 Trypanosoma brucei brucei
pinobanksin-3-o-acetate
-
 Trypanosoma brucei brucei
robinetinidin
-
 Trypanosoma brucei brucei

Organism

Organism UniProt Comment Textmining
Leishmania major Q01782
-
-
Trypanosoma brucei brucei O76290
-
-

Synonyms

Synonyms Comment Organism
LmPTR1
-
 Leishmania major
More cf. EC 1.5.1.3 Leishmania major
pteridine reductase 1
-
 Leishmania major
pteridine reductase 1
-
 Trypanosoma brucei brucei
PTR1
-
 Leishmania major
PTR1
-
 Trypanosoma brucei brucei
Tb-PR
-
 Leishmania major
Tb-PR
-
 Trypanosoma brucei brucei
TbPTR1
-
 Trypanosoma brucei brucei

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Leishmania major
NADPH
-
 Trypanosoma brucei brucei

General Information

General Information Comment Organism
additional information active-site structure analysis using computational docking and virtual screening techniques. Active site structure comparisons of Tb-PR (PDB ID 3JQ9) with Leishmania major pteridine reductase (Lm-PR). The size of substrate binding cleft is reduced in TbPTR1 due to differences in specific amino acids, the presence of Trp221, adjustment of the beta6-alpha6 loop. Formation of the triad is due to the presence of Cys168, C-terminal carboxyl group and His267 in TbPTR1, detailed overview Trypanosoma brucei brucei
additional information active-site structure analysis using computational docking and virtual screening techniques. Active site structure comparisons of Trypanosoma brucei pteridine reductase Tb-PR (PDB ID 3JQ9) with Lm-PR. The size of substrate binding cleft is reduced in TbPTR1 due to differences in specific amino acids, the presence of Trp221, adjustment of the beta6-alpha6 loop. Formation of the triad is due to the presence of Cys168, C-terminal carboxyl group and His267 in TbPTR1, detailed overview Leishmania major
physiological function the enzyme plays a critical role in the pterin metabolic pathway that is absolutely essential for the parasite's survival in the human host Leishmania major
physiological function the enzyme plays a critical role in the pterin metabolic pathway that is absolutely essential for the parasite's survival in the human host Trypanosoma brucei brucei