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Literature summary extracted from

  • Marchese, L.; Olavarria, K.; Mantilla, B.S.; Avila, C.C.; Souza, R.O.O.; Damasceno, F.S.; Elias, M.C.; Silber, A.M.
    Trypanosoma cruzi synthesizes proline via a delta1-pyrroline-5-carboxylate reductase whose activity is fine-tuned by NADPH cytosolic pools (2020), Biochem. J., 477, 1827-1845 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.2 NADPH substrate inhibition Trypanosoma cruzi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.2 0.0128
-
 NADPH pH 7, 28°C Trypanosoma cruzi
1.5.1.2 0.0277
-
 1-pyrroline-5-carboxylate pH 7, 28°C Trypanosoma cruzi

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.5.1.2 cytosol
-
 Trypanosoma cruzi 5829
-

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.2 Trypanosoma cruzi Q4DH60
-
-
1.5.1.2 Trypanosoma cruzi CL Brener Q4DH60
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.2 1-pyrroline-5-carboxylate + NADPH + H+
-
 Trypanosoma cruzi L-proline + NADP+
-
 ?
1.5.1.2 1-pyrroline-5-carboxylate + NADPH + H+
-
 Trypanosoma cruzi CL Brener L-proline + NADP+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.5.1.2 P5CR
-
 Trypanosoma cruzi
1.5.1.2 TcCLB.509207.90
-
 Trypanosoma cruzi

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.1.2 1
-
 1-pyrroline-5-carboxylate pH 7, 28°C Trypanosoma cruzi
1.5.1.2 1.99
-
 NADPH pH 7, 28°C Trypanosoma cruzi

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.5.1.2 0.045
-
 pH 7, 28°C Trypanosoma cruzi NADPH

General Information

EC Number General Information Comment Organism
1.5.1.2 physiological function Trypanosoma cruzi biosynthesizes proline from 1-pyrroline-5-carboxylate, which is produced exclusively from glutamate. P5CR shows a higher expression in the insect-resident form of the parasite. The model that best explains the obtained data includes a non-competitive substrate inhibition mechanism Trypanosoma cruzi