EC Number | Cloned (Comment) | Organism |
---|---|---|
1.5.5.2 | gene Tc00.1047053506411.30, sequence comparisons, recombinant expression of the active His6-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3) cells, reverse transcription PCR (RT-PCR) and quantitative real-time PCR (qRT-PCR) expression analysis, functional complementation of ProDH-deficient, PUT1 mutant Saccharomyces cerevisiae strain YLR142W. TcPRODH gene expression in the mutant diminishes free intracellular proline levels and an enhances sensitivity to oxidative stress | Trypanosoma cruzi |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.5.2 | 0.01658 | - |
L-proline | recombinant enzyme, pH 7.5, 37°C, with 2,6-dichlorphenol-indophenol | Trypanosoma cruzi |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.5.5.2 | mitochondrial inner membrane | TcPRODH is associated with the mitochondrial inner membrane, identification of a predicted N-terminal mitochondrial targeting signal, followed by a putative transmembrane alpha helix spanning domain | Trypanosoma cruzi | 5743 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.5.2 | L-proline + a quinone | Trypanosoma cruzi | the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2 | (S)-1-pyrroline-5-carboxylate + a quinol | - |
ir | |
1.5.5.2 | L-proline + a quinone | Trypanosoma cruzi CL Brener | the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2 | (S)-1-pyrroline-5-carboxylate + a quinol | - |
ir |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.5.2 | Trypanosoma cruzi | Q4CVA1 | - |
- |
1.5.5.2 | Trypanosoma cruzi CL Brener | Q4CVA1 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.5.5.2 | recombinant active His6-tagged enzyme from Escherichia coli strain BL21-CodonPlus (DE3) by nickel affinity chromatography | Trypanosoma cruzi |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.5.5.2 | epimastigote | TcPRODH mRNA and protein expression are strongly upregulated in the intracellular epimastigote, a stage which requires an external supply of proline | Trypanosoma cruzi | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.5.2 | L-proline + 2,6-dichlorphenol-indophenol | - |
Trypanosoma cruzi | (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol | - |
? | |
1.5.5.2 | L-proline + 2,6-dichlorphenol-indophenol | - |
Trypanosoma cruzi CL Brener | (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol | - |
? | |
1.5.5.2 | L-proline + a quinone | the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2 | Trypanosoma cruzi | (S)-1-pyrroline-5-carboxylate + a quinol | - |
ir | |
1.5.5.2 | L-proline + a quinone | the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2 | Trypanosoma cruzi CL Brener | (S)-1-pyrroline-5-carboxylate + a quinol | - |
ir | |
1.5.5.2 | L-proline + cytochrome c | the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2 | Trypanosoma cruzi | (S)-1-pyrroline-5-carboxylate + reduced cytochrome c | - |
ir | |
1.5.5.2 | L-proline + cytochrome c | the reverse reaction is catalyzed by pyrroline-5-carboxylate reductase, EC 1.5.1.2 | Trypanosoma cruzi CL Brener | (S)-1-pyrroline-5-carboxylate + reduced cytochrome c | - |
ir | |
1.5.5.2 | L-proline + NAD+ | NADP+ is a poor electron acceptor | Trypanosoma cruzi | (S)-1-pyrroline-5-carboxylate + NADH | - |
? | |
1.5.5.2 | L-proline + NAD+ | NADP+ is a poor electron acceptor | Trypanosoma cruzi CL Brener | (S)-1-pyrroline-5-carboxylate + NADH | - |
? | |
1.5.5.2 | additional information | poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid | Trypanosoma cruzi | ? | - |
? | |
1.5.5.2 | additional information | poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid | Trypanosoma cruzi CL Brener | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.5.5.2 | dimer | - |
Trypanosoma cruzi |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.5.5.2 | FAD-dependent L-proline oxidoreductase | - |
Trypanosoma cruzi |
1.5.5.2 | PRODH | - |
Trypanosoma cruzi |
1.5.5.2 | Tc00.1047053506411.30 | - |
Trypanosoma cruzi |
1.5.5.2 | TcPRODH | - |
Trypanosoma cruzi |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.5.5.2 | 37 | - |
recombinant enzyme | Trypanosoma cruzi |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.5.5.2 | 7.5 | - |
recombinant enzyme | Trypanosoma cruzi |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.5.5.2 | cytochrome c | - |
Trypanosoma cruzi | |
1.5.5.2 | FAD | TcPRODH is a FAD-dependent protein, key residues involved in cofactor (FAD) binding are Arg431 and Glu559 | Trypanosoma cruzi |
EC Number | Organism | Comment | Expression |
---|---|---|---|
1.5.5.2 | Trypanosoma cruzi | TcPRODH mRNA and protein expression are strongly upregulated in the intracellular epimastigote, a stage which requires an external supply of proline | up |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.5.5.2 | additional information | key residues involved in substrate binding are Asp370, Tyr 540, Arg555, Arg556, and Leu513 | Trypanosoma cruzi |
1.5.5.2 | physiological function | in trypanosomatids, L-proline is involved in a number of key processes, including energy metabolism, resistance to oxidative and nutritional stress and osmoregulation. In addition, this amino acid supports critical parasite life cycle processes by acting as an energy source, thus enabling host-cell invasion by the parasite and subsequent parasite differentiation. Proline dehydrogenase regulates redox state and respiratory metabolism in Trypanosoma cruzi, free proline accumulation constitutes a defense against oxidative imbalance | Trypanosoma cruzi |