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Literature summary for 1.5.5.2 extracted from

  • Paes, L.S.; Suarez Mantilla, B.; Zimbres, F.M.; Pral, E.M.; Diogo de Melo, P.; Tahara, E.B.; Kowaltowski, A.J.; Elias, M.C.; Silber, A.M.
    Proline dehydrogenase regulates redox state and respiratory metabolism in Trypanosoma cruzi (2013), PLoS ONE, 8, e69419 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.5.5.2

Cloned(Commentary)

Cloned (Comment) Organism
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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01658
-
 L-proline recombinant enzyme, pH 7.5, 37°C, with 2,6-dichlorphenol-indophenol Trypanosoma cruzi

Localization

Localization Comment Organism GeneOntology No. Textmining
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
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
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

Organism

Organism UniProt Comment Textmining
Trypanosoma cruzi Q4CVA1
-
-
Trypanosoma cruzi CL Brener Q4CVA1
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant active His6-tagged enzyme from Escherichia coli strain BL21-CodonPlus (DE3) by nickel affinity chromatography Trypanosoma cruzi

Source Tissue

Source Tissue Comment Organism Textmining
epimastigote TcPRODH mRNA and protein expression are strongly upregulated in the intracellular epimastigote, a stage which requires an external supply of proline Trypanosoma cruzi
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-proline + 2,6-dichlorphenol-indophenol
-
 Trypanosoma cruzi (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
 ?
L-proline + 2,6-dichlorphenol-indophenol
-
 Trypanosoma cruzi CL Brener (S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
 ?
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
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
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
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
L-proline + NAD+ NADP+ is a poor electron acceptor Trypanosoma cruzi (S)-1-pyrroline-5-carboxylate + NADH
-
 ?
L-proline + NAD+ NADP+ is a poor electron acceptor Trypanosoma cruzi CL Brener (S)-1-pyrroline-5-carboxylate + NADH
-
 ?
additional information poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid Trypanosoma cruzi ?
-
 ?
additional information poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid Trypanosoma cruzi CL Brener ?
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Trypanosoma cruzi

Synonyms

Synonyms Comment Organism
FAD-dependent L-proline oxidoreductase
-
 Trypanosoma cruzi
PRODH
-
 Trypanosoma cruzi
Tc00.1047053506411.30
-
 Trypanosoma cruzi
TcPRODH
-
 Trypanosoma cruzi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 recombinant enzyme Trypanosoma cruzi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 recombinant enzyme Trypanosoma cruzi

Cofactor

Cofactor Comment Organism Structure
cytochrome c
-
 Trypanosoma cruzi
FAD TcPRODH is a FAD-dependent protein, key residues involved in cofactor (FAD) binding are Arg431 and Glu559 Trypanosoma cruzi

Expression

Organism Comment Expression
Trypanosoma cruzi TcPRODH mRNA and protein expression are strongly upregulated in the intracellular epimastigote, a stage which requires an external supply of proline up

General Information

General Information Comment Organism
additional information key residues involved in substrate binding are Asp370, Tyr 540, Arg555, Arg556, and Leu513 Trypanosoma cruzi
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