BRENDA - Enzyme Database show
show all sequences of 1.5.5.2

Proline dehydrogenase regulates redox state and respiratory metabolism in Trypanosoma cruzi

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.; PLoS ONE 8, e69419 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
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
Commentary
Organism
Structure
0.01658
-
L-proline
recombinant enzyme, pH 7.5, 37C, with 2,6-dichlorphenol-indophenol
Trypanosoma cruzi
Localization
Localization
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
Textmining
Trypanosoma cruzi
Q4CVA1
-
-
Trypanosoma cruzi CL Brener
Q4CVA1
-
-
Purification (Commentary)
Commentary
Organism
recombinant active His6-tagged enzyme from Escherichia coli strain BL21-CodonPlus (DE3) by nickel affinity chromatography
Trypanosoma cruzi
Source Tissue
Source Tissue
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-proline + 2,6-dichlorphenol-indophenol
-
743635
Trypanosoma cruzi
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
743635
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
743635
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
743635
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
743635
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
743635
Trypanosoma cruzi CL Brener
(S)-1-pyrroline-5-carboxylate + reduced cytochrome c
-
-
-
ir
L-proline + NAD+
NADP+ is a poor electron acceptor
743635
Trypanosoma cruzi
(S)-1-pyrroline-5-carboxylate + NADH
-
-
-
?
L-proline + NAD+
NADP+ is a poor electron acceptor
743635
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
743635
Trypanosoma cruzi
?
-
-
-
-
additional information
poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid
743635
Trypanosoma cruzi CL Brener
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
-
Trypanosoma cruzi
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
recombinant enzyme
Trypanosoma cruzi
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
recombinant enzyme
Trypanosoma cruzi
Cofactor
Cofactor
Commentary
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
Cloned(Commentary) (protein specific)
Commentary
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
Cofactor (protein specific)
Cofactor
Commentary
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
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01658
-
L-proline
recombinant enzyme, pH 7.5, 37C, with 2,6-dichlorphenol-indophenol
Trypanosoma cruzi
Localization (protein specific)
Localization
Commentary
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) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant active His6-tagged enzyme from Escherichia coli strain BL21-CodonPlus (DE3) by nickel affinity chromatography
Trypanosoma cruzi
Source Tissue (protein specific)
Source Tissue
Commentary
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) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-proline + 2,6-dichlorphenol-indophenol
-
743635
Trypanosoma cruzi
(S)-1-pyrroline-5-carboxylate + reduced 2,6-dichlorphenol-indophenol
-
-
-
?
L-proline + 2,6-dichlorphenol-indophenol
-
743635
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
743635
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
743635
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
743635
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
743635
Trypanosoma cruzi CL Brener
(S)-1-pyrroline-5-carboxylate + reduced cytochrome c
-
-
-
ir
L-proline + NAD+
NADP+ is a poor electron acceptor
743635
Trypanosoma cruzi
(S)-1-pyrroline-5-carboxylate + NADH
-
-
-
?
L-proline + NAD+
NADP+ is a poor electron acceptor
743635
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
743635
Trypanosoma cruzi
?
-
-
-
-
additional information
poor activity with D-proline, hydroxyproline, L-pipecolic acid, nicotinic acid, and thiazolidine-4-carboxylic acid
743635
Trypanosoma cruzi CL Brener
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
-
Trypanosoma cruzi
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
recombinant enzyme
Trypanosoma cruzi
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
recombinant enzyme
Trypanosoma cruzi
Expression
Organism
Commentary
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
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Expression (protein specific)
Organism
Commentary
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
Other publictions for EC 1.5.5.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743834
Huijbers
Proline dehydrogenase from Th ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Sci. Rep.
7
43880
2017
-
-
1
1
1
-
-
3
-
-
-
2
-
6
-
-
-
-
-
-
4
-
4
1
1
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3
1
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3
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1
3
1
1
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3
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2
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-
-
-
-
4
-
4
1
1
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-
3
1
-
-
-
-
-
-
-
3
3
741588
Hancock
Co-regulation of mitochondria ...
Homo sapiens, Mus musculus
Amino Acids
48
859-872
2016
-
-
2
-
1
-
12
-
2
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
2
-
-
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2
-
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2
-
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2
2
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1
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12
-
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2
-
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1
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-
-
2
-
-
-
2
-
-
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6
6
-
-
-
741858
Cabassa-Hourton
Proteomic and functional anal ...
Arabidopsis thaliana
Biochem. J.
473
2623-2634
2016
-
-
-
-
1
-
-
-
3
-
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-
5
-
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1
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1
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3
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1
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-
1
1
1
1
-
-
741642
Wang
Molecular cloning and express ...
Jatropha curcas
Appl. Biochem. Biotechnol.
175
2413-2426
2015
-
-
1
-
-
-
-
-
-
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4
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6
-
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2
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1
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1
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6
-
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2
-
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-
-
-
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-
1
1
2
2
1
-
-
742162
Huijbers
High yields of active Thermus ...
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Biotechnol. J.
10
395-403
2015
-
1
1
-
-
-
1
-
1
-
3
2
-
5
-
-
1
-
-
-
1
-
6
1
1
-
2
-
1
-
-
1
-
-
-
-
1
1
1
-
-
-
-
1
-
-
1
-
3
2
-
-
-
1
-
-
1
-
6
1
1
-
2
-
1
-
-
-
-
1
1
-
-
-
740734
Moxley
Evidence for hysteretic substr ...
Escherichia coli
J. Biol. Chem.
289
3639-3651
2014
-
-
-
-
-
-
-
3
-
-
-
-
-
2
-
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2
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1
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3
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2
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1
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-
-
3
3
742487
Schertl
Biochemical characterization ...
Arabidopsis thaliana
FEBS J.
281
2794-2804
2014
-
-
-
-
-
-
2
-
2
-
-
1
-
4
-
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-
-
-
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2
1
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2
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2
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2
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2
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1
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2
1
-
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-
-
-
-
1
2
2
1
-
-
724389
Serrano
Kinetic and isotopic character ...
Mycobacterium tuberculosis
Biochemistry
52
5009-5015
2013
-
-
-
-
2
-
-
3
-
-
1
-
-
2
-
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1
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1
1
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2
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1
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1
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2
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3
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1
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1
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1
1
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2
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2
2
741732
Kawakami
Comparative analysis of the c ...
Pyrococcus furiosus, Pyrococcus horikoshii, Pyrococcus horikoshii OT-3, Thermococcus kodakarensis, Thermococcus kodakarensis KOD1 JCM12380, Thermococcus profundus, Thermococcus profundus DSM 9503
Appl. Microbiol. Biotechnol.
97
3419-3427
2013
-
-
4
-
-
-
8
-
-
-
-
-
-
13
-
-
4
-
-
-
-
-
22
7
4
-
4
-
4
-
-
4
-
-
-
-
-
7
7
-
-
-
-
14
-
-
-
-
-
-
-
-
-
7
-
-
-
-
22
7
7
-
7
-
7
-
-
-
-
8
14
-
-
-
742641
Omidinia
Expression, purification and ...
Pseudomonas putida, Pseudomonas putida POS-F84
Indian J. Microbiol.
53
297-302
2013
-
-
1
-
1
-
-
-
-
-
-
-
-
5
-
-
1
-
-
-
-
-
2
2
1
1
-
-
1
1
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1
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1
1
-
1
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-
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-
1
-
-
-
-
2
2
1
1
-
-
1
1
-
-
-
1
1
-
-
-
743635
Paes
Proline dehydrogenase regulat ...
Trypanosoma cruzi, Trypanosoma cruzi CL Brener
PLoS ONE
8
e69419
2013
-
-
1
-
-
-
-
1
1
-
-
2
-
5
-
-
1
-
-
1
-
-
10
1
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
1
1
-
-
2
-
-
-
1
-
1
-
-
10
1
1
-
-
-
1
-
-
-
1
2
2
1
-
-
724345
Moxley
Rapid reaction kinetics of pro ...
Escherichia coli
Biochemistry
51
511-520
2012
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
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-
-
-
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1
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1
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1
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1
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1
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-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
739932
Kawakami
L-proline dehydrogenases in hy ...
Pyrococcus horikoshii
Appl. Microbiol. Biotechnol.
93
83-93
2012
-
-
-
-
-
-
-
1
-
-
3
1
-
5
-
-
-
-
-
-
1
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