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Information on EC 5.1.1.4 - proline racemase and Organism(s) Trypanosoma cruzi and UniProt Accession Q4DA80
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5.1.1.4 proline racemaseSpecify your search results
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- 5.1.1.4
- trypanosoma
- cruzi
- d-proline
- chagas
-
oversaturated
- diaminopimelate
-
2-epimerase
-
pyrrole-2-carboxylic
-
stickland
- medicine
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abeles
-
trypanosomosis
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stereoinversion
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pracs
- lumazine
- drug development
The taxonomic range for the selected organisms is: Trypanosoma cruzi
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
proline racemase, tcprac, tvprac, prac1, tryprac, tcpraca, tcpracb, proline racemase a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
TcPRACA
PRAC
proline racemase
Racemase, proline
-
-
-
-
TcPRAC
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-proline = D-proline
a new combined quantum mechanical and molecular mechanical (QM/MM) potential to study the reaction mechanism of proline racemase is used. Three critical points are identified: two almost isoenergetic minima (M1a and M2a), in which the enzyme is bound to L- and D-Pro, respectively, and a transition state (TSCa), unveiling a highly asynchronous concerted process
L-proline = D-proline
quantum mechanical and molecular mechanical study reveals two almost isoenergetic minima M1a and M2a, in which the enzyme is bound to L-proline and D-proline, respectively, and a transition state TSCa, unveiling a highly asynchronous concerted process. Residues Asn133, Asp296, and Gly301 destabilize M2a. Conversely, both Gly131and Gly303 stabilize M2a. Residues Gly131, Gly301, and Thr302 stabilize TSCa
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
racemization
racemization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
proline racemase
-
CAS REGISTRY NUMBER
COMMENTARY
9024-09-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Pro
D-Pro
overexpression of TcPRAC leads to an increase in parasite differentiation into infective forms and its subsequent penetration into host cells. During infection of its mammalian host, the parasite secretes a proline racemase that contributes to parasite immune evasion by acting as a B-cell mitogen
-
-
?
L-proline
D-proline
-
the simplest mechanism for ProR isomerization of L-Pro to D-Pro entails the Cys130/Cys300 dyad in the thiolate/thiol forms, respectively, while His132 and Asp296 are in their neutral and carboxylate forms, in this scheme Cys130 is deprotonated either by a water molecule or an initially neutral form of the amine moiety of the substrate, thus, His132 and Asp296 do not serve a catalytic acid-base role in the racemization step but interact tightly with the ammonium moiety of the substrate, the ProR catalytic cycle involves 2 proton-transfer reactions in either direction of the racemization
-
-
r
additional information
?
-
a free and intact active site of the enzyme is necessary to allow mitogenicity
-
?
additional information
?
-
-
a free and intact active site of the enzyme is necessary to allow mitogenicity
-
?
additional information
?
-
TcPRACB: no reaction with L-hydroxyproline
-
?
additional information
?
-
TcPRACB: no reaction with L-hydroxyproline
-
?
additional information
?
-
-
TcPRACB: no reaction with L-hydroxyproline
-
?
additional information
?
-
-
quantum mechanical and molecular mechanical study reveals two almost isoenergetic minima M1a and M2a, in which the enzyme is bound to L-proline and D-proline, respectively, and a transition state TSCa, unveiling a highly asynchronous concerted process. Residues Asn133, Asp296, and Gly301 destabilize M2a. Conversely, both Gly131 and Gly303 stabilize M2a. Residues Gly131, Gly301, and Thr302 stabilize TSCa
-
-
?
additional information
?
-
quantum mechanical and molecular mechanical study reveals two almost isoenergetic minima M1a and M2a, in which the enzyme is bound to L-proline and D-proline, respectively, and a transition state TSCa, unveiling a highly asynchronous concerted process. Residues Asn133, Asp296, and Gly301 destabilize M2a. Conversely, both Gly131 and Gly303 stabilize M2a. Residues Gly131, Gly301, and Thr302 stabilize TSCa
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Pro
D-Pro
overexpression of TcPRAC leads to an increase in parasite differentiation into infective forms and its subsequent penetration into host cells. During infection of its mammalian host, the parasite secretes a proline racemase that contributes to parasite immune evasion by acting as a B-cell mitogen
-
-
?
L-proline
D-proline
-
the simplest mechanism for ProR isomerization of L-Pro to D-Pro entails the Cys130/Cys300 dyad in the thiolate/thiol forms, respectively, while His132 and Asp296 are in their neutral and carboxylate forms, in this scheme Cys130 is deprotonated either by a water molecule or an initially neutral form of the amine moiety of the substrate, thus, His132 and Asp296 do not serve a catalytic acid-base role in the racemization step but interact tightly with the ammonium moiety of the substrate, the ProR catalytic cycle involves 2 proton-transfer reactions in either direction of the racemization
-
-
r
additional information
?
-
a free and intact active site of the enzyme is necessary to allow mitogenicity
-
?
additional information
?
-
-
a free and intact active site of the enzyme is necessary to allow mitogenicity
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(E)-4-oxopent-2-enoic acid
-
an irreversible strong competitive inhibitor, which hampers Trypanosoma cruzi intracellular differentiation and fate in mammalian host cells
(E)-5-bromo-4-oxopent-2-enoic acid
-
an irreversible strong competitive inhibitor, which hampers Trypanosoma cruzi intracellular differentiation and fate in mammalian host cells
pyrrole-2-carboxylic acid
-
inhibitor significantly affects parasite infection of Vero cells in vitro, inhibitor also hampers Trypanosoma cruzi intracellular differentiation, inhibitor reduces host cell invasion in Vero cells by Trypanososma cruzi in a dose-dependent manner, pre-treatment of the parasites with 1 mM of inhibitor does not lead to changes in their morphology and motility, but results in an up to 54% reduction in the percentage of parasitized cells and about 30% less parasites per cell when cultures are counted at day 4 after infection
additional information
-
synthesized soluble pyrazole derivatives prove to be weak or inactive TcPRAC inhibitors
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006 - 0.01
2-pyrrolecarboxylic acid
-
recombinant His-tagged enzyme, pH 6.0, 37°C
1
4-bromopyrazole-3-carboxylic acid
-
recombinant His-tagged enzyme, pH 6.0, 37°C
2
4-chloro-5-methyl-pyrazole-3-carboxylic acid
-
recombinant His-tagged enzyme, pH 6.0, 37°C
0.3
4-chloropyrazole-3-carboxylic acid
-
recombinant His-tagged enzyme, pH 6.0, 37°C
2
4-ethylpyrazole-3-carboxylic acid
-
recombinant His-tagged enzyme, pH 6.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
TcPRACB secretes the intracellular isoform of the enzyme. TcPRACA gene can generate both secreted and intracellular isoforms (by an alternative trans-splicing mechanism)
membrane-bound and secreted forms of enzyme are present upon differentiation of the parasite into non-dividing infective forms
-
TcPRAC localizes in the cytoplasm of intracellular amastigote forms of the parasite, near the flagellar pocket of the parasites
in replicative non-infective forms of Trypanosoma cruzi
membrane-bound and secreted forms of enzyme are present upon differentiation of the parasite into non-dividing infective forms
-
during infection of its mammalian host, the parasite secretes a proline racemase that contributes to parasite immune evasion by acting as a B-cell mitogen
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
phylogenetic and syntenic data support a single horizontal transference to a Trypanosoma ancestor of a prokaryotic proline racemase implicated in parasite evasion from host defences. TryPRAC homologues as single copy genes per haploid genome in 12 of 15 Trypanosoma species, including Trypanosoma cruzi and Trypanosoma cruzi marinkellei, Trypanosoma dionisii, Trypanosoma erneyi, Trypanosoma rangeli, Trypanosoma conorhini and Trypanosoma lewisi, all parasites of mammals. Polymorphisms in TcPRAC genes match Trypanosoma cruzi genotypes: TcI-TcIV and Tcbat have unique genes, while the hybrids TcV and TcVI contain TcPRACA and TcPRACB from parental TcII and TcIII, respectively. PRAC homologues are identified in trypanosomes from anurans, snakes, crocodiles, lizards, and birds. Most trypanosomes have intact PRAC genes. Trypanosoma rangeli possesses only pseudogenes, maybe in the process of being lost. Trypanosoma brucei, Trypanosoma congolense and their allied species, except the more distantly related Trypanosoma vivax, have completely lost PRAC genes. The genealogy of TryPRAC homologs supports an evolutionary history congruent with the Trypanosoma phylogeny
physiological function
proline racemase participates in mechanisms of virulence acquisition
evolution
phylogenetic and syntenic data support a single horizontal transference to a Trypanosoma ancestor of a prokaryotic proline racemase implicated in parasite evasion from host defences. TryPRAC homologues as single copy genes per haploid genome in 12 of 15 Trypanosoma species, including Trypanosoma cruzi and Trypanosoma cruzi marinkellei, Trypanosoma dionisii, Trypanosoma erneyi, Trypanosoma rangeli, Trypanosoma conorhini and Trypanosoma lewisi, all parasites of mammals. Polymorphisms in TcPRAC genes match Trypanosoma cruzi genotypes: TcI-TcIV and Tcbat have unique genes, while the hybrids TcV and TcVI contain TcPRACA and TcPRACB from parental TcII and TcIII, respectively. PRAC homologues are identified in trypanosomes from anurans, snakes, crocodiles, lizards, and birds. Most trypanosomes have intact PRAC genes. Trypanosoma rangeli possesses only pseudogenes, maybe in the process of being lost. Trypanosoma brucei, Trypanosoma congolense and their allied species, except the more distantly related Trypanosoma vivax, have completely lost PRAC genes. The genealogy of TryPRAC homologs supports an evolutionary history congruent with the Trypanosoma phylogeny
physiological function
physiological function
-
proline racemase is an effective mitogen for B cells, thus contributing to the parasites immune evasion and persistence in the human host
physiological function
proline racemase participates in mechanisms of virulence acquisition
physiological function
-
proline racemase is a T-cell-independent B-cell mitogen, stimulation of murine splenocytes with recombinant proline racemase C induces B-cell proliferation, antibody secretion, interleukin-10 production, and upregulation of CD69 and CD86 on B cells
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homodimer
homodimer
-
enzyme comprises of 2 alpha/beta units containing 414 amino acids which are separated by a deep cleft. Each monomer possesses an independent active site pocket, which is sequestered from water
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
best crystals are obtained by mixing 2-3 microliter of the protein solution with an equal volume of crystallization buffer (0.1 M ammonium acetate/50 mM tri-sodium citrate dihydrate, pH 5.6/15% w/v polyethylene glycol 4000), equilibrated over 1 ml of the same buffer
crystal structure analysis shows that TcPRACA is a homodimer, with each monomer folded in two symmetric alpha/beta subunits separated by a deep crevice. The structure of TcPRACA in complex with a transition-state analog, pyrrole-2-carboxylic acid, reveals the presence of one reaction center per monomer, with two Cys residues optimally located to perform acid/base catalysis through a carbanion stabilization mechanism
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C130S
mutation of the catalytic Cys residues abolishes the enzymatic activity but preserves the mitogenic properties of the protein
C300S
mutation of the catalytic Cys residues abolishes the enzymatic activity but preserves the mitogenic properties of the protein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% glycerol or diluted in sodium acetate buffer, pH 6.0, activity is impaired
23°C, 0.5 M imidazole buffer, pH 8.0, 10 days, TcPRACA loses 84% of its activity
-20°C, 50% glycerol or diluted in sodium acetate buffer, pH 6.0, stable
23°C, 0.5 M imidazole buffer, pH 8.0, 10 days, TcPRACB is stable, TcPRACA loses 84% of its activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TcPRACA protein is purified with immobilized metal affinity chromatography on nickel columns. The active peak is further submitted to gel filtration chromatography at 2.5 ml/min in a Superdex200 26/60 column
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
the paralogous genes TcPRACA (A+) and TcPRACB (B++) are overexpressed in non-infective epimastigote forms using appropriate vectors to obtain stable chromosomal integration of these genes in sense and antisense orientations
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
the paralogous genes TcPRACA (A+) and TcPRACB (B++) are overexpressed in non-infective epimastigote forms using appropriate vectors to obtain stable chromosomal integration of these genes in sense and antisense orientations
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
2 paralogous copies of proline racemase genes are present per parasite haploid genome and they are differentially expressed during Trypanosoma cruzi development. Non-infective forms of the parasite expressing full length antisense TcPRACB RNA (functional knockdown) are not viable, whereas functional TcPRACA-knock down (A-) epimastigotes survive only poorly even under low selection pressure for recombinant parasites. Extracts from parasites overexpressing TcPRAC genes display more D-amino acid-containing peptides than wild type or knock down controls. The metacyclic form/epimastigote D-amino acid ratio obtained from parasites that developed in higher concentrations of proline (5.5) is greater than the metacyclic form/epimastigote D-amino acid ratio from wild type (2). Parasites overexpressing the intracytoplasmic isoform of proline racemase (B++) that has differentiated in 1x or 3x proline conditions display higher metacyclic form/epimastigote D-amino acid ratios than the respective wild type controls. Although they present a relative increase in metacyclic form/epimastigote D-amino acid ratios, overexpressors of the secreted version of TcPRAC (A+) show lower levels of D-amino acids than wild type or B++ parasites. Since TcPRACA transcripts appear to be more highly expressed at the end of metacyclogenesis, it is tempting to consider that racemisation of intracellular proline during this stage of development instead depends on the cytoplasmic version of the enzyme (TcPRACB)
2 paralogous copies of proline racemase genes are present per parasite haploid genome and they are differentially expressed during Trypanosoma cruzi development. Non-infective forms of the parasite expressing full length antisense TcPRACB RNA (functional knockdown) are not viable, whereas functional TcPRACA-knock down (A-) epimastigotes survive only poorly even under low selection pressure for recombinant parasites. Extracts from parasites overexpressing TcPRAC genes display more D-amino acid-containing peptides than wild type or knock down controls. The metacyclic form/epimastigote D-amino acid ratio obtained from parasites that developed in higher concentrations of proline (5.5) is greater than the metacyclic form/epimastigote D-amino acid ratio from wild type (2). Parasites overexpressing the intracytoplasmic isoform of proline racemase (B++) that has differentiated in 1x or 3x proline conditions display higher metacyclic form/epimastigote D-amino acid ratios than the respective wild type controls. Although they present a relative increase in metacyclic form/epimastigote D-amino acid ratios, overexpressors of the secreted version of TcPRAC (A+) show lower levels of D-amino acids than wild type or B++ parasites. Since TcPRACA transcripts appear to be more highly expressed at the end of metacyclogenesis, it is tempting to consider that racemisation of intracellular proline during this stage of development instead depends on the cytoplasmic version of the enzyme (TcPRACB)
in amastigote forms of the parasites, the intensity of anti-TcPRAC labeling varies according to the time post infection reaching the highest signal of TcPRAC expression after 48 h, while the number of intracellular parasites increases by amastigote multiplication
-
recombinant epimastigote parasites overexpressing TcPRAC genes coding for proline racemase present an augmented ability to differentiate into metacyclic infective forms and subsequently penetrate host-cells in vitro
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
potential of the enzyme as a critical target for drug development against Chagas disease. The enzyme is absent in mammalian host, suggesting that inhibition of proline racemase may have therapeutic potential
medicine
potential of the enzyme as a critical target for drug development against Chagas disease. The enzyme is absent in mammalian host, suggesting that inhibition of proline racemase may have therapeutic potential
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chamond, N.; Gregoire, C.; Coatnoan, N.; Rougeot, C.; Freitas-Junior, L.H.; da Silveira, J.F.; Degrave, W.M.; Minoprio, P.
Biochemical characterization of proline racemases from the human protozoan parasite Trypanosoma cruzi and definition of putative protein signatures
J. Biol. Chem.
278
15484-15494
2003
Trypanosoma cruzi (Q4DA80), Trypanosoma cruzi (Q868H8), Trypanosoma cruzi
Reina-San-Martin, B.; Degrave, W.; Rougeot, C.; Cosson, A.; Chamond, N.; Cordeiro-Da-Silva, A.; Arala-Chaves, M.; Coutinho, A.; Minoprio, P.
A B-cell mitogen from a pathogenic trypanosome is a eukaryotic proline racemase
Nat. Med.
6
890-897
2000
Trypanosoma cruzi (Q4DA80), Trypanosoma cruzi
Chamond, N.; Goytia, M.; Coatnoan, N.; Barale, J.C.; Cosson, A.; Degrave, W.M.; Minoprio, P.
Trypanosoma cruzi proline racemases are involved in parasite differentiation and infectivity
Mol. Microbiol.
58
46-60
2005
Trypanosoma cruzi (Q4DA80), Trypanosoma cruzi
Stenta, M.; Calvaresi, M.; Altoe, P.; Spinelli, D.; Garavelli, M.; Bottoni, A.
The Catalytic Activity of Proline Racemase: A Quantum Mechanical/Molecular Mechanical Study
J. Phys. Chem. B
112
1057-1059
2008
Trypanosoma cruzi, Trypanosoma cruzi (Q4DA80)
Buschiazzo, A.; Goytia, M.; Schaeffer, F.; Degrave, W.; Shepard, W.; Gregoire, C.; Chamond, N.; Cosson, A.; Berneman, A.; Coatnoan, N.; Alzari, P.M.; Minoprio, P.
Crystal structure, catalytic mechanism, and mitogenic properties of Trypanosoma cruzi proline racemase
Proc. Natl. Acad. Sci. USA
103
1705-1710
2006
Trypanosoma cruzi (Q4DA80), Trypanosoma cruzi
Rubinstein, A.; Major, D.T.
Catalyzing racemizations in the absence of a cofactor: the reaction mechanism in proline racemase
J. Am. Chem. Soc.
131
8513-8521
2009
Trypanosoma cruzi
Coutinho, L.; Ferreira, M.A.; Cosson, A.; Batista, M.M.; Batista, D.d.a..G.; Minoprio, P.; Degrave, W.M.; Berneman, A.; Soeiro Mde, N.
Inhibition of Trypanosoma cruzi proline racemase affects host-parasite interactions and the outcome of in vitro infection
Mem. Inst. Oswaldo Cruz
104
1055-1062
2009
Trypanosoma cruzi
Coatnoan, N.; Berneman, A.; Chamond, N.; Minoprio, P.
Proline racemases: Insights into Trypanosoma cruzi peptides containing D-proline
Mem. Inst. Oswaldo Cruz
104
295-300
2009
Trypanosoma cruzi (Q4DA80), Trypanosoma cruzi (Q868H8), Trypanosoma cruzi
Bryan, M.; Norris, K.
Genetic immunization converts the Trypanosoma cruzi B-cell mitogen proline racemase to an effective immunogen
Infect. Immun.
78
810-822
2010
Trypanosoma cruzi, Trypanosoma cruzi Y
Berneman, A.; Montout, L.; Goyard, S.; Chamond, N.; Cosson, A.; dArchivio, S.; Gouault, N.; Uriac, P.; Blondel, A.; Minoprio, P.
Combined approaches for drug design points the way to novel proline racemase inhibitor candidates to fight Chagas disease
PLoS ONE
8
e60955
2013
Trypanosoma cruzi
Caballero, Z.C.; Costa-Martins, A.G.; Ferreira, R.C.; P Alves, J.M.; Serrano, M.G.; Camargo, E.P.; Buck, G.A.; Minoprio, P.; G Teixeira, M.M.
Phylogenetic and syntenic data support a single horizontal transference to a Trypanosoma ancestor of a prokaryotic proline racemase implicated in parasite evasion from host defences
Parasit. Vectors
8
222
2015
no activity in Trypanosoma brucei, no activity in Trypanosoma congolense, Trypanosoma conorhini (A0A0F6YF18), Trypanosoma conorhini, Trypanosoma conorhini TCC025 (A0A0F6YF18), Trypanosoma cruzi (Q4DA80), Trypanosoma cruzi (Q868H8), Trypanosoma cruzi, Trypanosoma cruzi CL Brener (Q4DA80), Trypanosoma cruzi CL Brener (Q868H8), Trypanosoma cruzi marinkellei (A0A0F6VXD6), Trypanosoma cruzi marinkellei TCC344 (A0A0F6VXD6), Trypanosoma dionisii, Trypanosoma dionisii TCC211, Trypanosoma erneyi (A0A0F6VXE2), Trypanosoma erneyi TCC1946 (A0A0F6VXE2), Trypanosoma grayi, Trypanosoma grayi ANR4, Trypanosoma lewisi (A0A0F6VXM2), Trypanosoma lewisi, Trypanosoma lewisi TCC034 (A0A0F6VXM2), Trypanosoma rangeli, Trypanosoma serpentis (A0A0F6SCP6), Trypanosoma serpentis TCC1052 (A0A0F6SCP6), Trypanosoma sp. (A0A0F6VXD9), Trypanosoma sp. TCC1825 / RCF-2014 (A0A0F6VXD9), Trypanosoma sp. TCC339 (A0A0F6YER1), Trypanosoma sp. TCC878 (A0A0F6VXE6), Trypanosoma sp. TCC878 RCF-2014 (A0A0F6VXE6), Trypanosoma vivax (B8LFE4), Trypanosoma vivax, Trypanosoma vivax Y486 (B8LFE4)
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