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Information on EC 5.1.1.4 - proline racemase
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5.1.1.4 proline racemaseSpecify your search results
Word Map
- 5.1.1.4
- trypanosoma
- cruzi
- d-proline
- chagas
-
oversaturated
- vivax
-
2-epimerase
- diaminopimelate
-
pyrrole-2-carboxylic
-
abeles
- medicine
-
pracs
-
trypanosomosis
-
stereoinversion
-
stickland
- congolense
- drug development
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
CdPRAC, CdProR, FaProR, HjProR, PA45-A, PA45-B, PRAC, PRAC1, PrdF, proline racemase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CdPRAC
HjProR
PA45-A
PA45-B
PRAC
PRAC1
proline racemase
proline racemase A
proline racemase B
proline racemase/hydroxyproline epimerase
ProR/HypE
Racemase, proline
-
-
-
-
TcPRAC
TcPRACA
TcPRACB
Tgr.146.1080
TryPRAC
TvPRAC
proline racemase/hydroxyproline epimerase
bifunctional enzyme
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-proline = D-proline
-
-
-
-
L-proline = D-proline
racemization is accompanied by deuterium incorporation from the solvent into the alpha position of Pro, participation of two equivalent hydrogen acceptor sites
-
L-proline = D-proline
two-base mechanism in which one base on the enzyme removes the substrate alpha-hydrogen as a proton and the conjugate acid of another base donates a proton to the opposite side of the alpha-carbon
-
L-proline = D-proline
energetics of proline racemase: transition-state fractionation factors for the two protons involved in the catalytic steps
-
L-proline = D-proline
stepwise reaction for the interconversion of the free enzyme forms in which a proton is abstracted from a bound water molecule to give a reaction intermediate having a hydroxide ion bound to the diprotonated form of the enzyme
-
L-proline = D-proline
enzyme exists in two states, one of which binds and isomerizes L-Pro and the other of which binds and isomerizes D-Pro. It seems likely that the two enzyme forms differ only in the protonation states of the acidic and basic groups at the active site
-
L-proline = D-proline
fractionation factors for the essential catalytic groups in the enzyme-substrate complexes
-
L-proline = D-proline
mechanism is best accomodated by a route that involves a transition state or unstable intermediate in which the proline carbanion is flanked by the two catalytic thiols of the enzyme
-
L-proline = D-proline
the substrate and product 'on-off' steps are faster than the racemization step and the racemization reaction proceeds either in a concerted manner or in a stepwise fashion involving enzyme catalytic groups, e.g. thiols
-
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; 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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
racemization
racemization
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
proline racemase
-
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CAS REGISTRY NUMBER
COMMENTARY
9024-09-3
-
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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
D-proline
L-proline
the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site
-
-
?
D-proline
L-proline
the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site
-
-
?
L-azetidine-2-carboxylate
D-azetidine-2-carboxylate
low activity
-
-
?
L-azetidine-2-carboxylate
D-azetidine-2-carboxylate
low activity
-
-
?
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
-
two-base racemization mechanism via an aci-carboxylate intermediate
-
-
r
L-proline
D-proline
CdPRAC from Clostridium difficile racemizes both L- and D-Pro but not OH-L/D-Pro or any other natural amino acid
-
-
r
L-proline
D-proline
CdPRAC from Clostridium difficile racemizes both L- and D-Pro but not OH-L/D-Pro or any other natural amino acid
-
-
r
L-proline
D-proline
kcat/Km value for trans-4-hydroxy-L-proline is about 3fold lower than that for L-proline, which is attributed to a 17fold lower kcat value. The kinetic parameters of the epimerization of cis-4-hydroxy-D-proline can not be determined
-
-
r
L-proline
D-proline
the enzyme can utilize both proline and hydroxyprolines as substrate
-
-
r
L-proline
D-proline
the enzyme can utilize both proline and hydroxyprolines as substrate
-
-
r
L-proline
D-proline
the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site
-
-
r
L-proline
D-proline
the reaction is completely bi-directional, and the reverse reactions. The specific activity with D-proline is 130% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site
-
-
r
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
?
-
TcPRACB: no reaction with L-hydroxyproline
-
?
additional information
?
-
TcPRACB: no reaction with L-hydroxyproline
-
?
additional information
?
-
-
TcPRACB: no reaction with L-hydroxyproline
-
?
additional information
?
-
-
a free and intact active site of the enzyme is necessary to allow mitogenicity
-
?
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
-
-
-
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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
-
-
?
additional information
?
-
-
a free and intact active site of the enzyme is necessary to allow mitogenicity
-
?
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme is not pyridoxal 5'-phosphate-dependent
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
7-azabicyclo[2.2.1]heptan-7-ium-1-carboxylate
-
a weak inhibitor of proline racemase, 29% inhibition at 142.5 mM
tetrahydro-1H-pyrrolizine-7a(5H)-carboxylate
-
a bicyclic substrate-product analogue and noncompetitive inhibitor of proline racemase
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
-
substrate-product analogue inhibitors of racemases may only be effective when the active site is capacious and/or plastic, or when the inhibitor is sufficiently flexible
-
additional information
-
synthesized soluble pyrazole derivatives prove to be weak or inactive TcPRAC inhibitors
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SH compounds
-
activate, e.g. 2-mercaptoethanol, 1,3-dimercaptoethanol
additional information
-
pyridoxal 5'-phosphate is not involved in racemization
-
additional information
-
addition of pyridoxal 5'-phosphate does not increase activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
46.7
(25R)-3beta-hydroxycholest-5-en-27-oate
substrate: D-proline, Vmax= 0.000017 M/sec
60.2
(25R)-3beta-hydroxycholest-5-en-27-oate
substrate: L-proline, Vmax = 0.000027 M/sec
106
D-proline
-
40 mM substrate in 0.2 M sodium acetate, for 30 min at 37°C
5.7
L-proline
-
pH and temperature not specified in the publication
145
L-proline
-
40 mM substrate in 0.2 M sodium acetate, for 30 min at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
111
tetrahydro-1H-pyrrolizine-7a(5H)-carboxylate
-
pH and temperature not specified in the publication
0.02
pyrrole-2-carboxylic acid
-
0.005 mM pyrrole-2-carboxylic acid, serial concentrations of 20-160 mM L-proline
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
349
1-carboxy-7-azoniabicyclo[2.2.1]heptane
Acetoanaerobium sticklandii
-
pH and temperature not specified in the publication
67
tetrahydro-1H-pyrrolizine-7a(5H)-carboxylate
Acetoanaerobium sticklandii
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.6 - 8.1
-
pH 5.5: no detectable activity, rapid fall of activity below pH 6.5, activity is relatively stable between pH 6.7 and 8.1
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
90 - 100
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
TcPRAC localizes in the cytoplasm of intracellular amastigote forms of the parasite, near the flagellar pocket of the parasites
brenda
-
membrane-bound and secreted forms of enzyme are present upon differentiation of the parasite into non-dividing infective forms
brenda
-
membrane-bound and secreted forms of enzyme are present upon differentiation of the parasite into non-dividing infective forms
-
brenda
-
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
-
brenda
-
in replicative non-infective forms of Trypanosoma cruzi
brenda
-
TcPRACB secretes the intracellular isoform of the enzyme. TcPRACA gene can generate both secreted and intracellular isoforms (by an alternative trans-splicing mechanism)
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
catalyzes step 8 in the ornithine fermentation pathway
physiological function
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
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
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; 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
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
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
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
evolution
A0A0F6VXM2
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
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
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
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
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
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
evolution
-
phylogenetic and syntenic data support a single horizontal transfer 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
evolution
Trypanosoma conorhini TCC025
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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
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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; 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
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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
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evolution
Trypanosoma dionisii TCC211
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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
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evolution
Trypanosoma erneyi TCC1946
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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
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evolution
Trypanosoma grayi ANR4
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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
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evolution
Trypanosoma lewisi TCC034
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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
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evolution
Trypanosoma serpentis TCC1052
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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
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evolution
Trypanosoma sp. TCC1825 / RCF-2014
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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
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evolution
Trypanosoma sp. TCC878 RCF-2014
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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
-
evolution
-
phylogenetic and syntenic data support a single horizontal transfer 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
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physiological function
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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; proline racemase participates in mechanisms of virulence acquisition
physiological function
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enzyme is a T-cell-independent B-cell mitogen, enzyme displays mitogenic activity towards splenic cells from euthymic Swiss mice, since addition of 0.1 mg/ml of recombinant protein promotes a 13fold increase of thymidine incorporation when compared with untreated cells, mitogenic activity of recombinant enzyme seems to be dependent on the active enzyme, since inhibition with 10 mM pyrrole-2-carboxylic acid prior to its incubation with splenocytes specifically decreases proliferation by 44%, enzyme triggers high levels of B-cell activation, terminal differentiation and antibody secretion
physiological function
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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
physiological function
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inactivation of proline racemase PrdF by insertional mutagenesis does not affect early logarithmic growth but only attenuates growth in the mid- and late logarithmic phases. There is no effect of inactivation on virulence in vivo
physiological function
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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
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Show AA Sequence and Transmembrane Helices (520 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Trypanosoma cruzi (strain CL Brener)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
45000
80000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
homodimer
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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
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R240W
mutant enzyme shows similar kinetic constants for proline and hydroxyproline as compared to the wild-type enzyme
W241F the mutant enzyme
C130S
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mutation of the catalytic Cys residues abolishes the enzymatic activity but preserves the mitogenic properties of the protein
C300S
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mutation of the catalytic Cys residues abolishes the enzymatic activity but preserves the mitogenic properties of the protein
additional information
W241F the mutant enzyme
shows 5.3fold, 430fold, and 5.8fold lower kcat/Km values for trans-4-hydroxy-L-proline, trans-3-hydroxy-L-proline, and cis-4-hydroxy-D-proline respectively, mainly due to a marked decrease in kcat values, whereas no significant effects are found in the kinetic constants of proline, suggesting that this (hydrophobic and bulky) tryptophan residue plays an importance role in the recognition of hydroxyproline (more hydrophilic and bulky than proline)
W241F the mutant enzyme
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shows 5.3fold, 430fold, and 5.8fold lower kcat/Km values for trans-4-hydroxy-L-proline, trans-3-hydroxy-L-proline, and cis-4-hydroxy-D-proline respectively, mainly due to a marked decrease in kcat values, whereas no significant effects are found in the kinetic constants of proline, suggesting that this (hydrophobic and bulky) tryptophan residue plays an importance role in the recognition of hydroxyproline (more hydrophilic and bulky than proline)
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additional information
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development of a Trypanosoma vivax specific PCR detection method based on the Trypanosoma vivax proline racemase (TvPRAC) gene. Forward and reverse primers are designed that bind at 764-783 bp and 983-1002 bp of the gene. To assess its specificity, TvPRAC PCR is conducted on DNA extracted from different haemotropic pathogens.Analysis of the analytical sensitivity of the different PCR methods, method evaluation, overview. Usage of Trypanosoma vivax isolates from bovine specimens from Nigeria, Ethiopia and Venezuela
additional information
Trypanosoma vivax ILRAD 1392
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development of a Trypanosoma vivax specific PCR detection method based on the Trypanosoma vivax proline racemase (TvPRAC) gene. Forward and reverse primers are designed that bind at 764-783 bp and 983-1002 bp of the gene. To assess its specificity, TvPRAC PCR is conducted on DNA extracted from different haemotropic pathogens.Analysis of the analytical sensitivity of the different PCR methods, method evaluation, overview. Usage of Trypanosoma vivax isolates from bovine specimens from Nigeria, Ethiopia and Venezuela
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% glycerol or diluted in sodium acetate buffer, pH 6.0, activity is impaired
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23°C, 0.5 M imidazole buffer, pH 8.0, 10 days, TcPRACA loses 84% of its activity
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23°C, 0.5 M imidazole buffer, pH 8.0, 10 days, TcPRACB is stable, TcPRACA loses 84% of its activity
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stored 6 months in the refrigerator without significant loss of activity
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography using nickel-nitrilotriacetic acid-agarose columns
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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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
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview; DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
DNA and amino acid sequence determination and analysis, sequence comparisons and sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
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expression in Escherichia coli
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
recombinant expression of His6-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; 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
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
-
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
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DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
A0A0F6VXM2
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, genotyping and genetic organization, detailed overview
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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
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
enzyme has potential to be used as a drug target for this parasite-based trypanosomiasis
medicine
medicine
-
potential of the enzyme as a critical target for drug development against Chaga‘s disease. The enzyme is absent in mammalian host, suggesting that inhibition of proline racemase may have therapeutic potential; 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
-
proline racemase based PCR can be used, preferably in combination with ITS-1 PCR, as a speciesspecific diagnostic test for Trypanosoma vivax infections worldwide
medicine
Trypanosoma vivax ILRAD 1392
-
proline racemase based PCR can be used, preferably in combination with ITS-1 PCR, as a speciesspecific diagnostic test for Trypanosoma vivax infections worldwide
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stadtman, T.C.; Elliott, P.
Studies on the enzymic reduction of amino acids. II. Purification and properties of a D-proline reductase and a proline racemase from Clostridium sticklandii
J. Biol. Chem.
228
983-997
1957
Acetoanaerobium sticklandii
brenda
Cardinale, G.J.; Abeles, R.H.
Purification and mechanism of action of proline racemase
Biochemistry
7
3970-3978
1968
Acetoanaerobium sticklandii
brenda
Keenan, M.V.; Alworth, W.L.
The inhibition of proline racemase by a transition state analogue: DELTA-1-pyrroline-2-carboxylate
Biochem. Biophys. Res. Commun.
57
500-504
1974
Acetoanaerobium sticklandii
brenda
Rudnick, G.; Abeles, R.H.
Reaction mechanism and structure of the active site of proline racemase
Biochemistry
14
4515-4522
1975
Acetoanaerobium sticklandii
brenda
Fisher, L.M.; Albery, W.J.; Knowles, J.R.
Energetics of proline racemase: racemization of unlabeled proline in the unsaturated, saturated and oversaturated regimes
Biochemistry
25
2529-2537
1986
Acetoanaerobium sticklandii
brenda
Fisher, L.M.; Belasco, J.G.; Bruice, T.W.; Albery, W.J.; Knowles, J.R.
Energetics of proline racemase: transition-state fractionation factors for the two protons involved in the catalytic steps
Biochemistry
25
2543-2551
1986
Acetoanaerobium sticklandii
brenda
Belasco, J.G.; Bruice, T.W.; Fisher, L.M.; Albery, W.J.; Knowles, J.R.
Energetics of proline racemase: rates, fractionation factors, and buffer catalysis in the oversaturated region. Nature of the interconversion of the two forms of free enzyme
Biochemistry
25
2564-2571
1986
Acetoanaerobium sticklandii
brenda
Fisher, L.M.; Albery, W.J.; Knowles, J.R.
Energetics of proline racemase: tracer perturbation experiments using [14C]proline that measure the interconversion rate of the two forms of free enzyme
Biochemistry
25
2538-2542
1986
Acetoanaerobium sticklandii
brenda
Belasco, J.G.; Bruice, T.W.; Albery, W.J.; Knowles, J.R.
Energetics of proline racemase: fractionation factors for the essential catalytic groups in the enzyme-substrate complexes
Biochemistry
25
2558-2564
1986
Acetoanaerobium sticklandii
brenda
Albery, W.J.; Knowles, J.R.
Energetics and mechanism of proline racemase
Biochemistry
25
2572-2577
1986
Acetoanaerobium sticklandii
brenda
Belasco, J.G.; Albery, W.J.; Knowles, J.R.
Energetics of proline racemase: double fractionation experiment, a test for concertedness and for transition-state dominance
Biochemistry
25
2552-2558
1986
Acetoanaerobium sticklandii
brenda
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
brenda
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
brenda
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
brenda
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 (Q4DA80), Trypanosoma cruzi
brenda
Goytia, M.; Chamond, N.; Cosson, A.; Coatnoan, N.; Hermant, D.; Berneman, A.; Minoprio, P.
Molecular and structural discrimination of proline racemase and hydroxyproline-2-epimerase from nosocomial and bacterial pathogens
PLoS ONE
2
e885
2007
Clostridioides difficile (A8DEZ8), Clostridioides difficile VPI10463 (A8DEZ8)
brenda
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
brenda
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
brenda
Fonknechten, N.; Perret, A.; Perchat, N.; Tricot, S.; Lechaplais, C.; Vallenet, D.; Vergne, C.; Zaparucha, A.; Le Paslier, D.; Weissenbach, J.; Salanoubat, M.
A conserved gene cluster rules anaerobic oxidative degradation of L-ornithine
J. Bacteriol.
191
3162-3167
2009
Acetoanaerobium sticklandii (Q9L4Q3)
brenda
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
brenda
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 (Q4D480), Trypanosoma cruzi (Q868H8), Trypanosoma cruzi
brenda
Chamond, N.; Cosson, A.; Coatnoan, N.; Minoprio, P.
Proline racemases are conserved mitogens: characterization of a Trypanosoma vivax proline racemase
Mol. Biochem. Parasitol.
165
170-179
2009
Trypanosoma vivax (B8LFE4), Trypanosoma vivax
brenda
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
brenda
Harty, M.; Nagar, M.; Atkinson, L.; Legay, C.M.; Derksen, D.J.; Bearne, S.L.
Inhibition of serine and proline racemases by substrate-product analogues
Bioorg. Med. Chem. Lett.
24
390-393
2014
Acetoanaerobium sticklandii
brenda
Wu, X.; Hurdle, J.G.
The Clostridium difficile proline racemase is not essential for early logarithmic growth and infection
Can. J. Microbiol.
60
251-254
2014
Clostridioides difficile
brenda
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
brenda
Watanabe, S.; Tanimoto, Y.; Nishiwaki, H.; Watanabe, Y.
Identification and characterization of bifunctional proline racemase/hydroxyproline epimerase from archaea: discrimination of substrates and molecular evolution
PLoS One
10
e0120349
2015
Clostridioides difficile (Q17ZY4), Ferroplasma acidarmanus (S0APF4), Haloarcula japonica (M0LMI3), Haloarcula japonica DSM 6131 (M0LMI3), Thermococcus litoralis (H3ZMH5), Thermococcus litoralis, Thermococcus litoralis DSM 5473 (H3ZMH5)
brenda
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)
brenda
Fikru, R.; Hagos, A.; Roge, S.; Reyna-Bello, A.; Gonzatti, M.I.; Merga, B.; Goddeeris, B.M.; Buescher, P.
A proline racemase based PCR for identification of Trypanosoma vivax in cattle blood
PLoS ONE
9
e84819
2014
Trypanosoma vivax (B8LFE4), Trypanosoma vivax, Trypanosoma vivax ILRAD 1392 (B8LFE4)
brenda
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