Information on EC 5.1.1.4 - Proline racemase

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The expected taxonomic range for this enzyme is: Trypanosoma

EC NUMBER
COMMENTARY
5.1.1.4
-
RECOMMENDED NAME
GeneOntology No.
Proline racemase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-proline = D-proline
show the reaction diagram
-
-
-
-
L-proline = D-proline
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
mechanism
-
L-proline = D-proline
show the reaction diagram
energetics of proline racemase: transition-state fractionation factors for the two protons involved in the catalytic steps
-
L-proline = D-proline
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
fractionation factors for the essential catalytic groups in the enzyme-substrate complexes
-
L-proline = D-proline
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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 ACCESSION NO.
COMMENTARY
LITERATURE
isomerization
-
-
racemization
-
-
-
-
racemization
-
-
racemization
Q4D480
;
racemization
B8LFE4
-
PATHWAY
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
Metabolic pathways
-
ornithine degradation II (Stickland reaction)
-
SYSTEMATIC NAME
IUBMB Comments
Proline racemase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CdPRAC
Clostridium difficile
Q17ZY4
-
CdPRAC
Clostridium difficile VPI10463
Q17ZY4
-
-
PRAC
Trypanosoma cruzi Y
-
-
-
proline racemase
Clostridium difficile
Q17ZY4
-
proline racemase
Clostridium difficile VPI10463
Q17ZY4
-
-
proline racemase
Q9L4Q3
-
proline racemase
Q4D480, Q868H8
-
proline racemase
B8LFE4
-
Racemase, proline
-
-
-
-
TcPRAC
Q4D480, Q868H8
-
TcPRACA
Q4D480
isoform A
TcPRACB
Q868H8
isoform B
TvHYP1
B8LFE4
-
TvPRAC
B8LFE4
-
CAS REGISTRY NUMBER
COMMENTARY
9024-09-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Clostridium difficile
strain VPI10463
SwissProt
Manually annotated by BRENDA team
Clostridium difficile VPI10463
strain VPI10463
SwissProt
Manually annotated by BRENDA team
Trypanosoma cruzi Y
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
Q9L4Q3
catalyzes step 8 in the ornithine fermentation pathway
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
Q4D480
proline racemase participates in mechanisms of virulence acquisition; proline racemase participates in mechanisms of virulence acquisition
physiological function
B8LFE4
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
-
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
Trypanosoma cruzi Y
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Pro
D-Pro
show the reaction diagram
-
-
-
-
L-Pro
D-Pro
show the reaction diagram
-
-
-
-
L-Pro
D-Pro
show the reaction diagram
-
-
-
-
L-Pro
D-Pro
show the reaction diagram
-
-
-
-
L-Pro
D-Pro
show the reaction diagram
-
-
-
-
L-Pro
D-Pro
show the reaction diagram
-
-
-
-
L-Pro
D-Pro
show the reaction diagram
-
-
-
-
L-Pro
D-Pro
show the reaction diagram
-
-
-
-
L-Pro
D-Pro
show the reaction diagram
-
-
-
-
L-Pro
D-Pro
show the reaction diagram
-
-
-
-
L-Pro
D-Pro
show the reaction diagram
-
-
-
-
L-Pro
D-Pro
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
L-proline
D-proline
show the reaction diagram
-
-
-
-
r
L-proline
D-proline
show the reaction diagram
Q4DA80, Q868H8, -
-
-
?
L-proline
D-proline
show the reaction diagram
Q4DA80, Q868H8, -
-
-
-
-
L-proline
D-proline
show the reaction diagram
Q4D480
-
-
-
r
L-proline
D-proline
show the reaction diagram
Q9L4Q3
-
-
-
r
L-proline
D-proline
show the reaction diagram
B8LFE4, -
-
-
-
r
L-proline
D-proline
show the reaction diagram
Clostridium difficile
Q17ZY4
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
show the reaction diagram
-
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
L-proline
D-proline
show the reaction diagram
Clostridium difficile VPI10463
Q17ZY4
CdPRAC from Clostridium difficile racemizes both L- and D-Pro but not OH-L/D-Pro or any other natural amino acid
-
-
r
additional information
?
-
Q4DA80, Q868H8, -
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Pro
D-Pro
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
r
L-proline
D-proline
show the reaction diagram
Q4D480
-
-
-
r
L-proline
D-proline
show the reaction diagram
Q9L4Q3
-
-
-
r
L-proline
D-proline
show the reaction diagram
B8LFE4, -
-
-
-
r
L-proline
D-proline
show the reaction diagram
-
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
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
TcPRACB is a cofactor-independent racemase
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
37 mM, 25% inhibition
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
2-Furoic acid
-
weak
2-Thiophenecarboxylic acid
-
-
alpha-Pipecoline
-
-
DELTA1-pyrroline-2-carboxylate
-
-
HPO42-
-
no inhibition by H2PO4-
iodoacetamide
-
-
iodoacetate
-
DL-Pro and pyrrole-2-carboxylate can protect
Methoxyacetic acid
-
weak
pipecolic acid
-
weak
pyrrole-2-carboxylic acid
-
-
pyrrole-2-carboxylic acid
-
-
pyrrole-2-carboxylic acid
Clostridium difficile
Q17ZY4
-
pyrrole-2-carboxylic acid
-
PYC, competitive inhibitor
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
pyrrole-2-carboxylic acid
B8LFE4
competitive inhibitor
reduced glutathione
-
weak
Tetrahydrofuroic acid
-
weak
thioglycolate
-
weak
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activates
SH compounds
-
activate, e.g. 2-mercaptoethanol, 1,3-dimercaptoethanol
2-mercaptoethanol
-
activates; optimal concentration: 0.02 M
additional information
-
pyridoxal 5'-phosphate is not involved in racemization
-
additional information
-
addition of pyridoxal 5'-phosphate does not increase activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
106
-
D-proline
B8LFE4
40 mM substrate in 0.2 M sodium acetate, for 30 min at 37C
29
-
L-proline
-
pH 6.0, 37C
75
-
L-proline
-
pH 6.0, 37C
145
-
L-proline
B8LFE4
40 mM substrate in 0.2 M sodium acetate, for 30 min at 37C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0036
-
pyrrole-2-carboxylic acid
-
pH 6.0, 37C, TcPRACB
0.0057
-
pyrrole-2-carboxylic acid
-
pH 6.0, 37C, TcPRACA
0.02
-
pyrrole-2-carboxylic acid
B8LFE4
0.005 mM pyrrole-2-carboxylic acid, serial concentrations of 20-160 mM L-proline
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
Clostridium difficile
Q17ZY4
using NaOAc
6
-
B8LFE4
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24
37
-
at 37C the activity is 35-40% greater than at 24C
37
-
Clostridium difficile
Q17ZY4
assay at
37
-
-
assay at
37
-
B8LFE4
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
TcPRAC localizes in the cytoplasm of intracellular amastigote forms of the parasite, near the flagellar pocket of the parasites
Manually annotated by BRENDA team
-
membrane-bound and secreted forms of enzyme are present upon differentiation of the parasite into non-dividing infective forms
-
Manually annotated by BRENDA team
-
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
-
Manually annotated by BRENDA team
-
in replicative non-infective forms of Trypanosoma cruzi
Manually annotated by BRENDA team
-
TcPRACB secretes the intracellular isoform of the enzyme. TcPRACA gene can generate both secreted and intracellular isoforms (by an alternative trans-splicing mechanism)
Manually annotated by BRENDA team
-
membrane-bound and secreted forms of enzyme are present upon differentiation of the parasite into non-dividing infective forms
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40000
-
B8LFE4
recombinant enzyme, determined by SDS-PAGE
80000
-
-
TCPRACA, gel filtration, non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 38000, SDS-PAGE
?
-
x * 45000, SDS-PAGE
dimer
-
2 * 40100, TcPRACB, SDS-PAGE; 2 * 45800, TcPRACA, SDS-PAGE
homodimer
-
chrystal structure analysis
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
homodimer
Q4D480
;
monomer
-
1 * 45000, SDS-PAGE
monomer
Trypanosoma cruzi Y
-
1 * 45000, SDS-PAGE
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70
-
-
half-life: 3.6 min, in D2O 17 min
80
-
-
5 min, activity is abolished
80
-
-
10 min, inactivation
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stored 6 months in the refrigerator without significant loss of activity
-
-20C, 50% glycerol or diluted in sodium acetate buffer, pH 6.0, activity is impaired
-
-20C, 50% glycerol or diluted in sodium acetate buffer, pH 6.0, stable
-
-20C, as ammonium sulfate precipitate, stable
-
23C, 0.5 M imidazole buffer, pH 8.0, 10 days, TcPRACA loses 84% of its activity
-
23C, 0.5 M imidazole buffer, pH 8.0, 10 days, TcPRACB is stable, TcPRACA loses 84% of its activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 forms of enzyme: one binds L-Pro and the other D-Pro
-
cobalt metal-affinity resin column chromatography
-
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
-
by affinity chromatography using nickel-nitrilotriacetic acid-agarose columns
B8LFE4
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloned in Escherichia coli as a 6xHis-tag fusion protein
Clostridium difficile
Q17ZY4
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
TcPRACA is expressed in Escherichia coli 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
Q4D480
expression in Escherichia coli BL21 (DE3) with a C-terminal 6-His tag
B8LFE4
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
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)
Q4D480
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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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; 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
drug development
B8LFE4
enzyme has potential to be used as a drug target for this parasite-based trypanosomiasis