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Literature summary extracted from

  • 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 (2006), Proc. Natl. Acad. Sci. USA, 103, 1705-1710.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.4 TcPRACA is expressed in Escherichia coli BL21 (DE3) Trypanosoma cruzi

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.1.1.4 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 Trypanosoma cruzi
5.1.1.4 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 Trypanosoma cruzi

Protein Variants

EC Number Protein Variants Comment Organism
5.1.1.4 C130S mutation of the catalytic Cys residues abolishes the enzymatic activity but preserves the mitogenic properties of the protein Trypanosoma cruzi
5.1.1.4 C300S mutation of the catalytic Cys residues abolishes the enzymatic activity but preserves the mitogenic properties of the protein Trypanosoma cruzi

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.1.4 pyrrole-2-carboxylic acid PYC, competitive inhibitor Trypanosoma cruzi

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.4 Trypanosoma cruzi Q4DA80
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.4 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 Trypanosoma cruzi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.4 L-proline
-
 Trypanosoma cruzi D-proline
-
 ?

Subunits

EC Number Subunits Comment Organism
5.1.1.4 homodimer chrystal structure analysis Trypanosoma cruzi

Synonyms

EC Number Synonyms Comment Organism
5.1.1.4 proline racemase
-
 Trypanosoma cruzi
5.1.1.4 TcPRACA
-
 Trypanosoma cruzi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.1.4 37
-
 assay at Trypanosoma cruzi