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Literature summary for 5.1.1.4 extracted from

  • Stenta, M.; Calvaresi, M.; Altoe, P.; Spinelli, D.; Garavelli, M.; Bottoni, A.
    The Catalytic Activity of Proline Racemase: A Quantum Mechanical/Molecular Mechanical Study (2008), J. Phys. Chem. B, 112, 1057-1059.
    View publication on PubMed
Search for more literature for 5.1.1.4

Organism

Organism UniProt Comment Textmining
Trypanosoma cruzi
-
-
-
Trypanosoma cruzi Q4DA80
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-

Reaction

Reaction Comment Organism Reaction ID
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 Trypanosoma cruzi
a
L-proline = D-proline quantum mechanical and molecular mechanical study reveals two almost isoenergetic minima M1a and M2a, in which the enzyme is bound to L-proline and D-proline, respectively, and a transition state TSCa, unveiling a highly asynchronous concerted process. Residues Asn133, Asp296, and Gly301 destabilize M2a. Conversely, both Gly131and Gly303 stabilize M2a. Residues Gly131, Gly301, and Thr302 stabilize TSCa Trypanosoma cruzi
a

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
proline racemase
-
 Trypanosoma cruzi