EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.1.1.4 | Trypanosoma cruzi | - |
- |
- |
5.1.1.4 | Trypanosoma cruzi | Q4DA80 | - |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
5.1.1.4 | 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 | |
5.1.1.4 | 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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.1.4 | L-proline | - |
Trypanosoma cruzi | D-proline | - |
? | |
5.1.1.4 | 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 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
5.1.1.4 | proline racemase | - |
Trypanosoma cruzi |