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Literature summary for 1.14.19.70 extracted from
- QM/MM study of the C-C coupling reaction mechanism of CYP121, an essential cytochrome p450 of Mycobacterium tuberculosis (2014), Proteins, 82, 1004-1021 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | P9WPP7 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cyclo(L-tyrosyl-L-tyrosyl) + [reduced NADPH-hemoprotein reductase] + O2 | classical and quantum based computer simulation methods are used to study in detail the reaction mechanism. Substrate binding promotes formation of the initial oxy complex. Compound I is responsible for first Tyr radical formation, and that the second Tyr radical is formed subsequently, through a proton-coupled electron transfer reaction, promoted by the presence of key residue Arg386. The final C-C coupling reaction possibly occurs in bulk solution, thus yielding the product in one oxygen reduction cycle | Mycobacterium tuberculosis | mycocyclosin + [oxidized NADPH-hemoprotein reductase] + 2 H2O | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CYP121 | - |
Mycobacterium tuberculosis |
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Release 2023.1 (January 2023)
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