Literature summary extracted from

Dumas, V.; Defelipe, L.; Petruk, A.; Turjanski, A.; Marti, M.
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

EC Number	Organism	UniProt	Comment	Textmining
1.14.19.70	Mycobacterium tuberculosis	P9WPP7	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.14.19.70	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

EC Number	Synonyms	Comment	Organism
1.14.19.70	CYP121	-	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)