Literature summary for 1.14.19.70 extracted from

Dornevil, K.; Davis, I.; Fielding, A.J.; Terrell, J.R.; Ma, L.; Liu, A.
Cross-linking of dicyclotyrosine by the cytochrome P450 enzyme CYP121 from Mycobacterium tuberculosis proceeds through a catalytic shunt pathway (2017), J. Biol. Chem., 292, 13645-13657 .

Search for more literature for 1.14.19.70

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
cyclo(L-tyrosyl-L-tyrosyl) + [reduced NADPH-hemoprotein reductase] + O2	Mycobacterium tuberculosis	the enzyme is involved in the biosynthesis of mycocyclosin. It is crucial for the viability of this pathogen	mycocyclosin + [oxidized NADPH-hemoprotein reductase] + 2 H2O	-	?

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	the enzyme is involved in the biosynthesis of mycocyclosin. It is crucial for the viability of this pathogen	Mycobacterium tuberculosis	mycocyclosin + [oxidized NADPH-hemoprotein reductase] + 2 H2O	-	?
cyclo(L-tyrosyl-L-tyrosyl) + [reduced NADPH-hemoprotein reductase] + O2	study of substrate binding kinetics	Mycobacterium tuberculosis	mycocyclosin + [oxidized NADPH-hemoprotein reductase] + 2 H2O	-	?

Synonyms

Synonyms	Comment	Organism
CYP121	-	Mycobacterium tuberculosis

Cofactor

Cofactor	Comment	Organism	Structure
cytochrome P450	a plausible free radicalbased mechanisms for the CC bond coupling reaction is proposed	Mycobacterium tuberculosis

General Information

General Information	Comment	Organism
metabolism	the enzyme is involved in the biosynthesis of mycocyclosin. It is crucial for the viability of this pathogen	Mycobacterium tuberculosis

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)