Literature summary extracted from

Licht, S.S.; Lawrence, C.C.; Stubbe, J.
Thermodynamic and kinetic studies on carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: The importance of entropy in catalysis (1999), Biochemistry, 38, 1234-1242.

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1.17.4.2	ribonucleoside triphosphate + reduced thioredoxin + H2O	Lactobacillus leichmannii	-	2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O	-	r

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.17.4.2	Lactobacillus leichmannii	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.17.4.2	ribonucleoside triphosphate + reduced thioredoxin	-	Lactobacillus leichmannii	2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O	-	r
1.17.4.2	ribonucleoside triphosphate + reduced thioredoxin + H2O	-	Lactobacillus leichmannii	2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O	-	r

Synonyms

EC Number	Synonyms	Comment	Organism
1.17.4.2	RTPR	-	Lactobacillus leichmannii

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.17.4.2	coenzyme B12	adenosylcobalamin	Lactobacillus leichmannii

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Release 2023.1 (January 2023)