Literature summary for 1.17.4.2 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.

Search for more literature for 1.17.4.2

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Lactobacillus leichmannii	-	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
RTPR	-	Lactobacillus leichmannii

Cofactor

Cofactor	Comment	Organism	Structure
coenzyme B12	adenosylcobalamin	Lactobacillus leichmannii

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)