Literature summary extracted from

Larsson, K.M.; Jordan, A.; Eliasson, R.; Reichard, P.; Logan, D.T.; Nordlund, P.
Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase (2004), Nat. Struct. Mol. Biol., 11, 1142-1149.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.17.4.1	hanging drop method, crystal structures of the dimeric class II RNR in complex with four cognate allosteric specificity effector-substrate pairs (dTTP-GDP, dGTP-ADP, dATP-CDP or dATP-UDP), as well as structures with only the different effectors (dATP, dTTP or dGTP)	Thermotoga maritima
1.17.4.2	enzyme in complex with dATP, DTTP, dGTP, dTTP-GDP, dGTP-ADP, dATP-CDP or dATP-UDP	Thermotoga maritima

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.17.4.1	Thermotoga maritima	O33839	-	-
1.17.4.2	Thermotoga maritima	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.17.4.1	GDP + reduced thioredoxin	-	Thermotoga maritima	2'-dGDP + thioredoxin disulfide + H2O	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
1.17.4.2	class II ribonucleotide reductase	-	Thermotoga maritima

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Release 2023.1 (January 2023)