Literature summary for 1.17.4.1 extracted from

Sato, A.; Cory, J.G.
Differential sensitivities of the subunits of mammalian ribonucleotide reductase to proteases, sulfhydryl reagents, and heat (1986), Arch. Biochem. Biophys., 244, 572-579.

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Activating Compound

Activating Compound	Comment	Organism	Structure
dTTP	-	Mus musculus

General Stability

General Stability	Organism
effector-binding subunit of mammalia is more sensitive to proteolysis by chymotrypsin, to heating at 55°C and to sulfhydryl reagents e.g. p-chloromercuribenzoate and N-ethylmaleimide, than the nonheme iron subunit, the latter is more sensitive to trypsin treatment	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	-	Ehrlich ascites tumor cells	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
Ehrlich ascites carcinoma cell	-	Mus musculus	-
L-1210 cell	-	Mus musculus	-
L-cell	cell line	Mus musculus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ribonucleoside diphosphate + reduced thioredoxin	-	Mus musculus	2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O	-	ir

Subunits

Subunits	Comment	Organism
More	enzyme in Ehrlich ascites tumor cells consits of two nonidentical subunits: an effector-binding subunit, EB, and a non-heme iron containing subunit, NHI, since their relative levels are not coordinately regulated the stoichiometry of the whole enzyme varies with the cell cycle	Mus musculus

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Release 2023.1 (January 2023)