Literature summary for 1.17.4.1 extracted from

Qiu, W.; Zhou, B.; Darwish, D.; Shao, J.; Yen, Y.
Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits (2006), Biochem. Biophys. Res. Commun., 340, 428-434.

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q7LG56	ribonucleoside-diphosphate reductase subunit M2 B	-

Subunits

Subunits	Comment	Organism
More	ribonucleoside-diphosphate reductase subunit M2 B may substitute for small enzyme subunit hRRM2 to form a functional holoenzyme with large subunit hRRM1. The holoenzyme with subunit M2 B can only achieve 40-75% kinetic activity of that with hRRM2. Both small subunits share the same binding site on large subunit hRRM1. The effectors ATP or dATP can regulate holoenzyme activity independent of the small subunit	Homo sapiens

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Release 2023.1 (January 2023)