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Ribonucleoside-diphosphate reductase catalytic subunit M1 is the large and catalytic component of ribonucleotide reductase, an essential enzyme complex responsible for converting ribonucleotides into deoxyribonucleotides—the building blocks required for DNA synthesis during cell division. The human gene encoding this protein is called RRM1. This enzyme plays a critical role in maintaining balanced pools of deoxyribonucleotide triphosphates necessary for accurate DNA replication and repair. It is tightly regulated through allosteric mechanisms involving ATP/dATP binding that modulate both activity and substrate specificity.[2] Dysregulation or genetic alterations affecting this gene have been implicated in various cancers as well as genetic syndromes such as Beckwith-Wiedemann syndrome.[1] Because it is indispensable for DNA synthesis in proliferating cells, it serves as a key therapeutic target—especially in oncology—for drugs designed to disrupt tumor growth by blocking nucleotide biosynthesis.[2][3]
Drugs targeting this enzyme typically act by inhibiting its catalytic activity to block the production of deoxyribonucleotides required for DNA replication and repair, leading to cell cycle arrest or apoptosis in rapidly dividing cells such as cancer cells.[2][3]
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