dinucleotide phosphatase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: a dinucleotide + H2O = 2 mononucleotides. [PMID:2848456, PMID:4405504]

Dinucleotide phosphatase activity is a type of hydrolase activity that specifically removes a phosphate group from a dinucleotide. Dinucleotides are molecules composed of two nucleotide units linked by a phosphodiester bond. This enzymatic activity plays a crucial role in various cellular processes, including:

1. **Nucleotide metabolism:** Dinucleotide phosphatases are involved in the degradation of dinucleotides, generating mononucleotides that can be used as building blocks for nucleic acid synthesis or as substrates for other metabolic pathways.
2. **Signal transduction:** Some dinucleotides act as second messengers in signal transduction pathways, and their dephosphorylation by dinucleotide phosphatases can modulate signal duration and intensity.
3. **Regulation of gene expression:** Certain dinucleotides are involved in the regulation of gene expression, and their dephosphorylation can influence the activity of transcription factors or other regulatory proteins.
4. **Cellular detoxification:** Dinucleotide phosphatases can contribute to the detoxification of harmful dinucleotides, preventing their accumulation and potential deleterious effects.

The catalytic mechanism of dinucleotide phosphatases typically involves the formation of a transient covalent intermediate between the enzyme and the phosphate group being removed. This intermediate is then hydrolyzed, releasing the phosphate group and regenerating the active enzyme. The specific mechanism can vary depending on the enzyme and its substrate.'
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Proteins (1)

Compounds (8)