tetrahydrofolyl-poly(glutamate) polymer binding

Definition

Target type: molecularfunction

Binding to tetrahydrofolyl-poly(glutamate) polymer. [GO_REF:0000067, GOC:BHF, GOC:hal, GOC:TermGenie, PMID:24863754]

Tetrahydrofolyl-poly(glutamate) polymer binding describes the interaction of proteins with the polyglutamated forms of tetrahydrofolate (THF). THF is a crucial cofactor in various metabolic pathways, including nucleotide biosynthesis, amino acid metabolism, and the synthesis of DNA and RNA. Polyglutamylation of THF, the addition of multiple glutamate residues to the molecule, enhances its affinity for specific enzymes involved in these pathways.

The molecular function of tetrahydrofolyl-poly(glutamate) polymer binding involves the following steps:

1. **Recognition and Binding:** Proteins with tetrahydrofolyl-poly(glutamate) polymer binding activity possess specific binding sites that recognize and interact with the polyglutamate chain of THF. The number of glutamate residues in the polyglutamate chain can vary depending on the enzyme and cellular location.
2. **Conformation Change:** Upon binding of the polyglutamated THF, the protein may undergo a conformational change, bringing the active site closer to the substrate. This conformational change is crucial for the efficient catalysis of the enzymatic reaction.
3. **Substrate Delivery:** The polyglutamate chain acts as a tether, keeping the THF molecule in close proximity to the active site of the enzyme, ensuring efficient substrate delivery and preventing diffusion away from the enzyme.
4. **Regulation of Enzyme Activity:** The length of the polyglutamate chain can influence the activity of the enzyme. In some cases, longer polyglutamate chains can increase the affinity of the enzyme for the substrate, leading to enhanced catalytic activity.
5. **Subcellular Localization:** Polyglutamylation can also regulate the subcellular localization of enzymes, directing them to specific cellular compartments where their activity is required.

The specific interactions between the polyglutamate chain and the protein binding site vary depending on the protein and the cellular context. However, these interactions generally involve hydrogen bonds, ionic interactions, and hydrophobic interactions.

Overall, tetrahydrofolyl-poly(glutamate) polymer binding is a crucial process for the efficient and regulated activity of a wide range of metabolic enzymes. This process ensures the proper functioning of essential metabolic pathways, including nucleotide biosynthesis, amino acid metabolism, and DNA and RNA synthesis.'
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Proteins (1)

Compounds (13)