RNA ligase (ATP)

The 3 substrates of this enzyme are ATP, (ribonucleotide)n, and (ribonucleotide)m, whereas its 3 products are AMP, diphosphate, and (ribonucleotide)n+m.

This enzyme belongs to the family of ligases, specifically those forming phosphoric-ester bonds. The systematic name of this enzyme class is poly(ribonucleotide):poly(ribonucleotide) ligase (AMP-forming). Other names in common use include polyribonucleotide synthase (ATP), RNA ligase, polyribonucleotide ligase, and ribonucleic ligase.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1VDX and 2C5U.

References

Silber R, Malathi VG, Hurwitz J (1972). "Purification and properties of bacteriophage T4-induced RNA ligase". Proc. Natl. Acad. Sci. U.S.A. 69 (10): 3009–13. doi:10.1073/pnas.69.10.3009. PMC 389696. PMID 4342972.

Enzymes: Phosphoric ester and nitrogen-metal ligases (EC 6.5-6.6)

6.5: Phosphoric Ester	DNA ligase

6.6: Nitrogen-Metal	Magnesium chelatase Cobalt chelatase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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