| Accepted Name |
|---|
| RNA 5'-3' helicase
|
| Reaction catalysed |
|---|
| n ATP + n H2O + wound RNA = n ADP + n phosphate + unwound RNA |
| Comment(s) |
|---|
- RNA helicases, which participate in nearly all aspects of RNA
metabolism, utilize the energy from ATP hydrolysis to unwind RNA.
- The engine core of helicases is usually made of a pair of RecA-like
domains that form an NTP binding cleft at their interface.
- Changes in the chemical state of the NTP binding cleft (binding of
the NTP or its hydrolysis products) alter the relative positions of
the RecA-like domains and nucleic acid-binding domains, creating
structural motions that disrupt the pairing of the nucleic acid,
causing separation and unwinding.
- Most RNA helicases utilize a mechanism known as canonical duplex
unwinding, in which the helicase binds to a single stranded region
adjacent to the duplex and then translocates along the bound strand
with defined directionality, displacing the complementary strand.
- Most of these helicases proceed 3' to 5' (type A polarity - cf.
EC 5.6.2.6), but some proceed 5' to 3' (type B polarity), and some
are able to catalyze unwinding in either direction.
- Most canonically operating helicases require substrates with single
stranded regions in a defined orientation (polarity) with respect to
the duplex.
- A different class of RNA helicases, EC 5.6.2.7, use a different
mechanism and unwind short stretches of RNA with no translocation.
|
| Cross-references |
|---|
| BRENDA | 5.6.2.5 |
| EC2PDB | 5.6.2.5 |
| ExplorEnz | 5.6.2.5 |
| KEGG Ligand Database for Enzyme Nomenclature | 5.6.2.5 |
| IUBMB Enzyme Nomenclature | 5.6.2.5 |
| MEDLINE | Find literature relating to 5.6.2.5 |
| MetaCyc | 5.6.2.5 |
| Rhea expert-curated reactions | 5.6.2.5 |
| UniProtKB/Swiss-Prot |
|
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