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Literature summary for 5.6.2.4 extracted from
- Unwinding the structure and function of the archaeal MCM helicase (2009), Mol. Microbiol., 72, 286-296.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | a mutation of the MCM N-terminal beta-hairpin reduces but does not abolish DNA binding and helicase activity | Saccharolobus solfataricus |
| additional information | a mutation of the zinc finger motif of the MCM protein reduces single-stranded and double-stranded DNA binding and abolishes helicase activity. Removal of the HTH domain from the MCM protein results in an enzyme with increased ATPase and helicase activity. A mutation of the MCM N-terminal beta-hairpin completely abolishes DNA binding and helicase activity | Methanothermobacter thermautotrophicus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Methanothermobacter thermautotrophicus | during chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand | ADP + phosphate | - |
? |  |
| ATP + H2O | Saccharolobus solfataricus | during chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand | ADP + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanothermobacter thermautotrophicus | - |
- |
- |
| Saccharolobus solfataricus | Q9UXG1 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | during chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand | Methanothermobacter thermautotrophicus | ADP + phosphate | - |
? | |
| ATP + H2O | during chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand | Saccharolobus solfataricus | ADP + phosphate | - |
? | |
| ATP + H2O | ATP-dependent 3'-5' helicase activity. During chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand. ATP binding enhances DNA binding by the helicase. ATPase activity is substantially enhanced in presence of DNA. MCM protein binds DNA ends better than long circular substrates | Methanothermobacter thermautotrophicus | ADP + phosphate | - |
? | |
| ATP + H2O | ATP-dependent 3'-5' helicase activity. During chromosomal DNA replication, the replicative helicase unwinds the duplex DNA to provide the single-stranded DNA substrate for the polymerase. In archaea, the replicative helicase is the minichromosome maintenance complex. The enzyme utilizes the energy of ATP hydrolysis to translocate along one strand of the duplex and unwind the complementary strand. Very limited stimulation of its ATPase activity by DNA | Saccharolobus solfataricus | ADP + phosphate | - |
? | |
| additional information | the helicase is capable of unwinding DNA substrates coated with various proteins, including histones, transcription inhibitors, and the transcription initiation complex. Thus, the helicase can displace at least some of the proteins associated with chromatin | Methanothermobacter thermautotrophicus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heptamer | structural polymorphism: in addition to helical filaments and heptameric rings the protein also forms double heptamers, hexamers and double hexamers, octamers and open rings | Methanothermobacter thermautotrophicus |
| hexamer | - |
Saccharolobus solfataricus |
| hexamer | structural polymorphism: in addition to helical filaments and heptameric rings the protein also forms double heptamers, hexamers and double hexamers, octamers and open rings | Methanothermobacter thermautotrophicus |
| octamer | structural polymorphism: in addition to helical filaments and heptameric rings the protein also forms double heptamers, hexamers and double hexamers, octamers and open rings | Methanothermobacter thermautotrophicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MCM helicase | - |
Methanothermobacter thermautotrophicus |
| MCM helicase | - |
Saccharolobus solfataricus |
| MCM protein | - |
Methanothermobacter thermautotrophicus |
| MCM protein | - |
Saccharolobus solfataricus |
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