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Literature summary for 5.6.2.4 extracted from

  • Hong, Y.; Chu, M.; Li, Y.; Ni, J.; Sheng, D.; Hou, G.; She, Q.; Shen, Y.
    Dissection of the functional domains of an archaeal Holliday junction helicase (2012), DNA Repair, 11, 102-111.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Sulfurisphaera tokodaii the Hjm protein is essential for cell viability. The StoHjc protein regulates the helicase activity of StoHjm by inducing conformation change of the enzyme. Hjm/Hjc mediated resolution of stalled replication forks is of crucial importance in archaea. A tentative pathway with which Hjm/Hjc interaction could have occurred at stalled replication forks is discussed ADP + phosphate
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Organism

Organism UniProt Comment Textmining
Sulfurisphaera tokodaii
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O the Hjm protein is essential for cell viability. The StoHjc protein regulates the helicase activity of StoHjm by inducing conformation change of the enzyme. Hjm/Hjc mediated resolution of stalled replication forks is of crucial importance in archaea. A tentative pathway with which Hjm/Hjc interaction could have occurred at stalled replication forks is discussed Sulfurisphaera tokodaii ADP + phosphate
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ATP + H2O StoHjm has two main modules, the N-terminal ATPase and DNA binding module (1–431) and the C-terminal helicase regulation module (414–704). While the N-terminal module is active alone to hydrolyze ATP and to bind different types of DNA substrates, it does not show any helicase activity. DNA unwinding by the StoHjm protein requires the presence of domain III and IV of the C-terminal module in addition to the N-terminal module Sulfurisphaera tokodaii ADP + phosphate
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Synonyms

Synonyms Comment Organism
Holliday junction helicase
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Sulfurisphaera tokodaii
StoHjm
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Sulfurisphaera tokodaii