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Literature summary for 3.1.26.4 extracted from

  • Pallan, P.S.; Egli, M.
    Insights into RNA/DNA hybrid recognition and processing by RNase H from the crystal structure of a non-specific enzyme-dsDNA complex (2008), Cell Cycle, 7, 2562-2569.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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Halalkalibacterium halodurans

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the inability of the enzyme to cleave DNA is due to the deviating curvature of the DNA strand relative to the substrate RNA strand and the absence of Mg2+ at the active site Halalkalibacterium halodurans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Halalkalibacterium halodurans member of the nucleotidyl-transferase superfamily and endo-nucleolytically cleaves the RNA portion in RNA/DNA hybrids and removes RNA primers from Okazaki fragments. Enzyme binds RNA and DNA duplexes but is unable to cleave either ?
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?

Organism

Organism UniProt Comment Textmining
Halalkalibacterium halodurans Q9KEI9
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information member of the nucleotidyl-transferase superfamily and endo-nucleolytically cleaves the RNA portion in RNA/DNA hybrids and removes RNA primers from Okazaki fragments. Enzyme binds RNA and DNA duplexes but is unable to cleave either Halalkalibacterium halodurans ?
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?

Synonyms

Synonyms Comment Organism
ribonuclease HI
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Halalkalibacterium halodurans
RNase H
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Halalkalibacterium halodurans