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Literature summary extracted from

  • Livesay, D.R.; Jacobs, D.J.
    Conserved quantitative stability/flexibility relationships (QSFR) in an orthologous RNase H pair (2006), Proteins, 62, 130-143.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.26.4 additional information
-
 additional information thermodynamics, heat capacity measurement, thermal stability and flexibility of the enzyme Thermus thermophilus
3.1.26.4 additional information
-
 additional information thermodynamics, heat capacity measurement, thermal stability and flexibility of the enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.26.4 DNA-RNA duplex + H2O Thermus thermophilus specific cleavage of the RNA part ?
-
 ?
3.1.26.4 DNA-RNA duplex + H2O Escherichia coli specific cleavage of the RNA part ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.4 Escherichia coli
-
-
-
3.1.26.4 Thermus thermophilus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.26.4 Endonucleolytic cleavage to a 5'-phosphomonoester evolutionary conserved flexible regions are important for catalysis, structure function relationship, enthalpic/entropic compensation mechanism, overview Thermus thermophilus
a
3.1.26.4 Endonucleolytic cleavage to a 5'-phosphomonoester evolutionary conserved flexible regions are important for catalysis, structure function relationship, enthalpic/entropic compensation mechanism, overview Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.26.4 DNA-RNA duplex + H2O specific cleavage of the RNA part Thermus thermophilus ?
-
 ?
3.1.26.4 DNA-RNA duplex + H2O specific cleavage of the RNA part Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.26.4 More identification and analysis of folding core and flexible regions, which are evolutionary conserved important for catalysis, conserved quantitative stability/flexibility relationships, QSFR, overview Thermus thermophilus
3.1.26.4 More identification and analysis of folding core and flexible regions, which are evolutionary conserved important for catalysis, conserved quantitative stability/flexibility relationships, QSFR, overview Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.1.26.4 RNase H
-
 Thermus thermophilus
3.1.26.4 RNase H
-
 Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.26.4 additional information
-
 melting temperature is 66°C, conserved quantitative stability/flexibility relationships, QSFR, thermodynamics, thermal stability and flexibility of the enzyme Escherichia coli
3.1.26.4 additional information
-
 melting temperature is 86°C, conserved quantitative stability/flexibility relationships, QSFR, thermodynamics, thermal stability and flexibility of the enzyme Thermus thermophilus