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3.1.26.4: ribonuclease H

This is an abbreviated version!
For detailed information about ribonuclease H, go to the full flat file.

Word Map on EC 3.1.26.4

Reaction

Endonucleolytic cleavage to a 5'-phosphomonoester =

Synonyms

Ape-RNase HII, aRNase HII, Bh ribonuclease H, BhRNase H, CtepRNH, EcRNH, endoribonuclease H, endoribonuclease H (calf thymus), ERNH, huRNaseH1, hybrid nuclease, hybrid ribonuclease, hybridase, hybridase (ribonuclease H), KOD1, LC9-RNase H1, lmo1273, LRNase HII, More, nuclease, hybrid ribo-, nuclease, ribo-, H, P32, protein ST0753, reverse transcriptase, ribonuclease H, ribonuclease H I, ribonuclease H(42), ribonuclease H(70), ribonuclease H1, ribonuclease H2, ribonuclease H3, ribonuclease HI, ribonuclease HII, ribonuclease HIII, ribonulease H1, RNA*DNA hybrid ribonucleotidohydrolase, RNA*DNA hybrid ribonucleotiohydrolase, RNase H, RNase H type 2, RNase H(35), RNase H1, RNase H2, RNase H3, RNase HI, RNase HII, RNase HIII, RNaseH, Rnaseh1, RNASEH2A, RNH, RNH1, RNH2, rnhA, RnhB, rnhC, rnhD, Rv2228c, ST0519, STK_07530, Sto-RNase HI, T4 RNase H, Tk-RNase HII, Tk-Tk-RNase HII, TK0805, TRNH, TthRNH, Ty1 reverse transcriptase/RNase H, type 1 ribonuclease H, type 1 RNase H, type 2 ribonuclease H, type 2 RNase H, type II ribonuclease H

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.26 Endoribonucleases producing 5'-phosphomonoesters
                3.1.26.4 ribonuclease H

Renatured

Renatured on EC 3.1.26.4 - ribonuclease H

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
comparison of the folding trajectories of the three-state RNase H mutant D10A and the two-state RNase H mutant D10A/I53D, proteins with the same native-state topology but altered regional stability. Both versions of RNase H fold through a similar trajectory with similar high-energy conformations. Mutations in the core and the periphery of the protein affect similar aspects of folding for both variants
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recombinant I53 and L56 point mutants after being expressed insolubly in inclusion bodies in Escherichia coli
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refolding from purified urea-denatured form with low yield
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study on thermal and mechanical folding and unfolding mechanisms. Mechanical and thermal unfolding proceed through three stable states that are similar. The one difference between the two regimes is in the transition occurring at the most denaturing conditions. For the thermal case, both secondary and tertiary structures melt. For the mechanical case, the secondary structure of the helices remains largely intact, while the bundle itself unfolds. Of the major secondary structure motifs, alpha-helices are more stable than beta-sheets
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the denaturation by guanidinium chloride is completely reversible at 50°C, the unfolding and refolding reactions of the enzyme attain a two-state equilibrium in 2 weeks