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Information on EC 3.1.26.4 - ribonuclease H

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.26 Endoribonucleases producing 5'-phosphomonoesters
                3.1.26.4 ribonuclease H
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This record set is specific for:
UNIPROT: Q8TDP1 not found.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Endonucleolytic cleavage to a 5'-phosphomonoester
Synonyms
reverse transcriptase, ribonuclease h, rnase h2, rnase hii, rnaseh2a, rnaseh1, ribonuclease hi, ribonuclease h2, rnase hiii, ribonuclease h1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
endoribonuclease H
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hybrid nuclease
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hybrid ribonuclease
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hybridase
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hybridase (ribonuclease H)
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nuclease, hybrid ribo-
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nuclease, ribo-, H
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P32
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ribonuclease H
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RNA*DNA hybrid ribonucleotidohydrolase
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RNase H
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RNase H1
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RNase HI
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RNase HII
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RNase HIII
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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CAS REGISTRY NUMBER
COMMENTARY hide
9050-76-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
DNA12-RNA1-DNA27/DNA40 hybrid + H2O
?
show the reaction diagram
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enzyme cleaves RNA20/DNA20 hybrid and DNA12-RNA1-DNA27/DNA40 hybrid substrates with similar efficiency
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?
poly-rA/poly-dT + H2O
?
show the reaction diagram
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products are short oligonucleotides with very few intermediate-sized oligonucleotides
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?
RNA20/DNA20 hybrid + H2O
?
show the reaction diagram
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enzyme cleaves RNA20/DNA20 hybrid and DNA12-RNA1-DNA27/DNA40 hybrid substrates with similar efficiency
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
highest activity in presence of 5-10 mM
Mn2+
0.1-1 mM, 20-30% of maximum activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit H2C; isoform RNase H2
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RNH2C_HUMAN
164
0
17840
Swiss-Prot
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PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
heterotrimer of subunits H2A, H2B, H2C, SDS-PAGE and gel filtration
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K143I
mutation in subunit H2C associated with Aicardi-Goutieres' syndrome, near-normal activity
R69W
mutation in subunit H2C associated with Aicardi-Goutieres' syndrome, 30-40% of wild-type activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and in HeLa cell
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chon, H.; Vassilev, A.; DePamphilis, M.L.; Zhao, Y.; Zhang, J.; Burgers, P.M.; Crouch, R.J.; Cerritelli, S.M.
Contributions of the two accessory subunits, RNASEH2B and RNASEH2C, to the activity and properties of the human RNase H2 complex
Nucleic Acids Res.
37
96-110
2009
Homo sapiens, Homo sapiens (Q5TBB1), Homo sapiens (Q8TDP1)
Manually annotated by BRENDA team