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Enzyme Nomenclature
Information on EC 3.1.27.1 - ribonuclease T2
for references in articles please use BRENDA:EC3.1.27.1
Word Map on EC 3.1.27.1
- 3.1.27.1
-
antiviral
- viral
-
interferon
- oligoadenylate
-
endoribonuclease
-
double-stranded
- 2',5'-oligoadenylate
- viruses
-
dsrna
-
2-5a-dependent
-
interferon-induced
-
single-stranded
- s-rnases
- polynucleotide
-
ifn-induced
-
lauric
-
nucleases
- rhizopus
- niveus
-
omega-3
-
5'-terminal
-
solanaceous
-
xenotropic
-
ifn-beta
-
encephalomyocarditis
-
ifn-stimulated
-
s-locus
-
dsrna-dependent
-
omega-hydroxylation
- polyu
- pistil
-
anticodons
- exoribonucleases
-
interferon-regulated
-
oligoribonucleotides
- gametophytic
-
interferon-treated
- colicins
- alata
-
5'-phosphorylated
- medicine
- biotechnology
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.1.27.1
-
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RECOMMENDED NAME
GeneOntology No.
ribonuclease T2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
mechanism
-
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
similar enzyme with possilbly exonucleolytic mechanism
-
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
two-stage endonucleolytic cleavage to 3'-phosphomononucleotides and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates: first step reversible cleavage of phosphodiester bond between 3'-adenylic acid group and 5'-hydroxyl group at adjacent nucleotides in RNA chain with formation of nucleoside 2',3'-cyclic phosphates and oligonucleotides with 2',3'-cyclic phosphate at 3'-terminal, second step: hydrolysis of terminal cyclic phosphate groups with formation of corresponding 3'-phosphates
-
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
substrate recognition, binding and specificity, Asn71 and Leu73 are involved
-
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
Phe101 is important for catalytic activity
-
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
residues His34, His 83, Glu84, Lys87, and His88 may be involved in catalysis
-
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
active site structure, Glu32 is an essential part of the B2-substrate recognition and binding site
-
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
catalytic hydrolysis mechanism, active site structure, the conserved active site residues His39, His92, and His 97 are essential for activity, Glu93 and Lys96 are important
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
reaction mechanism
-
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
reaction mechanism
-
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
reaction mechanism, His109, Lys108, His104, and His46 are involved
-
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
mechanism of RNA recognition, binding and cleavage by RNase L, overview
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
37278-25-4
-
9075-06-3
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
multiple forms: RNase T2, RNase T2-L1-5, common protein moiety, heterogeneities due to carbohydrate content
-
-
rnalx gene, intracellular ribonuclease LX precursor; cv. Lukullus
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
RNS2 is part of a process that degrades rRNA to recycle its components and is conserved in all eukaryotes
evolution
-
involvement of the pseudokinase domain of the enzyme cofactor sensing, nucleotide binding, dimerization, and ribonuclease functions highlights the evolutionary adaptability of the eukaryotic protein kinase fold
evolution
-
involvement of the pseudokinase domain of the enzyme cofactor sensing, nucleotide binding, dimerization, and ribonuclease functions highlights the evolutionary adaptability of the eukaryotic protein kinase fold
evolution
RNase T2 is the only member of the Rh/T2/S family of acidic hydrolases in humans, its structure shows a typical fold for members of the T2 RNase family with seven alpha-helices and eight beta-strands constituting an alpha+beta motif, as most of the central anti-parallel beta-sheet is clearly separated in the sequence from the helical parts. The alpha + beta core fold shows high similarity to those of known T2 RNase structures from plants, while, in contrast, the external loop regions show distinct structural differences
evolution
-
RNase X25 belongs to the RNase T2 family which harbors enzymes associated with the secretory pathway that are almost absolutely conserved in all eukaryote
evolution
-
RNase T2 family, phylogenetic analysis, gene duplication events seem to have happened independently in each phylum. RNase T2 genes have undergone duplication events followed by divergence in several phyla, including the loss of catalytic residues, and suggest that RNase T2 proteins have acquired additional functions. Among those, it is likely that a role in host immunosuppression evolved independently in several groups, including parasitic Platyhelminthes and parasitoid wasps
evolution
-
RNase X25 belongs to the RNase T2 family which harbors enzymes associated with the secretory pathway that are almost absolutely conserved in all eukaryote
-
malfunction
-
mutants lacking RNS2 activity accumulate RNA intracellularly, and rRNA in these mutants has a longer half-life, rns2 mutants display constitutive autophagy, phenotypes, overview
malfunction
-
loss of rnaset2 in mutant zebrafish results in accumulation of undigested rRNA within lysosomes within neurons of the brain, the mutants show white matter lesions correlating with accumulation of amyloid precursor protein and astrocytes at sites of neurodegeneration
malfunction
-
RNaseT2 family members are implicated in human pathologies such as cancer and parasitic diseases. Humans lacking RNASET2 manifest a defect in neurological development, perhaps due to aberrant control of the immune system. Mutations in RNASET2 are identified as the causative lesion in an autosomal recessive disorder leading to cystic leukoencephalopathy, overview
malfunction
-
virus-mediated autophagy is deficient in cells lacking RNase L, overview
malfunction
mutations in the gene of human enzyme RNase T2 are associated with white matter disease of the human brain showing bilateral temporal lobe cysts and multifocal white matter lesions which lead to psychomotor impairments,spasticity and epilepsy
malfunction
-
siRNA-mediated depletion of endogenous enzyme in the human ovarian cancer cell line Hey1b increased the levels of LINE-1 retrotransposition by about 2fold. Recombinant expression of wild-type and a constitutively active deletion mutant enzyme form, but not a catalytically inactive enzyme mutant R667A, impair the mobility of engineered human LINE-1 and mouse intracisternal A-type particle retrotransposons in cultured human cells
malfunction
A3M929
disruption of the RNase T2 family gene limits the organism's ability to colonize polystyrene, polypropylene, glass, and stainless steel surfaces, transposon mutagenesis analysis of abiotic surface-colonization of wild-type and mutant strain 98-37-09, the mutant exhibits reduced expression of 29 genes, 15 of which are predicted to be associated with bacterial attachment and surface-associated motility, overview
malfunction
-
GFP-tagged enzyme wild-type and mutants N37Q/N70Q/N103Q/N123Q and W399R localize to the vacuole, the unglycosylated mutants are unable to be secreted, overview. Glycosylation-defective Rny1p mutants are not destroyed via the ERAD mechanism
malfunction
-
disruption of the RNase T2 family gene limits the organism's ability to colonize polystyrene, polypropylene, glass, and stainless steel surfaces, transposon mutagenesis analysis of abiotic surface-colonization of wild-type and mutant strain 98-37-09, the mutant exhibits reduced expression of 29 genes, 15 of which are predicted to be associated with bacterial attachment and surface-associated motility, overview
-
metabolism
-
the interferon-inducible antiviral state is mediated in part by the 2',5'-oligoadenylate synthetase/RNase L system
metabolism
-
cellular functions of RNase T2 proteins are associated with RNA recycling and maintenance of cellular homeostasis
metabolism
-
cellular functions of RNase T2 proteins are associated with RNA recycling and maintenance of cellular homeostasis
-
physiological function
the zebrafish genome contains two RNase T2 genes, RNase Dre1 and RNase Dre2. These genes are part of two phylogenetic clades, one conserved in all chordates (the RNase Dre2 clade), and another fish-specific (the RNase Dre1 clade). RNase T2 enzymes carry out a housekeeping function; the zebrafish genome contains two RNase T2 genes, RNase Dre1 and RNase Dre2. These genes are part of two phylogenetic clades, one conserved in all chordates (the RNase Dre2 clade), and another fish-specific (the RNase Dre1 clade). RNase T2 enzymes carry out a housekeeping function; the zebrafish genome contains two RNase T2 genes, RNase Dre1 and RNase Dre2. These genes are part of two phylogenetic clades, one conserved in all chordates (the RNase Dre2 clade), and another fish-specific (the RNase Dre1 clade). RNase T2 enzymes carry out a housekeeping function
physiological function
RNaseLER represents a constitutively expressed gene with a cell-specific role in stomata and trichomes and no involvement in stress responses
physiological function
-
RNS2, an intracellular RNase T2 from Arabidopsis thaliana, is essential for normal ribosomal RNA recycling. RNS2 is part of a process that degrades rRNA to recycle its components
physiological function
-
ACTIBIND inhibits the clonogenicity and invasiveness of various tumors in culture and in mouse models. ACTIBIND disrupts the fine actin networks at the interior of colon cancer cells. Interaction of RNaseT2 proteins with the actin cytoskeleton provides a possible mechanism for RNase-independent cytotoxicity
physiological function
-
the envelope glycoprotein, termed Erns, has an RNaseT2 domain and ribonuclease activity, and is secreted by infected cells, the RNaseT2 protein induces cytotoxicity against host lymphocytes, but not epithelial cells, of various host species, and modulates host immune cell function
physiological function
-
the envelope glycoprotein, termed Erns, has an RNaseT2 domain and ribonuclease activity, and is secreted by infected cells, the RNaseT2 protein induces cytotoxicity against host lymphocytes, but not epithelial cells, of various host species, and modulates host immune cell function
physiological function
-
RNaseT2 protein secreted by the purine auxotroph Entamoeba histolytica might function in scavenging purines from this amoeba's host
physiological function
-
RNaseT2 omega-1 is the major component in priming dendritic cells for Th2 polarization of CD4+ T cells during infection, a process depending on the RNase activity of omega-1
physiological function
-
ribonuclease T2 is known to play a role in senescence in plants and possibly mammalian cells and may be an important tumor suppressor
physiological function
-
the ribonuclease RNase L is activated by the binding to 2'-5'-oligoadenylates and it proceeds to cleave single-stranded RNA molecules, ultimately leading to apoptosis of the virally infected cell
physiological function
-
interferon-inducible 2',5'-oligoadenylate-dependent ribonuclease L is a uniquely regulated endoribonuclease, a key player in the innate antiviral immune defense mechanismsof mammalian cells induced by interferons. The enzyme might have more general cellular functions through protein-protein interactions in the spleen for immune response in mammals. Cellular enzyme-interacting proteins from spleen are fibronectin precursor, beta-actin, troponin I, myosin heavy chain 9 (non-muscle), growth-arrest specific protein 11, clathrin light chain B, a putative uncharacterized protein (Ricken cDNA 8030451F13) isoform (CRA d) and alanyl tRNA synthetase
physiological function
-
RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides and also possess antitumorigenic and antiangiogenic activities. The enzyme binds actin and interferes with the cytoskeletal network structure, thereby inhibiting cell motility and invasiveness in cancer and in endothelial cells. Two structural elements create the binding site for actin, that is composed of one cysteine residue and one conserved amino acid region. The actin binding sites possibly interfere with the cytoskeleton network structure and as such may be responsible for the antitumorigenic and antiangiogenic activities of the enzyme
physiological function
-
RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides and also possess antitumorigenic and antiangiogenic activities. The enzyme binds actin and interferes with the cytoskeletal network structure, thereby inhibiting cell motility and invasiveness in cancer and in endothelial cells. Two structural elements create the binding site for actin, that is composed of one cysteine residue and one conserved amino acid region. The actin binding sites possibly interfere with the cytoskeleton network structure and as such may be responsible for the antitumorigenic and antiangiogenic activities of the enzyme. The enzyme inhibits human umbilical vein endothelial cell tube formation
physiological function
-
the 2',5'-oligoadenylate/RNase L system is a RNA virus-activated host RNase pathway that disposes of or processes viral and cellular single-stranded RNAs. Activation of RNase L during viral infections induces autophagy, autophagy induction by RNase L modulates viral growth
physiological function
-
direct activation of the enzyme by transfection with 2',5'-oligoadenylate induces IFN-beta in embryonic fibroblasts but not in macrophages, RNA damage from the enzyme in virus-infected macrophages is likely responsible for reducing IFN-beta production. Apoptosis is known to occur in cells that sustain high levels of RNA damage due to RNase L enzyme activity
physiological function
-
RNase L is an ankyrin repeat domain-containing dual endoribonuclease-pseudokinase that is activated by unusual 2',5'-oligoadenylate second messengers and impedes viral infections in higher vertebrates. The enzyme is important in interferon-regulated antiviral innate immunity. Molecular basis for the regulation of the enzyme's antiviral function, overview
physiological function
-
RNase L is an ankyrin repeat domain-containing dual endoribonuclease-pseudokinase that is activated by unusual 2',5'-oligoadenylate second messengers and impedes viral infections in higher vertebrates. The enzyme is important in interferon-regulated antiviral innate immunity. Molecular basis for the regulation of the enzyme's antiviral function, overview
physiological function
-
the enzyme might function as a suppressor of structurally distinct retrotransposons, endogenous RNase L restricts L1 retrotransposition, overview. Wild-type enzyme, but not enzyme mutant R667A, prevents formation of LINE-1 cytoplasmic foci
physiological function
-
RNase X25 enzyme has a housekeeping role in recycling RNA and in stress responses, it is the major contributor of ribonuclease activity in flies, correlation between induction of RNase X25 expression and autophagy
physiological function
A3M929
the enzyme is a positive regulator of Acinetobacter baumannii's ability to colonize inanimate surfaces and motility
physiological function
-
the enzyme is a positive regulator of Acinetobacter baumannii's ability to colonize inanimate surfaces and motility
-
physiological function
-
RNase X25 enzyme has a housekeeping role in recycling RNA and in stress responses, it is the major contributor of ribonuclease activity in flies, correlation between induction of RNase X25 expression and autophagy
-
physiological function
-
interferon-inducible 2',5'-oligoadenylate-dependent ribonuclease L is a uniquely regulated endoribonuclease, a key player in the innate antiviral immune defense mechanismsof mammalian cells induced by interferons. The enzyme might have more general cellular functions through protein-protein interactions in the spleen for immune response in mammals. Cellular enzyme-interacting proteins from spleen are fibronectin precursor, beta-actin, troponin I, myosin heavy chain 9 (non-muscle), growth-arrest specific protein 11, clathrin light chain B, a putative uncharacterized protein (Ricken cDNA 8030451F13) isoform (CRA d) and alanyl tRNA synthetase
-
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
comparisons of basic structure and function of RNaseT2 family members and their biological roles. Ribonucleases of the T2 family are transferase-type RNases and are classified by their similarity to the RNase T2 protein from Aspergillus oryzae
additional information
-
a reduction in the level of RNase T2 by Tax may play a role in adult T-cell leukemia, ATL, development, one of the primary diseases caused by human T cell leukemia virus type 1, HTLV-1, infection, ability of the viral protein to directly deregulate expression of specific cellular genes through interactions with numerous transcriptional regulators, e.g. the virally-encoded Tax protein, overview. Tax is renriched at the RNASET2 gene
additional information
-
the kinase-like region is required for the ribonuclease activity of the enzyme
additional information
-
the enzyme catalytic site, which is responsible for RNA degradation is composed of residues His51, His110, His115, Glu111, Trp54, Asp56, and Tyr62 which are involved in binding the target base. These residues are located on the surface of the molecule, thereby creating a cavity for the substrate
additional information
-
involvement of the pseudokinase domain of the enzyme activator sensing, nucleotide binding, dimerization, and ribonuclease functions
additional information
-
involvement of the pseudokinase domain of the enzyme activator sensing, nucleotide binding, dimerization, and ribonuclease functions
additional information
enzyme mode of action independent of its enzymatic activity, overview. The enzyme has four disulfide bridges, connecting cysteine residues 48/55, 75/121, 184/241 and 202/213, its catalytic site comprises residues His65, His113, Glu114, Lys117 and His118
additional information
structure-function analysis, overview. The KH/KH and kinase extension nuclease (KEN)/KEN interfaces are important in 2',5'-oligoadenylate-dependent enzyme activation
additional information
-
enzyme Rny1p requires entering into the endoplasmic reticulum first to become active and uses the adaptor protein Erv29p for packaging into COPII vesicles and transport to the Golgi apparatus
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2',3'-cyclic NMP + H2O
3'(2')-NMP
-
slower side reaction, intrinsic cyclic nucleotide phosphodiesterase activity
-
-
?
nucleotidyl-3',5'-nuceotide + H2O
2',3'-cyclic NMP + 3'(2')-NMP
-
determination of base specificity
-
-
?
RNA
?
-
acetate buffer pH 5.0 or Tris-HCl pH 7.5, 37 °C, 5 min incubation
-
-
?
RNA + H2O
2',3'-cyclic NMP + 3'(2')-NMP
-
high-molecular weight fraction of RNA from Torula yeast, typeII-S
2',3'-cyclic NMPs are are further hydrolyzed in a side reaction
-
?
RNA + H2O
5'-phosphomononucleotides
-
hydrolyzes in 3'- to 5'-direction, hydrolyzes single stranded RNA
-
?
poly-8 adenylic acid
AMP + ?
-
pH 8, 1 mM MgCl2, incubation at 30°C for 5 min
-
-
?
poly-8 adenylic acid
AMP + ?
-
pH 8, 1 mM MgCl2, incubation at 30°C for 5 min
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
-
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
two-stage endonucleolytic cleavage to 3'-phosphomononucleotides and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates, first step reversible cleavage of phosphodiester bond between 3'-adenylic acid group and 5'-hydroxyl group at adjacent nucleotides in RNA chain with formation of nucleoside 2',3'-cyclic phosphates and oligonucleotides with 2',3'-cyclic phosphate at 3'-terminal, second step: hydrolysis of terminal cyclic phosphate groups with formation of corresponding 3'-phosphates, no base specificity
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
preference for adenylic acid linkages in RNA
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
rates of release of 2',3'-cyclic nucleotides in decreasing order: guanylic acid, adenylic acid, cytidylic acid, uridylic acid
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
release rates in decreasing order: GMP, UMP, AMP, CMP
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
2',3'-cyclic nucleotide intermediates
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
release rates in order 3'-UMP, 3'-GMP, 3'-AMP
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
poly(A), poly(I), poly(C), poly(U)
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
polyguanylic acid and duplexes of synthetic homopolymers less sensitive
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
preference for pC-purine bonds
-
-
?
RNA + H2O
?
-
RNase L cleaves RNAs predominantly after single-stranded UA and UU dinucleotides
-
-
?
RNA + H2O
nucleoside 3'-phosphates + 3'-phosphooligonucleotides
-
5S rRNA and tRNA from Escherichia coli
-
-
?
RNA + H2O
nucleoside 3'-phosphates + 3'-phosphooligonucleotides
-
5S rRNA and tRNA from Escherichia coli
-
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
from yeast
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
squid
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
-
-
via oligonucleotides or mononucleotides with 2',3'-cyclic phosphate at the 3'-side
-
?
additional information
?
-
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
-
additional information
?
-
-
the enzyme ACTIBIND is able to bind actin in vitro
-
-
-
additional information
?
-
-
transphosphorylation of adenylyl (3'-5') uridine and adenosine 3'-(1-naphthylphosphate)
-
-
-
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
-
additional information
?
-
-
RNase degrades uracil containing nucleic acids only
-
-
-
additional information
?
-
-
the enzyme protects the seed from pathogens
-
-
-
additional information
?
-
-
assay substrate is Torula yeast RNA
-
-
-
additional information
?
-
-
assay substrate is Torula yeast RNA
-
-
-
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
-
additional information
?
-
-
the enzyme ceases degradation when it approaches a double stranded region, the enzyme also cannot digest stable, helical regions of RNA
-
-
-
additional information
?
-
-
tRNAs that contains the hypermodified nucleoside queuosine, Q, at the wobble position
-
-
-
additional information
?
-
-
two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
-
-
-
additional information
?
-
-
enzyme concentration in plasma is increased in case of impaired glomerular filtration rate of the kidney, patients suffering chronic renal insufficiency accumulate the enzyme in the plasma low molecular weight fraction
-
-
-
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
-
additional information
?
-
cleavage of biological targets by the enzyme with site selection in mammalian ribosomes and hepatitis C virus RNA, overview
-
-
-
additional information
?
-
-
RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides
-
-
-
additional information
?
-
-
the enzyme cleaves single-stranded RNA molecules
-
-
-
additional information
?
-
-
the enzyme is active on rRNA, rRNA cleavage products are generated from intact ribosomes in ovarian cancer Hey1b cells
-
-
-
additional information
?
-
-
assay substrate is 32P-labeled synthetic substrate r(C11U2C7)
-
-
-
additional information
?
-
the enzyme cleaves 3' of UN sequences, RNA sequence recognition involves the KEN domain homodimer, RNA cleavage is carried out by the symmetry-related histidine H672 provided by homodimerization, a single H672 residue per a KEN/KEN dimer is necessary and sufficient for RNA cleavage, overview. With Angptl3 mRNA as substrate, RIDD cleavage sites and the consensus UN-N are utilized by RNase L, Cyp1 mRNAs and pre-mir-17microRNA are all cleaved at UG-C sites
-
-
-
additional information
?
-
-
the enzyme protects the seed from pathogens
-
-
-
additional information
?
-
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
-
additional information
?
-
-
the enzyme protects the seed from pathogens
-
-
-
additional information
?
-
-
enzyme preferentially cleaves the 5'-side of uridine, Asn71 and Leu73 are involved in substrate specificity
-
-
-
additional information
?
-
-
the enzyme serves as a self-incompatibility factor, a mechanism that prevents pollen from one flower from fertilizing other flowers of the same plant
-
-
-
additional information
?
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
-
additional information
?
-
-
induced upon tobacco mosaic virus infection, structure determined, substrate-binding sites studied with nucleoside monophosphates at concentrations between 1 and 10 mM followed by crystallization
-
-
-
additional information
?
-
-
the enzyme confers hypersensitive response and aquired resistance to pathogens
-
-
-
additional information
?
-
-
RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides
-
-
-
additional information
?
-
-
subsite base specificities at the B1 and B2 site of wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
-
subsite base specificities at the B1 and B2 site of wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
-
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
-
additional information
?
-
-
besides other physiological functions in leaf and flower senescence and response to plant hormones, phosphate starvation, and wounding, the enzymes play a role in self-incompatibility cell-to-cell interactions
-
-
-
additional information
?
-
-
RNase LX is related to RNA metabolism in the final stage of senescence, all enzyme forms are related in phosphate remobilization
-
-
-
additional information
?
-
-
enzymes show preference for release of guanine mononucleotides from diribonucleoside monophosphates or RNA, preference in descending order is G, A, U, C
-
-
-
additional information
?
-
induced expression upon phosphate-starvation, tissue-specific expression patterns in roots analyzed, role during the phosphate starvation response suggested
-
-
-
additional information
?
-
-
induced expression upon phosphate-starvation, tissue-specific expression patterns in roots analyzed, role during the phosphate starvation response suggested
-
-
-
additional information
?
-
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
RNA + H2O
?
-
RNase L cleaves RNAs predominantly after single-stranded UA and UU dinucleotides
-
-
?
additional information
?
-
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
-
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
-
additional information
?
-
-
RNase degrades uracil containing nucleic acids only
-
-
-
additional information
?
-
-
the enzyme protects the seed from pathogens
-
-
-
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
-
additional information
?
-
-
tRNAs that contains the hypermodified nucleoside queuosine, Q, at the wobble position
-
-
-
additional information
?
-
-
two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
-
-
-
additional information
?
-
-
enzyme concentration in plasma is increased in case of impaired glomerular filtration rate of the kidney, patients suffering chronic renal insufficiency accumulate the enzyme in the plasma low molecular weight fraction
-
-
-
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
-
additional information
?
-
Q05823
cleavage of biological targets by the enzyme with site selection in mammalian ribosomes and hepatitis C virus RNA, overview
-
-
-
additional information
?
-
-
RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides
-
-
-
additional information
?
-
-
the enzyme cleaves single-stranded RNA molecules
-
-
-
additional information
?
-
-
the enzyme is active on rRNA, rRNA cleavage products are generated from intact ribosomes in ovarian cancer Hey1b cells
-
-
-
additional information
?
-
-
the enzyme protects the seed from pathogens
-
-
-
additional information
?
-
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
-
additional information
?
-
-
the enzyme protects the seed from pathogens
-
-
-
additional information
?
-
-
the enzyme serves as a self-incompatibility factor, a mechanism that prevents pollen from one flower from fertilizing other flowers of the same plant
-
-
-
additional information
?
-
Q9SSV1
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
-
additional information
?
-
-
the enzyme confers hypersensitive response and aquired resistance to pathogens
-
-
-
additional information
?
-
-
RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides
-
-
-
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
-
additional information
?
-
-
the enzyme catalyzes the cleavage of ssRNA through a 2',3'-cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3' phosphate group
-
-
-
additional information
?
-
-
besides other physiological functions in leaf and flower senescence and response to plant hormones, phosphate starvation, and wounding, the enzymes play a role in self-incompatibility cell-to-cell interactions
-
-
-
additional information
?
-
-
RNase LX is related to RNA metabolism in the final stage of senescence, all enzyme forms are related in phosphate remobilization
-
-
-
additional information
?
-
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
additional information
-
Mg2+ and ATP or ADP protect the enzyme from proteolytic cleavage
additional information
no significant inhibitory effect of cobalt, nickel or magnesium at 50 mM concentration
additional information
-
RNases LE, LX and LV-3 do not require divalent cations
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
protein Im5
-
immunity protein, in the study different mutants of Im5 are investigated
-
diethyl dicarbonate
-
above pH 6.0, no inactivation in presence of 3'-AMP
iodoacetamide
-
irreversible inhibition at pH 5.0, modification site is one of the two catalytic His residues
iodoacetamide
-
irreversible inhibition at pH 5.0, modification site is one of the two catalytic His residues
iodoacetamide
-
irreversible inhibition at pH 5.0, modification site is one of the two catalytic His residues
iodoacetate
-
irreversible inhibition at pH 5.0, modification site is one of the two catalytic His residues
iodoacetate
-
irreversible inhibition at pH 5.0, modification site is one of the two catalytic His residues
iodoacetate
-
irreversible inhibition at pH 5.0, modification site is one of the two catalytic His residues
additional information
-
inhibitory effect of mononucleotide phosphates in descending order 2'-AMP, 2'-GMP, 3'-AMP, 2'-CMP, 2'(3')-UMP
-
additional information
-
inhibitory effect of mononucleotide phosphates in descending order 2'-AMP, 2'-GMP, 3'-AMP, 2'-CMP, 2'(3')-UMP
-
additional information
-
inhibitory effect of mononucleotide phosphates in descending order 2'-AMP, 2'-GMP, 3'-AMP, 2'-CMP, 2'(3')-UMP
-
additional information
-
no effect of 2.5 mM EDTA, no product inhibition
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2',5'-linked oligoadenylates
two different binding sites in the enzyme's ANK domain and a third site in the N lobe of the KH domain, sensing mechanism, structure-function analysis, overview. The KH/KH and kinase extension nuclease (KEN)/KEN interfaces are important in 2',5'-oligoadenylate-dependent enzyme activation
-
2'-5'-linked oligoadenylates
-
natural 2'-5'-linked tetraadenylates and three tetramers with 3'-end AMP units replaced with ribo-, arabino- and xylo-configured phosphonate analogues of AMP are enzyme activators with equal potency. The enzyme is activated by the binding of 2'-5'-linked oligoadenylates to the N-terminal ankyrin repeat domain, which causes the inactive monomer to form a catalytically active homodimer
-
2'-5'-oligoadenylate
-
short polyadenylate molecules that are connected by unique 2'-5' linkages, collectively referred to as 2-5A. 2-5A induces dimerization via the ANK domain and this dimerization correlates with activation of ribonuclease activity
citrate
-
25 mM sodium citrate buffer results in 170% activity compared to 100% activity in sodium acetate buffer, both pH 5.6
phosphate
-
25 mM sodium phosphate buffer results in 153% activity compared to 100% activity in sodium acetate buffer, both pH 5.6
viral dsRNA
-
viral dsRNA provokes the synthesis of 2'-5' oligoadenylate, 2-5A, binding of 2-5A to ankyrin repeats of monomeric RNase L leads to RNase L dimerization and activation
-
2',5'-Oligoadenylate
-
mediates the enzyme activity, absolutely required for activity
2',5'-Oligoadenylate
-
the enzyme's pseudokinase domain is involved in the natural activator sensing, binding site and structure, modeling, overview. Quantitative determination of specific binding of the full-length enzyme and of isolated enzyme ANK domain to immobilized biotinylated 2',5'-oligoadenylate
2',5'-Oligoadenylate
-
binds to and activates the enzyme. It is produced in response to viral double-stranded RNA by the 2',5'-oligoadenylate synthetase
2',5'-Oligoadenylate
-
the enzyme's pseudokinase domain is involved in the natural activator sensing, binding site and structure, modeling, overview. Quantitative determination of specific binding of the full-length enzyme and of isolated enzyme ANK domain to immobilized biotinylated 2',5'-oligoadenylate
additional information
-
EDTA activates soluble enzyme, no effect on immobilized
-
additional information
-
a dephosphorylated form of 2',5'-oligoadenylate does not activate RNase L
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
RNA: 555 mg/ml soluble enzyme, 266 mg/ml immobilized enzyme
-
additional information
additional information
-
pH-dependence of Km, 2 kinetically distinct forms
-
additional information
additional information
-
Km values for mutant enzymes with diverse dinucleotide substrates, overview
-
additional information
additional information
-
Km values for mutant enzymes with diverse dinucleotide substrates, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pH-dependence of turnover-number, 2 kinetically distinct forms
-
additional information
additional information
-
wild-type and mutant enzymes
-
additional information
additional information
-
consists of seven helices and seven beta strands, determined by crystallization
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1600
additional information
additional information
-
enzyme levels at different kidney glomerular filtration rates of blood
additional information
determined by total RNase activity and in-gel activity assay
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
5.5
6 - 6.3
-
hydrolysis of various nucleoside 2',3'-cyclic phosphates, degradation of 3'-nucleotide benzyl ester
6.5
7.4
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 5.5
-
pH 3.5, 5.5: about 70% of activity maximum, soluble and immobilized enzyme
3.5 - 6
-
pH 3.5: 80% of activity maximum, soluble and immobilized form, pH 6: soluble form 100%, immobilized form 90% of maximum acitivity
3.5 - 6.5
-
pH 3.5: about 20% of activity maximum, 6.5: less than 10% of activity maximum
additional information
additional information
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes; at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes; at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
additional information
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes; at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes; at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
additional information
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes; at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes; at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
additional information
-
at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes; at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes; at an acidic pH stronger activities in the 20-30 kDa range that may correspond to RNase T2 enzymes
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 70
40 - 70
-
40°C: about 60% of activity maximum, soluble and immobilized enzyme, 70°C: about 70% immobilized enzyme, 40% soluble enzyme, of activity maximum
40 - 70
-
40°C: 100% activity of immobilized enzyme, 70°C: 20% of maximum activity of immobilized enzyme
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
-
about, RNase LV-1, isoelectric focusing; about, RNase LV-2, isoelectric focusing; about, RNase LX, isoelectric focusing
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
RNaseLE transcript accumulation occurs preferentially upon wounding
additional information
-
Takadiastase powder
-
transfected with pcDNA3 vectors to establish a cell line overexpressing wild-type RNase L, with a dominant negative mutation, and control HeLa cells carrying the vector alone
-
e.g. ATCC CCL-2 and S3, express normal enzyme level, while strain HeLa-M is defective in RNase L expression
meristematic zone at root tip and elongation zone at root tip
additional information
-
the enzyme is the main endoribonuclease activity in plant cells
additional information
RNase Dre1 is absent from liver; RNase Dre1 is absent from liver
additional information
RNase Dre1 is absent from liver; RNase Dre1 is absent from liver
additional information
RNase Dre1 is absent from liver; RNase Dre1 is absent from liver
additional information
-
RNase Dre1 is absent from liver; RNase Dre1 is absent from liver
additional information
-
rnaset2 is expressed ubiquitously in zebrafish embryos and adults from conception
additional information
-
developmental profile of Drosophila melanogaster enzyme activities, overview
additional information