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2',3'-5-NO3-Up + H2O
?
-
-
-
-
?
2',3'-cAMP + H2O
?
-
-
-
-
?
2',3'-cGMP + H2O
?
-
-
-
-
?
2',3'-Cp + H2O
?
-
-
-
-
?
2',3'-cyclic NMP + H2O
3'(2')-NMP
-
slower side reaction, intrinsic cyclic nucleotide phosphodiesterase activity
-
-
?
2',3'-mUp + H2O
?
-
-
-
-
?
2',3'-Up + H2O
?
-
-
-
-
?
5'-CCCCACCACCAUCACUU-3'
?
-
37°C, single stranded 17-mer
-
-
?
adenosine-3'-(1-naphthyl)phosphate + H2O
?
-
-
-
-
?
adenylyl (3'-5')uridine + H2O
?
-
-
-
-
?
ApA + H2O
AMP + adenosine
-
-
-
-
?
ApC + H2O
AMP + cytosine
-
-
-
-
?
ApG + H2O
AMP + guanosine
-
-
-
-
?
ApU + H2O
AMP + uridine
-
-
-
-
?
CpA + H2O
CMP + adenosine
-
-
-
-
?
CpC + H2O
CMP + cytidine
-
-
-
-
?
CpG + H2O
CMP + guanosine
-
-
-
-
?
CpU + H2O
3'-CMP + uridine
-
-
-
-
?
cytidylyl-3',5'-uridine
?
37°C, pH 5.5
-
-
?
GpA + H2O
GMP + adenosine
GpC
?
-
pH 5.0, 22°C
-
-
?
GpC + H2O
GMP + cytosine
-
-
-
-
?
GpG + H2O
GMP + guanosine
-
best substrate
-
-
?
GpU + H2O
GMP + uridine
-
-
-
-
?
nucleotidyl-3',5'-nuceotide + H2O
2',3'-cyclic NMP + 3'(2')-NMP
-
determination of base specificity
-
-
?
poly-8 adenylic acid
AMP + ?
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
3'-phosphomononucleotides
RNA + H2O
nucleoside 3'-phosphates + 3'-phosphooligonucleotides
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
UpA + H2O
UMP + adenosine
-
-
-
-
?
UpC + H2O
UMP + cytosine
-
-
-
-
?
UpG + H2O
UMP + guanosine
-
-
-
-
?
UpU + H2O
UMP + uridine
-
-
-
-
?
additional information
?
-
2',3'-cCMP + H2O
?
-
-
-
-
?
2',3'-cCMP + H2O
?
-
-
-
-
?
2',3'-cUMP + H2O
?
-
-
-
-
?
2',3'-cUMP + H2O
?
-
-
-
-
?
ApA + H2O
?
-
-
-
-
?
ApG + H2O
?
-
-
-
-
?
GpA + H2O
GMP + adenosine
-
-
-
-
?
GpA + H2O
GMP + adenosine
-
-
-
-
?
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
-
-
-
-
?
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
-
e.g.: homopolynucleotides
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
-
-
-
?
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
-
-
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
release rates in decreasing order: GMP, UMP, AMP, CMP
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
-
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
hydrolyzes in 3'- to 5'-direction, hydrolyzes single stranded RNA
-
?
RNA + H2O
3'-phosphomononucleotides
-
-
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
-
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
2',3'-cyclic nucleotide intermediates
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
-
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
release rates in order 3'-UMP, 3'-GMP, 3'-AMP
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
-
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
poly(A), poly(I), poly(C), poly(U)
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
-
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
tRNA
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
rRNA
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
polyguanylic acid and duplexes of synthetic homopolymers less sensitive
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
polyuridylic acid
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
polyadenylic acid
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
preference for pC-purine bonds
-
-
?
RNA + H2O
3'-phosphomononucleotides
-
polycytidylic acid
-
-
?
RNA + H2O
?
-
-
-
?
RNA + H2O
?
-
enzyme is responsible for degradation of mRNA
-
-
?
RNA + H2O
?
-
enzyme is responsible for degradation of mRNA
-
-
?
RNA + H2O
?
-
degradation of RNA
-
-
?
RNA + H2O
?
-
yeast RNA
-
-
?
RNA + H2O
?
-
RNase L cleaves RNAs predominantly after single-stranded UA and UU dinucleotides
-
-
?
RNA + H2O
?
-
from yeast
-
-
?
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
?
-
-
RNS2 is not an acidic RNase
-
-
?
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
?
-
-
base specificity
-
-
?
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
?
-
-
base specificity
-
-
?
additional information
?
-
-
RNase degrades uracil containing nucleic acids only
-
-
?
additional information
?
-
-
the enzyme protects the seed from pathogens
-
-
?
additional information
?
-
-
the enzyme protects the seed from pathogens
-
-
?
additional information
?
-
-
base specificity
-
-
?
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
?
-
-
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
?
-
substrate is yeast RNA
-
-
?
additional information
?
-
-
substrate is yeast RNA
-
-
?
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 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 is active on rRNA
-
-
?
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
?
-
-
base specificity
-
-
?
additional information
?
-
-
enzyme preferentially cleaves the 5'-side of uridine, Asn71 and Leu73 are involved in substrate specificity
-
-
?
additional information
?
-
-
transphosphorylation
-
-
?
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
?
-
-
base specificity
-
-
?
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
?
-
broad substrate specificity
-
-
?
additional information
?
-
-
broad substrate specificity
-
-
?
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
?
-
-
not: DNA
-
-
?
additional information
?
-
-
enzyme plays a role in self-incompatibility cell-to-cell interactions
-
-
?
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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 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 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
-
the enzyme belongs to the ribonuclease T2 family
evolution
-
the enzyme belongs to the the T2 family of RNases
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
-
the enzyme belongs to the ribonuclease T2 family
-
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
-
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
-
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
-
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
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
-
virus-mediated autophagy is deficient in cells lacking RNase L, overview
malfunction
depletion of CP1412 from soluble egg antigen impairs the ability of soluble egg antigen to induce M2 type polarization of RAW264.7macrophages. Immunizing mice with CP1412 induces high antibody titers, increased serum IL-4 and TGF-beta levels and splenic CD4 + CD25 + Foxp3 + T cells, downregulated serum IFN-gamma levels and alleviated the egg granuloma pathology of schistosome infection. In vitro stimulation by rSj CP1412 significantly increased CD4 + CD25 + Foxp3 + T cell numbers in splenocytes of healthy mice. The CP1412 protein with RNase activity inactivated by diethyldicarbonate fails to induce M2 surface marker CD206 expression in RAW264.7 macrophages
malfunction
knockdown of the protein in an immortalized mouse cell line TM6 decreases the degradation rate
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
-
cellular functions of RNase T2 proteins are associated with RNA recycling and maintenance of cellular homeostasis
metabolism
-
the interferon-inducible antiviral state is mediated in part by the 2',5'-oligoadenylate synthetase/RNase L system
metabolism
modulates inflammasome-dependent IL-1beta secretion in macrophages
metabolism
stimulating RAW264.7 macrophages with recombinant CP1412 raises the expression of CD206, Arg-1 and IL-10, which are related to M2 type macrophage differentiation. Stimulating dendritic cells with rSjCP1412 fails to induce their maturation, and the recombinant protein also inhibits LPS-stimulated dendritic cell maturation
metabolism
the enzyme degrades mitochondrial RNAs and it is also responsible for selective degradation of the cytosolic rRNAs on the outer membrane. The degradation activity also has a positive effect on nuclear transcription of rRNAs, suggesting a compensatory feedback mechanism, and affects protein translations in and out of mitochondria
metabolism
the enzyme degrades mitochondrial RNAs and it is also responsible for selective degradation of the cytosolic rRNAs on the outer membrane. The degradation activity also has a positive effect on nuclear transcription of rRNAs, suggesting a compensatory feedback mechanism, and affects protein translations in and out of mitochondria
metabolism
there is a possible link between the hypoxic state experienced by cancer cells and the expression level of RNASET2. A role of this gene as a stress-response factor is postulated
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
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
-
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
RNaseLER represents a constitutively expressed gene with a cell-specific role in stomata and trichomes and no involvement in stress responses
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
-
RNaseT2 protein secreted by the purine auxotroph Entamoeba histolytica might function in scavenging purines from this amoeba's host
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
-
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
-
the enzyme has a role in neural development
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
-
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
-
key enzyme in the defense system
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
-
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
-
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
-
the enzyme is a positive regulator of Acinetobacter baumannii's ability to colonize inanimate surfaces and motility
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
-
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
-
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
-
the enzyme is a positive regulator of Acinetobacter baumannii's ability to colonize inanimate surfaces and motility
-
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
-
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
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
-
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
-
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
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
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
-
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
-
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
-
the kinase-like region is required for the ribonuclease activity of the enzyme
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C184R
-
RNASET2C184R, harboring a missense mutation as identified from a patient with cystic leukoencephalopathy, signal is retained within the endoplasmic reticulum
T304A
-
naturally occuring mutation, inactivce mutant AO127. A mutation within codon 118 of the rnaset2 ORF creates a premature stop codon truncating the protein before its second conserved catalytic site, CAS II, resulting in loss of essential catalytic residues and results in a dramatic down-regulation of the rnaset2 messenger RNA
D201N
-
<0.2% wild-type activity
D207N
-
12% wild-type activity
D210N
-
<0.3% wild-type activity
F358A
-
209% wild-type activity
Y253A
-
26% wild-type activity
Y253A/F358A
-
12% wild-type activity
D209N
-
inactivates the enzyme without affecting RNA binding
-
K392R
-
the mutation in the kinase ATP binding site of the nezyme results in greatly impaired RNase activity
R163A
action potential aI clamp enzyme mutant, which shows reduced activity compared to the wild-type enzyme
R412A
KH/KH interface enzyme mutant, which shows reduced activity compared to the wild-type enzyme
R427A
activator recognition enzyme mutant, which shows reduced activity compared to the wild-type enzyme
A105L
significant loss of activity, significant decrease in thermostability
D107A
little effect on thermostability
E84A
-
site-directed mutagenesis, decreased kcat, 90% reduced activity compared to the wild-type enzyme
F102A
considerable less stable than the wild-type in guanidine-HCl, significant decrease in thermostability
F190A
significant decrease in thermostability
G127A
moderate decrease in thermostability
G144A
moderate decrease in thermostability
G173A
little effect on thermostability
H34A
-
site-directed mutagenesis, active site residue, inactive mutant
H83A
-
site-directed mutagenesis, decreased kcat, 80% reduced activity compared to the wild-type enzyme
H88A
-
site-directed mutagenesis, active site residue, inactive mutant
K87A
-
site-directed mutagenesis, decreased kcat, 45% reduced activity compared to the wild-type enzyme
L73A
-
site-directed mutagenesis, slightly increased catalytic efficiency and 14.5fold decreased binding affinity compared to the wild-type enzyme
N71T
-
site-directed mutagenesis, 2.3fold decreased catalytic efficiency and 7.0fold decreased binding affinity compared to the wild-type enzyme
P125A
moderate decrease in thermostability
R74S
-
site-directed mutagenesis, decreased catalytic efficiency and 0.8fold increased binding affinity compared to the wild-type enzyme
V165A
moderate decrease in thermostability
V72L
-
site-directed mutagenesis, catalytic efficiency and binding affinity similar to the wild-type enzyme
Y101A
considerable less stable than the wild-type in guanidine-HCl, significant decrease in thermostability
D51A
-
high activity toward polyI and polyC and reduced activity toward polyA and polyU
D51E
-
high activity toward polyI and polyC and reduced activity toward polyA and polyU
D51K
-
high activity toward polyI and polyC and reduced activity toward polyA and polyU
D51N
-
high activity toward polyI and polyC and reduced activity toward polyA and polyU
D51NW49F
-
preference for cytidylic acid
D51Q
-
high activity toward polyI and polyC and reduced activity toward polyA and polyU
D51S
-
high activity toward polyI and polyC and reduced activity toward polyA and polyU
D51SY57W
-
preference for guanylic acid
D51T
-
high activity toward polyI and polyC and reduced activity toward polyA and polyU
D51TW49F
-
preference for cytidylic acid
D51TY57W
-
preference for guanylic acid
F101A
-
site-directed mutagenesis, below 1% activity compared to the wild-type enzyme
F101I
-
site-directed mutagenesis, 3.8% activity compared to the wild-type enzyme
F101K
-
site-directed mutagenesis, below 1% activity compared to the wild-type enzyme
F101L
-
site-directed mutagenesis, 20% activity compared to the wild-type enzyme
F101Q
-
site-directed mutagenesis, below 1% activity compared to the wild-type enzyme
F101W
-
site-directed mutagenesis, 7% activity compared to the wild-type enzyme
Q32D
-
site-directed mutagenesis, 26% activity compared to the wild-type enzyme
Q32E
-
site-directed mutagenesis, 78% activity compared to the wild-type enzyme
Q32F
-
site-directed mutagenesis, 9.3% activity compared to the wild-type enzyme
Q32L
-
site-directed mutagenesis, 112% activity compared to the wild-type enzyme
Q32N
-
site-directed mutagenesis, 21% activity compared to the wild-type enzyme
Q32T
-
site-directed mutagenesis, 125% activity compared to the wild-type enzyme
Q32V
-
site-directed mutagenesis, 39% activity compared to the wild-type enzyme
W49A
-
greatly increased activity
W49I
-
greatly increased activity
W49Y
-
greatly increased activity
Y57A
-
more active toward RNA and less active toward XpGs
Y57F
-
greatly increased activity
Y57G
-
more active toward RNA and less active toward XpGs
Y57K
-
more active toward RNA and less active toward XpGs
Y57M
-
more active toward RNA and less active toward XpGs
Y57V
-
more active toward RNA and less active toward XpGs
N37Q/N70Q/N103Q/N123Q
-
site-directed mutagenesis of N-glycosylation sites, the mutant is mislocated to the vacuole
W399R
-
site-directed mutagenesis, the mutant is mislocated to the vacuole
P509L
-
mutant contains a reduced RNase activity, the spindle-kinetochore interaction is abnormal in mutant cells, associated with mitotic arrest at a pre-anaphase stage
T808A
-
mutant contains a reduced RNase activity
H109F
site-directed mutagenesis, 35% activity compared to the wild-type enzyme
H134F
site-directed mutagenesis, 49% activity compared to the wild-type enzyme
H39F
site-directed mutagenesis, conserved active site residue, 0.18% activity compared to the wild-type enzyme
H92F
site-directed mutagenesis, conserved active site residue, 0.21% activity compared to the wild-type enzyme
H97F
site-directed mutagenesis, conserved active site residue, 0.12% activity compared to the wild-type enzyme
K390R
-
the mutation in the kinase ATP binding site of the nezyme results in greatly impaired RNase activity
D209N
-
inactivates the enzyme without affecting RNA binding
D209N
-
catalytically inactive mutant, able to bind the substrate
D209N
-
<0.1% wild-type activity
H672N
catalytically inactive enzyme mutant
H672N
RNA cleavage enzyme mutant, which shows reduced activity compared to the wild-type enzyme. The H672N mutation eliminates the proton transfer but preserves the H-bonding and space-filling character of histidine. Thus, the H672N mutant interacts with RNA analogous to the wild-type protein but without cleaving the RNA. A single H672N mutant is a potent in trans activator for wild-type RNase L, whereas a double H672N mutant is inactive
R667A
-
dominant negative mutation
R667A
-
a catalytically inactive RNase L mutant
W49F
-
16% activity of native enzyme
W49F
-
higher preference toward pyrimidine bases
Y57W
-
greatly increased activity
Y57W
-
higher preference toward purine bases
additional information
-
transposon mutagenesis analysis of abiotic surface-colonization of wild-type and enzyme-deletion 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
additional information
-
transposon mutagenesis analysis of abiotic surface-colonization of wild-type and enzyme-deletion 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
-
additional information
-
alteration of the RNase I by mutantion of 3 amino acids to RNase M sequence and confer of enzyme properties, comparison of RNase M mutant strain activities
additional information
-
expression of the enzyme in transgenic Nicotiana alata plants allows the plants to accept pollen from another Nicotiana alata self-incompatible plant
additional information
-
in addition the selenomethionine-derivatized D209N protein is produced
additional information
-
alteration of the RNase I by mutantion of 3 amino acids to RNase M sequence and confer of enzyme properties, comparison of RNase M mutant strain activities
-
additional information
construction of enzyme comprising residues 21-719
additional information
-
construction of enzyme comprising residues 21-719
additional information
-
deletion mutant NDELTA385 is a constitutively active form of RNase L
additional information
-
generation of the truncated enzyme mutant RNase L(1-333) by insering a TEV cleavage site into the recombinant enzyme and cleaving it into two proteins, truncated enzyme comprising residues 432-741 shows proteolytic stability and no change in oligomeric state in the absence and presence ofMg2+ and ATP
additional information
-
transgenic plants expressing the Escherichia coli gene instead of the endogenous gene do not reject the pollen of another self-incompatibele Nicotiana alata plant
additional information
-
construction of enzyme mutants which possess designed substrate specificity, conversion of the base-nonspecific wild-type to base-specific mutants
additional information
-
the DELAT18N mutant lacking the 18 N-terminal amino acids of the signal peptide is catalytically inactive
additional information
transgenic Nicotiana benthamiana plants carrying the uidA reporter gene under the control of a 900-bp RNaseLER promoter sequence express the reporter gene predominantly in guard cells and trichomes
additional information
-
transgenic Nicotiana benthamiana plants carrying the uidA reporter gene under the control of a 900-bp RNaseLER promoter sequence express the reporter gene predominantly in guard cells and trichomes
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Uchida, T.; Egami, F.
Microbial ribonucleases with special reference to RNases T1, T2, N1, and U2
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
205-250
1971
Aspergillus oryzae
-
brenda
Nomachi, Y.; Komano, T.
Purification and some properties of two acid ribonucleases from the mycelia of Aspergillus niger
J. Gen. Appl. Microbiol.
26
375-385
1980
Aspergillus niger
-
brenda
Piedade, J.; Zilhao, R.; Arraiano, C.M.
Construction and characterisation of an absolute deletion mutant of Escherichia coli ribonuclease II
FEMS Microbiol. Lett.
127
187-194
1995
Escherichia coli
brenda
Coburn, G.A.; Mackie, G.A.
Overexpression, purification, and properties of Escherichia coli ribonuclease II
J. Biol. Chem.
271
1048-1053
1996
Escherichia coli
brenda
Inada, Y.; Watanabe, H.; Ohgi, K.; Irie, M.
Isolation, characterization, and primary structure of a base non-specific and adenylic acid preferential ribonuclease with higher specific activity from Trichoderma viride
J. Biochem.
110
896-904
1991
Trichoderma viride
brenda
Gurucharan Reddy, L.; Shankar, V.
Preparation and properties of RNase T2 immobilized on concanavalin A-sepharose
Appl. Biochem. Biotechnol.
22
237-246
1989
Aspergillus oryzae
brenda
Kawata, Y.; Sakiyama, F.; Hayashi, F.; Kyogoku, Y.
Identification of two essential histidine residues of ribonuclease T2 from Aspergillus oryzae
Eur. J. Biochem.
187
255-262
1990
Aspergillus oryzae
brenda
Kawata, Y.; Sakiyama, F.; Tamaoki, H.
Amino-acid sequence of ribonuclease T2 from Aspergillus oryzae
Eur. J. Biochem.
176
683-697
1988
Aspergillus oryzae
brenda
Kaiser, P.M.; Bonacker, L.; Witzel, H.; Holy, A.
Studies on the reaction mechanism of a ribonuclease II from Aspergillus oryzae
Hoppe-Seyler's Z. Physiol. Chem.
356
143-155
1975
Aspergillus oryzae
brenda
Uchida, T.; Egami, F.
The specificity of ribonuclease T2
J. Biochem.
61
44-53
1967
Aspergillus oryzae
brenda
Yasuda, T.; Inoue, Y.
Evidence for the presence of two kinetically distinct active forms of ribonuclease T2. The pH dependence of the steady-state kinetic parameter, kcat, for transphosphorylation of both a natural and a synthetic substrate
Eur. J. Biochem.
114
229-234
1981
Aspergillus oryzae
brenda
Klemer, A.; Kuennemeyer, H.M.; Matern, H.
Isolation and structure investigations on the ribonuclease T2 from Aspergillus oryzae, I.
Z. Naturforsch. B
36
1163-1168
1981
Aspergillus oryzae
-
brenda
Kanaya, S.; Uchida, T.
An affinity adsorbent, 5-adenylate-aminohexyl-sepharose. II. Purification and characterization of multi-forms of RNase T2
J. Biochem.
90
473-481
1981
Aspergillus oryzae
brenda
Irie, M.; Ohgi, K.; Iwama, M.
Photooxidation and carbethoxylation of a minor ribonuclease from Aspergillus saitoi
J. Biochem.
82
1701-1706
1977
Aspergillus phoenicis
brenda
Watanabe, H.; Ohgi, K.; Irie, M.
Primary structure of a minor ribonuclease from Aspergillus saitoi
J. Biochem.
91
1495-1509
1982
Aspergillus phoenicis
brenda
Irie, M.; Ohgi, K.
Further studies on the specificity of the minor ribonuclease from Aspergillus saitoi
J. Biochem.
80
39-43
1976
Aspergillus phoenicis
brenda
Ohgi, K.; Irie, M.
Purification and properties of a new ribonuclease from Aspergillus saitoi
J. Biochem.
77
1085-1094
1975
Aspergillus phoenicis
brenda
Shen, V.; Schlessinger, D.
RNases, I, II, and IV of Escherichia coli
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
15B
501-515
1982
Aspergillus phoenicis, Escherichia coli
-
brenda
Imada, A.; Hunt, J.W.; van de Sande, H.; Sinskey, A.J.; Tannenbaum, S.R.
Purification and properties of an intracellular ribonuclease from Candida lipolytica
Biochim. Biophys. Acta
395
490-500
1975
Yarrowia lipolytica
brenda
Pietrzak, M.; Cudny, H.; Maluszynski, M.
Purification and properties of two ribonucleases and a nuclease from barley seeds
Biochim. Biophys. Acta
614
102-112
1980
Hordeum vulgare
brenda
Shimada, H.; Inokuchi, N.; Oduwaki, H.; Koyama, T.; Irie, M.
Purification and characterization of a base non-specific and adenylic acid preferring ribonuclease from the fruit bodies of Lentinus edodes
Agric. Biol. Chem.
55
1167-1169
1991
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Homo sapiens, Rattus norvegicus
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Homo sapiens, Sus scrofa
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Homo sapiens (O00584), Homo sapiens
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Homo sapiens
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Phylogenetic analyses and characterization of RNase X25 from Drosophila melanogaster suggest a conserved housekeeping role and additional functions for RNase T2 enzymes in protostomes
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Drosophila melanogaster, Drosophila melanogaster w1118/w1118, Protostomia
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An ribonuclease T2 family protein modulates Acinetobacter baumannii abiotic surface colonization
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Acinetobacter baumannii, Acinetobacter baumannii 98-37-09
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Han, Y.; Donovan, J.; Rath, S.; Whitney, G.; Chitrakar, A.; Korennykh, A.
Structure of human RNase L reveals the basis for regulated RNA decay in the IFN response
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Homo sapiens (Q05823), Homo sapiens
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Golgi-mediated glycosylation determines residency of the T2 RNase Rny1p in Saccharomyces cerevisiae
Traffic
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Saccharomyces cerevisiae
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New insights into hypoxia-related mechanisms involved in different microvascular patterns of bronchopulmonary carcinoids and poorly differentiated neuroendocrine carcinomas. Role of ribonuclease T2 (RNASET2) and HIF-1alpha
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Homo sapiens (O00584)
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The Schistosoma mansoni T2 ribonuclease omega-1 modulates inflammasome-dependent IL-1beta secretion in macrophages
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Schistosoma mansoni (Q2Y2H5), Schistosoma mansoni
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Huang, J.; Liu, P.; Wang, G.
Regulation of mitochondrion-associated cytosolic ribosomes by mammalian mitochondrial ribonuclease T2 (RNASET2)
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Homo sapiens (C0HKG5), Mus musculus (C0HKG5), Mus musculus
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Ke, X.D.; Shen, S.; Song, L.J.; Yu, C.X.; Kikuchi, M.; Hirayama, K.; Gao, H.; Wang, J.; Yin, X.; Yao, Y.; Liu, Q.; Zhou, W.
Characterization of Schistosoma japonicum CP1412 protein as a novel member of the ribonuclease T2 molecule family with immune regulatory function
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Schistosoma japonicum (Q6PYW1), Schistosoma japonicum
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