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Information on EC 4.6.1.24 - ribonuclease T1
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4.6.1.24 ribonuclease T1Specify your search results
Word Map
- 4.6.1.24
- pancreatic
- lysozyme
-
refolding
- amide
- trna
- nucleic
-
alpha-helix
-
angiogenin
-
single-stranded
- dnase
-
ribonucleolytic
-
isomerization
- guanosine
- cytidine
- ribonucleoproteins
- myoglobin
-
subsite
-
two-state
-
globular
- amyloliquefaciens
-
ribonucleic
-
enthalpy
-
seminal
-
native-like
- s-protein
-
phosphodiester
- polynucleotide
- intermedius
-
micrococcal
-
transesterification
- polycation
- nucleases
-
monolith
- oligoribonucleotides
- trnaphe
-
anticodon
- alpha-lactalbumin
- dinucleoside
-
domain-swapped
- beta-lactoglobulin
-
eosinophil-derived
-
rna-protein
- 3'-phosphate
-
3'-terminal
- polyu
- pumilus
-
dimethacrylate
- biotechnology
- drug development
- polyribonucleotides
- medicine
-
transphosphorylation
-
burial
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
=
+
[RNA] containing guanosine
+
=
an [RNA fragment]-3'-guanosine-3'-phosphate
+
a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
Synonyms
rnase a, ribonuclease a, barnase, rnase t1, ribonuclease t1, binase, rnase g, rnase sa, rnase ms, ribonuclease sa, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aspergillus oryzae ribonuclease
-
-
-
-
barnase
Binase
EC 2.7.7.26
-
-
formerly
-
EC 3.1.27.3
-
-
formerly
-
EC 3.1.4.8
-
-
formerly
-
Gln25-RNase T1
-
two isoforms of RNase T1 exist in nature: one has Gln and the other Lys at position 25
Guanyl-specific RNase
-
-
-
-
Guanyloribonuclease
-
-
-
-
Nuclease, guanyloribo-
-
-
-
-
Nuclease, ribo-, Aspergillus oryzae
-
-
-
-
ribonuclease
Ribonuclease C2
-
-
-
-
Ribonuclease Ch
-
-
-
-
Ribonuclease F1
-
-
-
-
Ribonuclease guaninenucleotido-2'-transferase (cyclizing)
-
-
-
-
Ribonuclease N1
-
-
-
-
Ribonuclease N3
-
-
-
-
Ribonuclease PP1
-
-
-
-
Ribonuclease SA
ribonuclease T1
Ribonuclease U1
-
-
-
-
RNase E/G
RNase F1
-
-
-
-
RNase Fl1
-
-
-
-
RNase Fl2
-
-
-
-
RNase G
RNase Ms
-
-
-
-
RNase N1
RNase N2
-
-
-
-
RNase Pb1
-
-
-
-
RNase Pc
-
-
-
-
RNase Po1
RNase Sa
RNase Sa3
-
-
-
-
RNase St
-
-
-
-
RNase T1
RNase Th1
-
-
-
-
RNase U1
-
-
-
-
additional information
Binase
-
-
-
-
Ribonuclease SA
-
-
-
-
RNase G
-
-
-
-
RNase N1
-
-
-
-
RNase Po1
-
-
-
-
RNase Sa
-
-
-
-
RNase T1
-
-
-
-
RNase T1
-
-
additional information
-
the enzyme belongs to the superfamily of microbial N1/T1 RNases
additional information
-
the enzyme belongs to the superfamily of microbial N1/T1 RNases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[RNA fragment]-3'-guanosine-2',3'-cyclophosphate + H2O = [RNA fragment]-3'-guanosine-3'-phosphate
(1b)
-
-
-
[RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
[RNA] containing guanosine = [RNA fragment]-3'-guanosine-2',3'-cyclophosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
(1a)
-
-
-
[RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
mechanism
-
[RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
hydrolysis of the phosphodiester bonds of single-stranded RNA at the 3'-side of guanosine nucleotides occurs with high specificity
[RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
small single-domain protein of 104 amino acid residues that cleaves single-stranded RNA specifically at the 3'-side of guanine residues in a two-step mechanism
-
[RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
the conjugate base of the gamma-carboxyl group of Clu46 is required for tight binding of guanine and hypoxanthine moieties at the primary recognition site of the enzyme
-
[RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
the enzyme is composed of 104 amino acid residues and it cleaves single-stranded RNA specifically after guanosine residues to produce mono or oligo-ribonucleotides with terminal 3'-phosphate
-
[RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
the reaction is a transphosphorylation yielding a 2',3'-cyclophosphate. This cyclic intermediate is hydrolyzed by a water molecule to a 3'-phosphate in a separate step which is the reversal of the transphosphorylation. The transphosphorylation consists of a nucleophilic in-line inversion displacement at the phosphorous atom of the 5'-leaving group by the entering 2'-oxygen. Tyr38, His40, Glu58, His92 and Phe100 are involved in the catalysis of RNA degradation. During cyclization, Glu58 and His92 serve as the catalytic base and acid, respectively
-
[RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
the side chain carboxyl of Glu54 accepts a proton from the ribose 2'OH group and the protonated imidazole ring of His85 donates a proton to the leaving 5'O group. The positively charged side chain of Arg65 is to promote the formation of a negatively charged, pentacovalent intermediate state of the phosphate group
-
[RNA] containing guanosine + H2O = an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
overall reaction
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
9026-12-4
-
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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
adenylyl-3',5'-cytidine
adenosine-2',3'-cyclic phosphate + cytidine
-
ApC
-
-
?
guanosine-2',3'-cyclic phosphate + H2O
guanosine 3'-phosphate
-
hydrolysis
-
-
?
guanylyl(3',5') adenosine + H2O
?
shift in nucleotide conformational equilibrium contributes to increased rate of catalysis of guanylyl(3',5') adenosine 3'-monophosphate versus guanylyl(3',5') adenosine
-
-
?
guanylyl(3',5') adenosine 3'-monophosphate + H2O
?
shift in nucleotide conformational equilibrium contributes to increased rate of catalysis of guanylyl(3',5') adenosine 3'-monophosphate versus guanylyl(3',5') adenosine
-
-
?
guanylyl-3',5'-cytidine
guanosine-2',3'-cyclic phosphate + cytidine
-
Transphosphorylation reaction
-
-
?
guanylyl-3',5'-cytidine + H2O
guanosine 3'-phosphate + cytidine
-
GpC
-
-
?
guanylyl-3',5'-uridine
guanosine-2',3'-cyclic phosphate + uridine
-
Transphosphorylation reaction with GpU or the diastereomers resulting from thio-substitution of a nonbridging oxygen of GpU, RpGp(S)U and SpGp(S)U as substrates. SpGp(S)U is a very poor substrate for wild type enzyme
-
-
?
[RNA] containing guanosine + H2O
an [RNA fragment]-3'-guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA fragment]
-
energetics of ribonuclease catalysis
-
-
?
adenylyl-3',5'-cytidine + H2O
adenosine 3'-phosphate + cytidine
-
kcat/Km(GpC)/kcat/Km(ApC) is 284000 for wild-type enzyme, 195 for mutant enzyme E46N and 137 for mutant enzyme E46N/Y45W
-
-
?
adenylyl-3',5'-cytidine + H2O
adenosine 3'-phosphate + cytidine
kcat/Km(GpC)/kcat/Km(ApC) is 284000 for wild-type enzyme, and 39 for mutant enzyme K41E/Y42F/N43R/Y45W/E46N/W59Y (RNase T1-R2) and mutant enzyme K41E/Y42F/N43R/Y45W/E46N (RNase RV)
-
-
?
guanosine 2',3'-cyclic phosphate + H2O
guanosine-3'-phosphate
-
-
-
-
?
guanosine 2',3'-cyclic phosphate + H2O
guanosine-3'-phosphate
-
Ustilago sphaerogena, RNase U1
-
-
?
guanylyl-3',5'-cytidine + H2O
?
-
kcat/Km(GpC)/kcat/Km(ApC) is 284000 for wild-type enzyme, 195 for mutant enzyme E46N and 137 for mutant enzyme E46N/Y45W
-
-
?
guanylyl-3',5'-cytidine + H2O
?
kcat/Km(GpC)/kcat/Km(ApC) is 284000 for wild-type enzyme, and 39 for mutant enzyme K41E/Y42F/N43R/Y45W/E46N/W59Y (RNase T1-R2) and mutant enzyme K41E/Y42F/N43R/Y45W/E46N (RNase RV)
-
-
?
RNA + H2O
?
-
two-stage endonucleolytic cleavage to 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp with 2,3'-cyclic phosphate intermediates
-
-
?
RNA + H2O
?
-
identification of RNase T1 cleavage fragments of Bacillus megaterium ribosomal 5S RNA
-
-
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
essential requirements: keto group at 6 position, trivalent nitrogen at 7 position of purine base
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
essential requirements: keto group at 6 position, trivalent nitrogen at 7 position of purine base
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
first step (r): cleavage of internucleotide bonds between 3'-guanylic acid groups and the 5'-hydroxyl groups of the adjacent nucleotides with the intermediary formation of guanosine 2',3'-cyclic phosphate, second step (ir): hydrolysis of cyclic phosphate to produce 3'-guanylate
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
first step (r): cleavage of internucleotide bonds between 3'-guanylic acid groups and the 5'-hydroxyl groups of the adjacent nucleotides with the intermediary formation of guanosine 2',3'-cyclic phosphate, second step (ir): hydrolysis of cyclic phosphate to produce 3'-guanylate
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
specificity
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
specificity
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
RNA + H2O
Hydrolyzed RNA
-
-
3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp
?
single-stranded RNA + H2O
?
the enzyme specifically hydrolyzes single-stranded RNA at G sites. RNase T1 does not recognize sites containing 8-oxo-7,8-dihydroguanosine
-
-
?
single-stranded RNA + H2O
?
the enzyme specifically hydrolyzes single-stranded RNA at G sites. RNase T1 does not recognize sites containing 8-oxo-7,8-dihydroguanosine
-
-
?
additional information
?
-
-
synthesis of guanylylnucleosides, oligoguanylate, guanosine-containing oligonucleotides with (3'-5')phosphodiester bonds, synthetic reaction can lead to the formation of unnatural (2'-5')-phosphodiester bonds, not: DNA, L-guanosine 2',3'-cyclic phosphate, L-inosine 2',3'-cyclic phosphate
-
-
?
additional information
?
-
-
heteroduplex of ribooligonucleotides are substrates for the enzyme
-
-
?
additional information
?
-
-
the backbone dynamics of RNase T1, complexed with the productive substrate exo-cGPS isomer, in comparison to the RNase T1, complexed with the nonproductive substrate 3'GMP, is analyzed
-
-
?
additional information
?
-
-
the enzyme cleaves single-stranded RNA by catalyzing the hydrolysis of phosphodiester bonds specifically at the 3'-side of guanosine nucleotides
-
-
?
additional information
?
-
-
the enzyme hydrolyzes specifically the 3'-phosphodiester bond of guanylic acid in RNA, mechanism of interaction of RNase T1 with its substrates, overview. His40 and His92 are deduced to be involved in the active site, overview. Carboxymethylated-RNase T1 possesses almost the same binding ability toward guanosine as intact RNase T1, whereas the binding ability toward 2' or 3'-guanylic acid is considerably lowered by carboxymethylation of Glu58
-
-
?
additional information
?
-
-
barnase catalyses the overall hydrolysis of single-stranded RNA preferentially at guanylyl residues, yielding new guanosine 3'-phosphate and 5'-OH ends, in a two-step process with cleavage of the RNA chain by transesterification of a 5'-phosphoester bond to form a guanosine 2',3'-cyclic phosphate terminus in the first step, followed by its hydrolysis to a 3'-phosphate product in the second independent step
-
-
?
additional information
?
-
in vivo binase affects the quantity of proapoptotic and antiapoptotic mRNAs, as expression of the p53 and hSK4 genes is increased and expression of the bcl-2 gene is reduced
-
-
?
additional information
?
-
-
in vivo binase affects the quantity of proapoptotic and antiapoptotic mRNAs, as expression of the p53 and hSK4 genes is increased and expression of the bcl-2 gene is reduced
-
-
?
additional information
?
-
-
binase catalyses the overall hydrolysis of single-stranded RNA preferentially at guanylyl residues, yielding new guanosine 3'-phosphate and 5'-OH ends, in a two-step process with cleavage of the RNA chain by transesterification of a 5'-phosphoester bond to form a guanosine 2',3'-cyclic phosphate terminus in the first step, followed by its hydrolysis to a 3'-phosphate product in the second independent step
-
-
?
additional information
?
-
-
endonucleolytic activity is assayed using derivates of BR13, 5'-GGGACAGUAUUUG-3', a model oligonucleotide substrate for studies of RNase E and RNase G
-
-
?
additional information
?
-
assay substrate is commercial yeast RNA, rates of release of GMP and cGMP show base specificity of enzyme mutant D19N/D22N/E25Q/D31N/D38N/E50Q/E57Q/E76Q/D77N/D79N/E92Q/D93N
-
-
?
additional information
?
-
-
assay substrate is commercial yeast RNA, rates of release of GMP and cGMP show base specificity of enzyme mutant D19N/D22N/E25Q/D31N/D38N/E50Q/E57Q/E76Q/D77N/D79N/E92Q/D93N
-
-
?
additional information
?
-
assay substrate is commercial yeast RNA, the enzyme is a guanylic acid-specific RNase
-
-
?
additional information
?
-
-
assay substrate is commercial yeast RNA, the enzyme is a guanylic acid-specific RNase
-
-
?
additional information
?
-
the enzyme is a guanylic acid-specific ribonuclease
-
-
?
additional information
?
-
-
the enzyme is a guanylic acid-specific ribonuclease
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
RNA + H2O
?
-
two-stage endonucleolytic cleavage to 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Gp with 2,3'-cyclic phosphate intermediates
-
-
?
additional information
?
-
-
barnase catalyses the overall hydrolysis of single-stranded RNA preferentially at guanylyl residues, yielding new guanosine 3'-phosphate and 5'-OH ends, in a two-step process with cleavage of the RNA chain by transesterification of a 5'-phosphoester bond to form a guanosine 2',3'-cyclic phosphate terminus in the first step, followed by its hydrolysis to a 3'-phosphate product in the second independent step
-
-
?
additional information
?
-
-
binase catalyses the overall hydrolysis of single-stranded RNA preferentially at guanylyl residues, yielding new guanosine 3'-phosphate and 5'-OH ends, in a two-step process with cleavage of the RNA chain by transesterification of a 5'-phosphoester bond to form a guanosine 2',3'-cyclic phosphate terminus in the first step, followed by its hydrolysis to a 3'-phosphate product in the second independent step
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H+
-
the cation produces two different tautomers of the histidine residues His53 and His85
Sr2+
-
the enzyme contains a divalent ion-binding site involving Asp49, with preference for this cation. The ion binding at this site stabilizes the protein
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3'-N-hydroxyurea-3'-deoxythymidine-5'-phosphate
competitive, inhibition is enhanced by nearly 10fold in presence of Zn2 in wild-type enzyme, no enhancement in mutant enzyme E54Q
iodoacetamide
-
iodoacetamide, but not iodoacetate, reacts with these His residues at pH 8.0, but not at pH 5.5
Ozone
-
loss of activity at pH 7.5, at pH 4.75 the enzyme retains a decreased but distinct enzyme activity towards RNA without alteration of substrate specificity
barstar
-
a small protein of 89 amino acids, specifically inhibits barnase, barnase and barstar form a noncovalent one-to-one complex. Barstar inhibits barnase activity by sterically blocking its active site with an alpha-helix and adjacent loop. The association is stabilized by charge interaction involving the positively charged amino acid residues Lys27, Arg59, Arg83 and Arg87 of barnase and the negatively charged Asp35, Asp39 and Glu76 of barstar
-
barstar
dimerization can compete with binase inhibition by barstar, the ratio of competitve reaction rates depends on pH and ionic strength of the solution
-
iodoacetate
-
reaction of iodoacetate with the gamma-carboxyl group of Glu58 in RNase T1. The iodoacetate reaction is inhibited by substrate analogues 2- or 3-guanylic acid, by phosphate or citrate ions, and by Zn2+ or Cu2+
Phenylglyoxal
-
inactivates the enzyme by specific reaction with Arg77 at the active site
additional information
-
fairly resistant to proteases, e.g. carboxypeptidase A, leucine aminopeptidase, trypsin, chymotrypsin
-
additional information
-
carboxymethylated-RNase T1 possesses almost the same binding ability toward guanosine as intact RNase T1, whereas the binding ability toward 2' or 3'-guanylic acid is considerably lowered by carboxymethylation of Glu58
-
additional information
-
no effective inhibition of barnase by RNase inhibitor YrdF
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1670
guanosine-2',3'-cyclic monophosphate
-
pH 6.0, 25ºC, wild type enzyme
additional information
additional information
-
Kcat/Km values of 1000 mM-1 S-1, 0.458 mM-1 S-1, 7520 mM-1 S-1, and 8.65 mM-1 S-1 for wild type enzyme and Y38F, E58A, H92Q and F100A mutants, respectively, with GpU as substrate. Kcat/Km values of 11.3 mM-1 S-1, 15.1 mM-1 S-1, 0.153 mM-1 S-1, 27.4 mM-1 S-1, 0.117 mM-1 S-1, 1.38 mM-1 S-1 for wild type enzyme and Y38F, H40A, E58A, and F100A mutants, respectively, with SpGp(S)U as substrate. Kcat/Km values of 665 mM-1 S-1, 210 mM-1 S-1, 0.029 mM-1 S-1, 5.35 mM-1 S-1, 0.028 mM-1 S-1 and 0.508 mM-1 S-1 for wild type enzyme and Y38F, H40A, E58A, H92Q and F100A mutants, respectively, with RpGp(S)U as substrate
-
additional information
additional information
-
kcat/Km(GpC)/kcat/Km(ApC) is 284000 for wild-type enzyme, 195 for mutant enzyme E46N and 137 for mutant enzyme E46N/Y45W
-
additional information
additional information
kcat/Km(GpC)/kcat/Km(ApC) is 284000 for wild-type enzyme, and 39 for mutant enzyne K41E/Y42F/N43R/Y45W/E46N/W59Y (RNase T1-R2) and mutant enzyme K41E/Y42F/N43R/Y45W/E46N (RNase RV)
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kcat/Km(GpC)/kcat/Km(ApC) is 284000 for wild-type enzyme, 195 for mutant enzyme E46N and 137 for mutant enzyme E46N/Y45W
-
additional information
additional information
kcat/Km(GpC)/kcat/Km(ApC) is 284000 for wild-type enzyme, and 39 for mutant enzyne K41E/Y42F/N43R/Y45W/E46N/W59Y (RNase T1-R2) and mutant enzyme K41E/Y42F/N43R/Y45W/E46N (RNase RV)
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.95
3'-N-hydroxyurea-3'-deoxythymidine-5'-phosphate
25°C, pH 6.2, wild-type enzyme
1.15
3'-N-hydroxyurea-3'-deoxythymidine-5'-phosphate
25°C, pH 6.2, mutant enzyme E54Q
0.000033
chitosan
-
poly(I) substrate, measurement is performed in 10 mM Tris, pH 7.0, containing 0.14 M NaCl and 0.1 mM EDTA
0.00008
chitosan
-
poly(A) * poly(U) substrate, measurement is performed in 10 mM Tris, pH 7.0, containing 0.14 M NaCl and 0.1 mM EDTA
0.00009
chitosan
-
poly(I) substrate, measurement is performed in 10 mM Tris, pH 7.0, containing 0.14 M NaCl and 0.1 mM EDTA
0.0001
chitosan
-
poly(I) substrate, measurement is performed in 10 mM Tris, pH 7.0, containing 0.14 M NaCl and 0.1 mM EDTA
0.00012
chitosan
-
poly(I) substrate, measurement is performed in 10 mM Tris, pH 7.0, containing 0.14 M NaCl and 0.1 mM EDTA
0.00012
chitosan
-
poly(I) substrate, measurement is performed in 10 mM Tris, pH 7.0, containing 0.14 M NaCl and 0.1 mM EDTA
0.00021
chitosan
-
poly(I) * poly(C) substrate, measurement is performed in 10 mM Tris, pH 7.0, containing 0.14 M NaCl and 0.1 mM EDTA
0.00022
chitosan
-
poly(I) substrate, measurement is performed in 10 mM Tris, pH 7.0, containing 0.14 M NaCl and 0.1 mM EDTA
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
7.5
8.5
7.5
recombinant mutant D19N/D22N/E25Q/D31N/D38N/E50Q/E57Q/E76Q/D77N/D79N/E92Q/D93N
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
-
3: 25% of activity maximum, 6: about 10% of activity maximum, Aspergillus niger RNase II
4 - 9
-
4: 10% (native), 20% (immobilized) of activity maximum, 9: 32% (native), 25% (immobilized) of activity maximum, 10: immobilized enzyme, some activity, native enzyme, inactive
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
65 - 70
65 - 70
wild-type enzyme and recombinant mutant D19N/D22N/E25Q/D31N/D38N/E50Q/E57Q/E76Q/D77N/D79N/E92Q/D93N
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 55
-
20°C: 18% of activity maximum, 55°C: 15% of activity maximum, inactive at 60°C, native enzyme
38 - 80
-
38°C: 55% of activity maximum, 80°C: 40% of activity maximum, immobilized enzyme
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
4.2
4.9
6.9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
binase is not produced by Bacillus pumilus when bacteria are grown on medium containing an inorganic source of nitrogen. Expression of binase is possible only in Spo0A-OFF cells
brenda
-
Taka-diastase, commercial product of Aspergillus oryzae
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
in contrast to the wild-type strain in which the inactivated RNase T1-GFP fusion protein is localized at the vacuole only under cold stress or nitrogen starvation, the inactivated RNase T1-GFP fusion protein expressed in the rns4 mutant is localized at the ER and vacuole, both under normal growth conditions and upon ambient stress conditions
brenda
additional information
additional information
-
about 3040% of barnase can be stored inside the cells for up to 90 min in complex with inhibitor barstar
-
brenda
additional information
-
99% of binase is present outside of the cell and only below 1% is localized intracellularly
-
brenda
additional information
RNase Po1 might bind to the plasma membrane electrostatically
-
brenda
additional information
-
RNase Po1 might bind to the plasma membrane electrostatically
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to the RNase T1 family, comparison of the amino acid sequences, overview
malfunction
-
deletion of gene rng leads to accumulation of 23S rRNA precursors in Escherichia coli
malfunction
-
deletion of gene rng leads to accumulation of 23S rRNA precursors in Escherichia coli
-
metabolism
-
binase is involved in phosphate metabolism, low concentrations of extracellular inorganic phosphate induce the expression of phosphate regulon, Pho, genes, as well as the binase gene, binase expression is strongly dependent on a functional PhoP-PhoR two-component system
metabolism
-
distinct roles of RNase E and RNase G in mRNA decay and tRNA processing, overview
physiological function
binase is a regulator of RNA-dependent processes of cell proliferation and apoptosis. Binase affects the total amount of intracellular RNA and the expression of proapoptotic and antiapoptotic mRNAs
physiological function
-
barnase can help the population to win the competition with other bacteria for ecological niches, acting as a toxin. Toxic extracellular RNases and antitoxic barstar build an analogous system
physiological function
-
binase can help the population to win the competition with other bacteria for ecological niches, acting as a toxin
physiological function
-
RNase G is involved in maturation of the 5' end of the 23S rRNA processing the 5' region by cleaving the 77 extra nucleotides at the 5' end
physiological function
-
RNase G is involved in the maturation of the 5' terminus of 16S rRNA, the processing of a few tRNAs, and the initiation of decay of a limited number of mRNAs but is not required for cell viability and cannot substitute for RNase E under normal physiological conditions
physiological function
the enzyme from Pleurotus ostreatus inhibits human tumor cell proliferation, e.g. of neuroblastoma cell lines IMR-32 and SK-N-SH and leukemia cell lines HL-60 and Jurkat. The enzyme causes a sub-G1-cell population formation in HL-60 cells, overview
physiological function
the enzyme inhibits human tumor cell line proliferation
physiological function
the enzyme is cytotoxic and inhibits the proliferation of human tumor cells, the enzyme is internalized into tumour cells
physiological function
the wild-type enzyme shows little inhibition of human tumor cell proliferation, but the mutant D19N/D22N/E25Q/D31N/D38N/E50Q/E57Q/E76Q/D77N/D79N/E92Q/D93N is inhibiting proliferation in human leukemia cell lines, HL-60 and Jurkat with IC50 values of 100 nM and 0.002 mM, respectively, mutant D31N/D38N/E92Q/D93N is inactive
physiological function
-
ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
physiological function
-
ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
physiological function
-
ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
physiological function
-
ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
physiological function
-
ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
physiological function
ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
physiological function
RNase He1 shows little inhibition of human tumor cell proliferation
physiological function
-
ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
-
physiological function
Escherichia coli BL21alpha
-
ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
-
physiological function
-
RNase G is involved in maturation of the 5' end of the 23S rRNA processing the 5' region by cleaving the 77 extra nucleotides at the 5' end
-
physiological function
-
ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
-
physiological function
-
ribonuclease T1 preserves ribosomal integrity while thoroughly converting polysomes to monosomes
-
additional information
-
analysis of cumulative permeation and skin deposition of negatively charged RNAse T1 using porcine ear skin. RNAse T1 permeation is dependent upon current density,while skin deposition is not. RNAse T1 retains structural integrity and enzymatic function postiontophoresis. RNAse T1 appears to be bound to the epidermis alone
additional information
-
comparison with barnase from Bacillus amyloliquefaciens, overview. Mutation in resD leads to a significant decrease in binase production, whereas mutation in spo0A causes its hyperproduction. Expression of binase is possible only in Spo0A-OFF cells
additional information
-
comparison with binase from Bacillus pumilus, overview. Barnase expression is strictly dependent on activating Spo0A, the Spo0A protein is a multifunctional regulator that controls stress-related processes, such as sporulation, biofilm formation and cannibalism
additional information
-
effects of water-water hydrogen bonding types upon the activity of the enzyme ribonuclease t1 through perturbation of the water hydrogen bonding distribution by using various salts, overview. Various salts differ in their ability to reduce the enzymatic activity of ribonuclease t1 correlated with the ability of each salt to promote high-angle hydrogen bonding in water. Increasing the population of high-angle hydrogen bonds among water molecules stabilizes the more compact, less active conformations of the enzyme
additional information
-
neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneD1018 alleles, encoding RNase E, even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the predicted RNase H domain of RNase G, generating the rng-219 and rng-248 alleles, result in complementation of the growth defect associated with various RNase E mutants. Complementation of the growth defect associated with RNase E-deficient strains is dependent on the intracellular level of the Rng-219 and Rng-248 proteins
additional information
comparison of the electrostatic potential of the molecular surfaces of RNase Po1 and RNase T1 shows that RNase T1 is anionic whereas RNase Po1 is cationic, so RNase Po1 might bind to the plasma membrane electrostatically, determination of the three-dimensional X-ray structure of RNase Po1 and comparison to that of RNase T1. One of the additional disulfide bond is in the catalytic and binding site of RNase Po1, and makes RNase Po1 more stable than RNase T1. The base recognition site of RNase T1 consists of Tyr42, Asn43, Asn44, Glu46, Tyr45, and Asn98 and is located in the loop between beta3-4 strands (Asn43, Asn44, Tyr45, Glu46) and in the loop between beta6-7 strands (Asn98). In case of the base recognition site of RNase Po1, the amino acid residues Tyr38, Asn39, Asn40, Phe41, Glu42, and Asn94 correspond to those of RNase T1
additional information
-
comparison of the electrostatic potential of the molecular surfaces of RNase Po1 and RNase T1 shows that RNase T1 is anionic whereas RNase Po1 is cationic, so RNase Po1 might bind to the plasma membrane electrostatically, determination of the three-dimensional X-ray structure of RNase Po1 and comparison to that of RNase T1. One of the additional disulfide bond is in the catalytic and binding site of RNase Po1, and makes RNase Po1 more stable than RNase T1. The base recognition site of RNase T1 consists of Tyr42, Asn43, Asn44, Glu46, Tyr45, and Asn98 and is located in the loop between beta3-4 strands (Asn43, Asn44, Tyr45, Glu46) and in the loop between beta6-7 strands (Asn98). In case of the base recognition site of RNase Po1, the amino acid residues Tyr38, Asn39, Asn40, Phe41, Glu42, and Asn94 correspond to those of RNase T1
additional information
-
Trp59 may play an important role in folding as well as in modulating the geometry of the RNase T1 active site. Trp59-water pairs appear to preferentially participate in a hydrogen bond network incorporating polar amino acid moieties on the protein surface and bulk waters, providing the structural dynamic features of the connecting loop region in RNase T1, molecular dynamic simulations, overview
additional information
fluorescence spectroscopy of wild type (containing a single tryptophan, Trp59), 7-azatryptophan ((7-aza)Trp59-), and 2,7-diazatryptophan ((2,7-aza)Trp59-) substituted RNase T1 to probe the water environment of Trp59 near the connecting loop region gives insight of the structure-water network relationship
additional information
-
fluorescence spectroscopy of wild type (containing a single tryptophan, Trp59), 7-azatryptophan ((7-aza)Trp59-), and 2,7-diazatryptophan ((2,7-aza)Trp59-) substituted RNase T1 to probe the water environment of Trp59 near the connecting loop region gives insight of the structure-water network relationship
-
Show AA Sequence and Transmembrane Helices (800 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11000
26000
-
2 * 26000, fusion protein of the antiferritin antibody VL domain and barnase, SDS-PAGE
53000
-
fusion protein of the antiferritin antibody VL domain and barnase, gel filtration
71100
-
apparent molecular mass of the monomer, determined by sedimentation equilibrium analysis
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
dimer
-
2 * 26000, fusion protein of the antiferritin antibody VL domain and barnase, SDS-PAGE
additional information
-
comparisons of primary enzyme structure, overview
additional information
-
the secondary structure of RNase T1 includes a long alpha-helix and two beta-sheets connected by extended loop regions, structure of hydrated RNase T1 in loop-close and loop-open forms, overview
additional information
comparison of primary, secondary, and tertiary structures of RNase Po1 and RNase T1, overview
additional information
-
comparison of primary, secondary, and tertiary structures of RNase Po1 and RNase T1, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of RNase T1-T2 (K41E/Y42F/N43R/Y45W/E46N/W59Y), hanging drop vapor diffusion method, 2.1 A resolution
hanging drop vapor diffusion method, crystallization of RNase T1 variant RV (mutant RNase T1 K41E/Y42F/N43R/Y45W/E46N)
two crystal forms obtained, the classic crystal form I, and the crystals of form II, obtained by repeated seeding
-
the X-ray coordinates of barnase for this study are obtained from the Protein Data Bank, PDB code 1rnb
-
three-dimensional X-ray crystal structure of RNase He1 in complex with Zn
mutant enzyme Q94K, hanging-drop vapor-diffusion method at 18°C
structures of two crystal forms (I and II) of ribonuclease Sa2 are presented at 1.8 A and 1.5 A resolution. Vapour diffusion from a solution of 1.0% protein by weight in 0.1 M phosphate buffer at pH 7.2 and room temperature with 40% saturated ammonium sulfate as precipitant
-
the crystal structures of RNase NT in complex with either 5'-AMP, 5'-GMP, or 2'-UMP are determined at 1.8 A resolutions by molecular replacement
-
purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 500 nl of 10 mg/mL protein in 20 mM Tris-HCl, pH 7.5, with 500 nl of reservoir solution containing 4 M sodium formate, 0.1 M Bis-Tris propane, pH 7.0, 10% PEG 400, and 300 nl 2 M caesium chloride, 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.85 A resolution, molecular replacement method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E41K
-
with almost the same activity as wild-type enzyme. Glu41 is not involved in substrate binding
E46N
-
mutant shows an improved ApC/GpC preference with a 1450fold increase in comparison to wild-type activity
E74K
-
less active than the wild-type enzyme due to a change in the orientation of the catalytic groups
K41E/Y42F/N43R/Y45W/E46N/W59Y
RNase T1-R2 contains the additional mutation W59Y compared to RNase T1-RV variant. RNase T1-RV is a variant where the specificity is changed from guanine to purine, accompanied with a reduced activity. The additional mutation W59Y increases the activity in comparison to variant RV to 425%
K41M
-
mutant with identical catalytic properties as the wild type enzyme with guanosine-2',3'-cyclic monophosphate as substrate, but less active with polyinosinic acid as substrate
K41T
-
mutant with identical catalytic properties as the wild type enzyme with guanosine-2',3'-cyclic monophosphate as substrate, but less active with polyinosinic acid as substrate
Q46_G47insL
-
mutant with a Leu insertion in 47, less active than the wild type enzyme
Q46_N47insQ
-
mutant with a Glu insertion in 47, less active than the wild type enzyme
Q46_P47insP
-
mutant with a Pro insertion in 47, less active than the wild type enzyme
Q46_P47insQ
-
mutant with a Glu insertion in 47, as active as the wild type enzyme
Q46_P47insY
-
mutant with a Tyr insertion in 47, less active than the wild type enzyme
Q46_Q47insP
-
mutant with a Pro insertion in 47, less active than the wild type enzyme
Q46_R47insR
-
mutant with an Arg insertion in 47, less active than the wild type enzyme
Q46_S47insG
-
mutant with a Gly insertion in 47, less active than the wild type enzyme
Q46_S47insS
-
mutant with a Ser insertion in 47, less active than the wild type enzyme
Q46_T47insS
-
mutant with a Ser insertion in 47, less active than the wild type enzyme
Y45W/E46N
-
mutant shows an improved ApC/GpC preference with a 2100fold increase in comparison to wild-type activity
D54A
-
mutant is modeled in silico for gaining insight into modulations of diffusional association behavior, which is reflected in the association rate
D54A/E60A
-
mutant is modeled in silico for gaining insight into modulations of diffusional association behavior, which is reflected in the association rate
E60A
-
mutant is modeled in silico for gaining insight into modulations of diffusional association behavior, which is reflected in the association rate
H102A
-
the secondary structure unit mutant S2354 is expressed in Escherichia coli only when His102 is substituted by alanine (H102A). The mutant S2354 102A has secondary and tertiary structures and unfolds in a cooperative manner during urea-induced unfolding experiments. S2354H102A interacts with other barnase mutants to hydrolyze RNA
K27A
-
mutant is modeled in silico for gaining insight into modulations of diffusional association behavior, which is reflected in the association rate
K66A
-
mutant is modeled in silico for gaining insight into modulations of diffusional association behavior, which is reflected in the association rate
K66A/D54A
-
mutant is modeled in silico for gaining insight into modulations of diffusional association behavior, which is reflected in the association rate
R59A
-
mutant is modeled in silico for gaining insight into modulations of diffusional association behavior, which is reflected in the association rate
R83Q
-
mutant is modeled in silico for gaining insight into modulations of diffusional association behavior, which is reflected in the association rate
R87A
-
mutant is modeled in silico for gaining insight into modulations of diffusional association behavior, which is reflected in the association rate
D303N
-
mutant with amino acid substitution in the binding pocket, inactive enzyme
R169A
-
mutant with amino acid substitution in the binding pocket, inactive enzyme
D19N/D22N/E25Q/D31N/D38N/E50Q/E57Q/E76Q/D77N/D79N/E92Q/D93N
site-directed mutagenesis using three different PCR primers
D31N/D38N/E92Q/D93N
site-directed mutagenesis using two different PCR primers
D1W
-
the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties
D33A
Tm-value at pH 7.0 in Mops buffer is 16 °C lower than wild-type value. The stability of the mutant enzyme is 6 kcal/mol less than wild-type RNase Sa
D79A
Tm-value at pH 7.0 in Mops buffer is 9.2 °C higher than wild-type value. The stability of the mutant enzyme is 3.3 kcal/mol less than wild-type RNase Sa
D79E
Tm-value at pH 7.0 in Mops buffer is 0.8 °C lower than wild-type value. kcat/Km is identical to wild-type value
D79F
Tm-value at pH 7.0 in Mops buffer is 9.9 °C higher than wild-type value
D79H
Tm-value at pH 7.0 in Mops buffer is 5.6 °C higher than wild-type value
D79I
Tm-value at pH 7.0 in Mops buffer is 9.6 °C higher than wild-type value. kcat/Km is 1.3fold lower than wild-type value
D79K
Tm-value at pH 7.0 in Mops buffer is 7.6 °C higher than wild-type value. kcat/Km is 1.1fold lower than wild-type value
D79L
Tm-value at pH 7.0 in Mops buffer is 8.7 °C higher than wild-type value
D79N
Tm-value at pH 7.0 in Mops buffer is 5.5 °C higher than wild-type value. kcat/Km is 1.1fold lower than wild-type value
D79R
Tm-value at pH 7.0 in Mops buffer is 9.0 °C higher than wild-type value. kcat/Km is 1.1fold higher than wild-type value
D79W
Tm-value at pH 7.0 in Mops buffer is 7.6 °C higher than wild-type value. kcat/Km is 1.2fold lower than wild-type value
D79Y
Tm-value at pH 7.0 in Mops buffer is 9.6 °C higher than wild-type value
Q94K
Tm-value at pH 7.0 in Mops buffer is 0.8 °C higher than wild-type value. Crystal structure shows that the amino group of the Lys forms a hydrogen-bonded ion pair with the carboxyl group of Asp79. The stability of the mutant is about the same as the wild-type at pH 3, where Asp79 is uncharged, but 1 kcal/mol greater than that of wild-type RNase Sa at pH 8.5, where Asp79 is charged
T76W
-
the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties
Y52W
-
the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties
Y55W
-
the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties
Y81W
-
the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties
additional information
additional information
two extended replica-exchange molecular dynamics simulations on RNase T1, each with different histidine protonation states, corresponding to pH 6 and pH8. At high pH, the appearance of partially unfolded states is evident. This pH-induced destabilization originates from increased global repulsion as well as reduced local favorable electrostatic interactions and reduced H-bonding strength of His27, His40, and His92. At high pH, alternative tryptophan rotamers appear and are linked to a distorted environment of the tryptophan, which also acts as a separate source of ground-state heterogeneity
additional information
-
fusion of the antiferritin antibody VL domain to barnase results in enhanced solubility and altered pH stability
additional information
-
two distinct spontaneously derived single amino acid substitutions within the predicted RNase H domain of RNase G, generate the rng-219 and rng-248 alleles, which complement the rne mutant strains. Domain swaps between RNase E and RNase G generate proteins that do not complement RNase E deficiency
additional information
generation of enzyme mutants by replacing 12 Asn/Gln residues with Asp/Glu residues in analogy to the amino acid sequence of RNase Po1 from Pleurotus ostreatus. One mutant shows modified higher optimal pH for enzyme activity compared to the wild-type enzyme and inhibits the proliferation of cells in a human leukemia cell line
additional information
-
generation of enzyme mutants by replacing 12 Asn/Gln residues with Asp/Glu residues in analogy to the amino acid sequence of RNase Po1 from Pleurotus ostreatus. One mutant shows modified higher optimal pH for enzyme activity compared to the wild-type enzyme and inhibits the proliferation of cells in a human leukemia cell line
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 9
4 - 10
-
37°C, 33 h, immobilized enzyme, highest stability at pH 7, at pH 1.0 and 10.0: about 60% of activity maximum
24202
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
90
purified recombinant enzyme, 5 min, over 80% activity remaining
additional information
-
the reversibility of the thermal denaturation is generally between 90% and 95%. Q38A and E74K mutants are slightly more stable than the wild-type enzyme. E41K, E54A and R65A mutants are less stable than the wild-type enzyme
100
-
30 min, immobilized enzyme: 5% loss of activity, native enzyme: about 60% loss of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NaCl and low concentrations of guanidinium chloride stabilize RNase Sa, conformational stability is studied by NMR-monitored hydrogen exchange
NaCl, protects from thermal denaturation, increases transition temperature, suppresses unfolding of enzyme by a denaturant, urea, increases conformational stability
-
Proteases, fairly resistant to proteases: carboxypeptidase A, leucine aminopeptidase, trypsin, chymotrypsin <1>, resistant to trypsin and chymotrypsin, sensitive to pepsin
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Photooxidation, in presence of Methylene Blue, riboflavine or Rose Bengal inactivation
-
24191
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
fusion protein of the antiferritin antibody VL domain and barnase
-
ion-exchange chromatography and gel filtration
recombinant enzyme from Escherichia coli strain BL21(DE3)pLysS to homogeneity by ammonium sulfate fractionation, gel filtration, cation exchange and anion exchange chromatography, and again gel filtration, heparin affinity chromatography, and dialysis
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) pLysS to homogeneity by ammonium sulfate fractionation, gel filtration, cation exchange and anion exchange chromatography, and again gel filtration, heparin affinity chromatography, and dialysis
similar enzyme
similar enzyme, partial
using a Super Q Toyopearl column and ion-exchange chromatography on a column of resource Q
-
recombinant enzyme from Escherichia coli strain BL21(DE3)pLysS to homogeneity by ammonium sulfate fractionation, gel filtration, cation exchange and anion exchange chromatography, and again gel filtration, heparin affinity chromatography, and dialysis
recombinant enzyme from Escherichia coli strain BL21(DE3)pLysS to homogeneity by ammonium sulfate fractionation, gel filtration, cation exchange and anion exchange chromatography, and again gel filtration, heparin affinity chromatography, and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a 1.8 kb DNA fragment, encoding the C-terminal portion of the MycRne polypeptide, residues 332-953, is cloned into p6HisF-11d for expression in Escherichia coli BL21-CodonPlusDE3-RIL cells
-
chemically synthesized gene, mutant Gln58Asp, expressed in Escherichia coli host
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)pLysS
DNA and amino acid sequence determination and analysis, sequence comparisons, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) pLysS
expression in Escherichia coli
expression in Escherichia coli BL21 carrying plasmid pGEMGX1/ent/Bi as a homogeneous protein
expression of the enzyme in Trp-auxotrophic Escherichia coli, resulting in site-specifically replacement of Trp residues with (2,7-aza)Trp
-
fusion of the antiferritin antibody VL domain to barnase and expression in Escherichia coli
-
gene rng, overexpression of wild-type rng and of mutant rngs in rne-1 or rneD1018 alleles mutant strains
-
genetic organization, low level expression of barnase by recombinant Bacillus subtilis strains bearing phoPR-null mutations
-
genetic organization, production of binase by recombinant Bacillus subtilis strains bearing phoPR-null mutations is impossible
-
into the pGEM-T vector for transformation of Escherichia coli JM109 cells, into pPIC9K for expression in Pichia pastoris
-
into the pQE30 vector for expression in Escherichia coli M15 cells
-
overexpression in Neurospora crassa, different promoters are tested, the most promising promoter for recombinant expression is the cfp promoter
overexpression in Saccharomyces cerevisiae. Characterization of an rns4/vps32 mutation in the RNase T1 expression-sensitive strain of Saccharomyces cerevisiae. The rns4 mutant is sensitive to both RNase T1 and ambient stress. In contrast to the wild-type strain in which the inactivated RNase T1-GFP fusion protein is localized at the vacuole only under cold stress or nitrogen starvation, the inactivated RNase T1-GFP fusion protein expressed in the rns4 mutant is localized at the ER and vacuole, both under normal growth conditions and upon ambient stress conditions
-
recombinant enzyme expression in Escherichia coli strain BL21(DE3) pLysS
the secondary structure unit mutant S2354 is expressed in Escherichia coli only when His102 is substituted by alanine (H102A)
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
low concentrations of extracellular inorganic phosphate induce the expression of the binase gene
-
upregulation of the KCa channels and the apoptotic p53 genes, downregulation of the antiapoptotic bcl-2 gene under binase action
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
salts induce chain folding of disulfide-reduced and modified RNase T1 into native conformation, enzyme activity is not restored
-
the enzyme can be reversibly unfolded and refolded by heating and high concentration of denaturants, such as urea and guanidine hydrochloride, without forming noticeable amounts of aggregates
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
the RNase G mutation could be applied in the breeding of producer strains of pyruvate and its derivatives such as valine
drug development
bacterial RNases are promising tools for the development of anticancer drugs. Binase affects the total amount of intracellular RNA and the expression of proapoptotic and antiapoptotic mRNAs
medicine
additional information
medicine
-
RNase inhibitors appear to be promising for therapy of cancer
medicine
-
RNase inhibitors appear to be promising for therapy of cancer
medicine
-
RNase inhibitors appear to be promising for therapy of cancer
medicine
-
RNase inhibitors appear to be promising for therapy of cancer
additional information
-
acquisition of male, female or bisexual sterility by transgenic plants with the help of barnase. The enzyme is useful in medical research, overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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1971
Aspergillus oryzae
-
brenda
Takahashi, K.; Moore, S.
Ribonuclease T1
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
15
435-468
1982
Aspergillus oryzae
-
brenda
Pace, C.N.; Grimsley, G.R.; Barnett, B.J.
Purification of ribonuclease T1
Anal. Biochem.
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1987
Aspergillus oryzae
brenda
Jervis, L.; Pettit, N.M.
Purification of ribonuclease T1 on porous glass affinity adsorbents
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97
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1974
Aspergillus oryzae
brenda
Fields, R.; Dixon, H.B.F.; Law, G.R.; Yui, C.
Purification of ribonuclease T 1 by diethylaminoethylcellulose chromatography
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121
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1971
Aspergillus oryzae
brenda
Kanaya, S.; Uchida, T.
Purification of ribonuclease T1 by affinity chromatography
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89
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1981
Aspergillus oryzae
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Conformational stability of ribonuclease T1. I. Thermal denaturation and effects of salts
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86
55-63
1979
Aspergillus oryzae
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Conformational stability of ribonuclease T1. II. Salt-induced renaturation
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86
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1979
Aspergillus oryzae
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Tamaoki, H.; Sakiyama, F.; Narita, K.
Chemical modification of ribonuclease T1 with ozone
J. Biochem.
83
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1978
Aspergillus oryzae
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Ruterjans, H.; Pongs, O.
On the mechanism of action of ribonuclease T1. Nuclear magnetic resonance study on the active site
Eur. J. Biochem.
18
313-318
1971
Aspergillus oryzae
brenda
Takahashi, K.
The structure and function of ribonuclease T1. VII. Further investigations on amino acid composition and some other properties of ribonuclease T1
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60
239-245
1966
Aspergillus oryzae
brenda
Ito, H.; Hagiwara, M.; Takahashi, K.; Ichikizaki, I.
The structure and function of ribonuclease T1 XXIV. Preparation and properties of a stable water-insoluble polyacrylamide derivative of ribonuclease T1
J. Biochem.
82
877-883
1977
Aspergillus oryzae
brenda
Koepke, J.; Maslowska, M.; Heinemann, U.; Saenger, W.
Three-dimensional structure of ribonuclease T1 complexed with guanylyl-2,5-guanosine at 1.8 A resolution
J. Mol. Biol.
206
475-488
1989
Aspergillus oryzae
brenda
Pace, C.N.; Grimsley, G.R.
Ribonuclease T1 is stabilized by cation and anion binding
Biochemistry
27
3242-3246
1988
Aspergillus oryzae
brenda
Walz, F.G.; Kitareewan, S.
Spermine stabilization of folded ribonuclease T1
J. Biol. Chem.
265
7127-7137
1990
Aspergillus oryzae
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Thomson, J.A.; Shirley, B.A.; Grimsley, G.R.; Pace, C.N.
Conformational stability and mechanism of folding of ribonuclease T1
J. Biol. Chem.
264
11614-11620
1989
Aspergillus oryzae
brenda
Kiefhaber, T.; Quaas, R.; Hahn, U.; Schmid, F.X.
Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization
Biochemistry
29
3053-3061
1990
Aspergillus oryzae
brenda
Pace, C.N.; Laurents, D.V.; Thomson, J.A.
pH Dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1
Biochemistry
29
2564-2572
1990
Aspergillus oryzae
brenda
Lee, J.C.
Preparation and properties of water-insoluble derivatives of ribonuclease T1
Biochim. Biophys. Acta
235
435-441
1971
Aspergillus oryzae
brenda
Kasai, K.; Uchida, T.; Egami, F.; Yoshida, K.; Nomoto, M.
Purification and crystallization of ribonuclease N1 from Neurospora crassa
J. Biochem.
66
389-396
1969
Neurospora crassa
brenda
Lindberg, R.A.; Drucker, H.
Characterization and comparison of a Neurospora crassa RNase purified from cultures undergoing each of three different states of derepression
J. Bacteriol.
157
375-379
1984
Neurospora crassa
brenda
Kenney, W.C.; Dekker, C.A.
Ribonuclease U1. Physical and chemical characterization of the purified enzyme
Biochemistry
10
4962-4970
1971
Ustilago sphaerogena
brenda
Hashimoto, J.; Uchida, T.; Egami, F.
Purification of ribonuclease U 1 and some properties of ribonucleases U 1 and N 1
J. Biochem.
70
903-911
1971
Ustilago sphaerogena
brenda
Fletcher, P.L.; Hash, J.H.
Ribonuclease of Chalaropsis species. I. Isolation and physical properties
Biochemistry
11
4274-4280
1972
Chalara sp.
brenda
Fletcher, P.L.; Hash, J.H.
Ribonuclease of Chalaropsis species. II. Chemical properties
Biochemistry
11
4281-4285
1972
Chalara sp.
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
Sevcik, J.; Sanishvili, R.G.; Pavlovsky, A.G.; Polyakov, K.M.
Comparison of active sites of some microbial ribonucleases: structural basis for guanylic specificity
Trends Biochem. Sci.
15
158-162
1990
Fungi
brenda
Yoshida, H.; Fukuda, I.; Hashiguchi, M.
Purification by affinity chromatography and physicochemical properties of the guanine-specific ribonuclease of Fusarium moniliforme
J. Biochem.
88
1813-1818
1980
Fusarium verticillioides
brenda
Nishikawa, S.; Morioka, H.; Fuchimura, K.; Tanaka, T.; Uesugi, S.; Ohtsuka, E.; Ikehara, M.
Modification of Glu 58, an amino acid of the active center of ribonuclease T1, to Gln and Asp
Biochem. Biophys. Res. Commun.
138
789-794
1986
Escherichia coli
brenda
Sevcik, J.; Lamzin, V.S.; Dauter, Z.; Wilson, K.S.
Atomic resolution data reveal flexibility in the structure of RNase Sa
Acta Crystallogr. Sect. D
58
1307-1313
2002
Kitasatospora aureofaciens (P05798), Kitasatospora aureofaciens
brenda
Jo Chitester, B.; Walz, F.G., Jr.
Kinetic studies of guanine recognition and a phosphate group subsite on ribonuclease T1 using substitution mutants at Glu46 and Lys41
Arch. Biochem. Biophys.
406
73-77
2002
Aspergillus oryzae
brenda
De Vos, S.; Backmann, J.; Prevost, M.; Steyaert, J.; Loris, R.
Hydrophobic core manipulations in ribonuclease T1
Biochemistry
40
10140-10149
2001
Aspergillus oryzae (P00651)
brenda
Kumar, K.; Walz, F.G., Jr.
Probing functional perfection in substructures of ribonuclease T1: double combinatorial random mutagenesis involving Asn43, Asn44, and Glu46 in the guanine binding loop
Biochemistry
40
3748-3757
2001
Aspergillus oryzae
brenda
Korn, K.; Wennmalm, S.; Foerster, H.H.; Hahn, U.; Rigler, R.
Analysis of the RNase T1 mediated cleavage of an immobilized gapped heteroduplex via fluorescence correlation spectroscopy
Biol. Chem.
381
259-263
2000
Aspergillus oryzae
brenda
Nonaka, G.; Ishikawa, T.; Liu, T.T.; Nakajima, H.; Kitamoto, K.
Genetic analysis of growth inhibition of yeast cells caused by expression of Aspergillus oryzae RNase T1
Biosci. Biotechnol. Biochem.
64
2152-2158
2000
Aspergillus oryzae
brenda
Loverix, S.; Winqvist, A.; Stromberg, R.; Steyaert, J.
Mechanism of RNase T1: concerted triester-like phosphoryl transfer via a catalytic three-centered hydrogen bond
Chem. Biol.
7
651-658
2000
Aspergillus oryzae
brenda
Deswarte, J.; De Vos, S.; Langhorst, U.; Steyaert, J.; Loris, R.
The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution
Eur. J. Biochem.
268
3993-4000
2001
Aspergillus oryzae
brenda
Huyghues-Despointes, B.M.; Thurlkill, R.L.; Daily, M.D.; Schell, D.; Briggs, J.M.; Antosiewicz, J.M.; Pace, C.N.; Scholtz, J.M.
pK values of histidine residues in ribonuclease Sa: effect of salt and net charge
J. Mol. Biol.
325
1093-1105
2003
Aspergillus oryzae
brenda
Shaw, K.L.; Grimsley, G.R.; Yakovlev, G.I.; Makarov, A.A.; Pace, C.N.
The effect of net charge on the solubility, activity, and stability of ribonuclease Sa
Protein Sci.
10
1206-1215
2001
Aspergillus oryzae
brenda
Yakovlev, G.I.; Mitkevich, V.A.; Shaw, K.L.; Trevino, S.; Newsom, S.; Pace, C.N.; Makarov, A.A.
Contribution of active site residues to the activity and thermal stability of ribonuclease Sa
Protein Sci.
12
2367-2373
2003
Aspergillus oryzae
brenda
Sevcik, J.; Dauter, Z.; Wilson, K.S.
Crystal structure reveals two alternative conformations in the active site of ribonuclease Sa2
Acta Crystallogr. Sect. D
D60
1198-1204
2004
Kitasatospora aureofaciens
brenda
Makarov, A.A.; Yakovlev, G.I.; Mitkevich, V.A.; Higgin, J.J.; Raines, R.T.
Zinc(II)-mediated inhibition of ribonuclease Sa by an N-hydroxyurea nucleotide and its basis
Biochem. Biophys. Res. Commun.
319
152-156
2004
Kitasatospora aureofaciens (P05798), Kitasatospora aureofaciens
brenda
Czaja, R.; Perbandt, M.; Betzel, C.; Hahn, U.
Purine activity of RNase T1RV is further improved by substitution of Trp59 by tyrosine
Biochem. Biophys. Res. Commun.
336
882-889
2005
Aspergillus oryzae (P00651)
brenda
Czaja, R.; Struhalla, M.; Hoschler, K.; Saenger, W.; Strater, N.; Hahn, U.
RNase T1 variant RV cleaves single-stranded RNA after purines due to specific recognition by the Asn46 side chain amide
Biochemistry
43
2854-2862
2004
Aspergillus oryzae (P00651)
brenda
Tsuji, T.; Yanagawa, H.
Foldability, enzymic activity, and interacting ability of barnase mutants obtained by permutation of secondary structure units
Biochemistry
43
6968-6975
2004
Bacillus amyloliquefaciens
brenda
Laurents, D.V.; Scholtz, J.M.; Rico, M.; Pace, C.N.; Bruix, M.
Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange
Biochemistry
44
7644-7655
2005
Kitasatospora aureofaciens (P05798)
brenda
Hatano, K.; Kojima, M.; Suzuki, E.; Tanokura, M.; Takahashi, K.
Determination of the NMR structure of Gln25-ribonuclease T1
Biol. Chem.
384
1173-1183
2003
Aspergillus oryzae
brenda
Stuhalla, M.; Czaja, R.; Hahn, U.
Addressing the chalange of changing the specificity of RNase T1 with rational and evolutionary approaches
ChemBioChem
5
200-205
2004
Aspergillus oryzae
brenda
Unno, K.; Juvvadi, P.R.; Nakajima, H.; Shirahige, K.; Kitamoto, K.
Identification and characterization of rns4/vps32 mutation in the RNase T1 expression-sensitive strain of Saccharomyces cerevisiae: Evidence for altered ambient response resulting in transportation of the secretory protein to vacuoles
FEMS Yeast Res.
5
801-812
2005
Aspergillus oryzae
brenda
Trevino, S.R.; Gokulan, K.; Newsom, S.; Thurlkill, R.L.; Shaw, K.L.; Mitkevich, V.A.; Makarov, A.A.; Sacchettini, J.C.; Scholtz, J.M.; Pace, C.N.
Asp79 makes a large, unfavorable contribution to the stability of RNase Sa
J. Mol. Biol.
354
967-978
2005
Kitasatospora aureofaciens (P05798)
brenda
Schrift, G.L.; Waldron, T.T.; Timmons, M.A.; Ramaswamy, S.; Kearney, W.R.; Murphy, K.P.
Molecular basis for nucleotide-binding specificity: role of the exocyclic amino group "N2" in recognition by a guanylyl-ribonuclease
J. Mol. Biol.
355
72-84
2006
Kitasatospora aureofaciens (P05798), Kitasatospora aureofaciens
brenda
Martsev, S.P.; Tsybovsky, Y.I.; Stremovskiy, O.A.; Odintsov, S.G.; Balandin, T.G.; Arosio, P.; Kravchuk, Z.I.; Deyev, S.M.
Fusion of the antiferritin antibody VL domain to barnase results in enhanced solubility and altered pH stability
Protein Eng. Des. Sel.
17
85-93
2004
Bacillus amyloliquefaciens
brenda
Giraldo, J.; De Maria, L.; Wodak, S.J.
Shift in nucleotide conformational equilibrium contributes to increased rate of catalysis of GpAp versus GpA in barnase
Proteins
56
261-276
2004
Bacillus amyloliquefaciens (P00648)
brenda
Yakovlev, G.I.; Mitkevich, V.A.; Struminskaya, N.K.; Varlamov, V.P.; Makarov, A.A.
Low molecular weight chitosan is an efficient inhibitor of ribonucleases
Biochem. Biophys. Res. Commun.
357
584-588
2007
Aspergillus oryzae, Bacillus amyloliquefaciens, Bacillus intermedius, Bos taurus, Penicillium brevicompactum, Kitasatospora aureofaciens
brenda
Kim, J.H.; Marshall, A.G.
Identification and assignment of base pairs in four helical segments of Bacillus megaterium ribosomal 5S RNA and its ribonuclease T1 cleavage fragments by means of 500-MHz proton homonuclear Overhauser enhancements
Biochemistry
29
632-640
1990
Aspergillus oryzae
brenda
Kawano, S.; Kakuta, Y.; Nakashima, T.; Kimura, M.
Crystal structures of the Nicotiana glutinosa ribonuclease NT in complex with nucleoside monophosphates
J. Biochem.
140
375-381
2006
Nicotiana glutinosa
brenda
Sakai, T.; Nakamura, N.; Umitsuki, G.; Nagai, K.; Wachi, M.
Increased production of pyruvic acid by Escherichia coli RNase G mutants in combination with cra mutations
Appl. Microbiol. Biotechnol.
76
183-192
2007
Escherichia coli
brenda
Zeller, M.E.; Csanadi, A.; Miczak, A.; Rose, T.; Bizebard, T.; Kaberdin, V.R.
Quaternary structure and biochemical properties of mycobacterial RNase E/G
Biochem. J.
403
207-215
2007
Mycobacterium tuberculosis
brenda
Ermakova, E.
Brownian dynamics simulation of the competitive reactions: binase dimerization and the association of binase and barstar
Biophys. Chem.
130
26-31
2007
Bacillus intermedius (P00649)
brenda
Spaar, A.; Dammer, C.; Gabdoulline, R.R.; Wade, R.C.; Helms, V.
Diffusional encounter of barnase and barstar
Biophys. J.
90
1913-1924
2006
Bacillus amyloliquefaciens
brenda
Alston, R.W.; Lasagna, M.; Grimsley, G.R.; Scholtz, J.M.; Reinhart, G.D.; Pace, C.N.
Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa
Biophys. J.
94
2288-2296
2008
Kitasatospora aureofaciens
brenda
Yoshida, Y.; Tanaka, M.; Ohkuri, T.; Tanaka, Y.; Imoto, T.; Ueda, T.
Analysis of internal motions of RNase T1 complexed with a productive substrate involving 15N NMR relaxation measurements
J. Biochem.
140
43-48
2006
Aspergillus oryzae
brenda
Yin, J.; Bowen, D.; Southerland, W.M.
Barnase thermal titration via molecular dynamics simulations: Detection of early denaturation sites
J. Mol. Graph. Model.
24
233-243
2006
Bacillus amyloliquefaciens
brenda
Gu, J.; Wang, J.; Leszczynski, J.
Molecular basis of the recognition process: hydrogen-bonding patterns in the guanine primary recognition site of ribonuclease T1
J. Phys. Chem. B
110
13590-13596
2006
Aspergillus oryzae (P00651)
brenda
Horie, Y.; Ito, Y.; Ono, M.; Moriwaki, N.; Kato, H.; Hamakubo, Y.; Amano, T.; Wachi, M.; Shirai, M.; Asayama, M.
Dark-induced mRNA instability involves RNase E/G-type endoribonuclease cleavage at the AU-box and SD sequences in cyanobacteria
Mol. Genet. Genomics
278
331-346
2007
Synechocystis sp. PCC 6803
brenda
Jourdan, S.S.; McDowall, K.J.
Sensing of 5 monophosphate by Escherichia coli RNase G can significantly enhance association with RNA and stimulate the decay of functional mRNA transcripts in vivo
Mol. Microbiol.
67
102-115
2008
Escherichia coli
brenda
Roca, M.; De Maria, L.; Wodak, S.J.; Moliner, V.; Tunon, I.; Giraldo, J.
Coupling of the guanosine glycosidic bond conformation and the ribonucleotide cleavage reaction: implications for barnase catalysis
Proteins Struct. Funct. Bioinform.
70
415-428
2007
Bacillus amyloliquefaciens (P00648)
-
brenda
Makarov, A.A.; Kolchinsky, A.; Ilinskaya, O.N.
Binase and other microbial RNases as potential anticancer agents
Bioessays
30
781-790
2008
Bacillus amyloliquefaciens (P00648), Bacillus intermedius (P00649), Bacillus intermedius, Bacillus intermedius 7P (P00649)
brenda
Zasedateleva, O.A.; Mikheikin, A.L.; Turygin, A.Y.; Prokopenko, D.V.; Chudinov, A.V.; Belobritskaya, E.E.; Chechetkin, V.R.; Zasedatelev, A.S.
Gel-based oligonucleotide microarray approach to analyze protein-ssDNA binding specificity
Nucleic Acids Res.
36
e61
2008
Bacillus intermedius
brenda
Allgaier, S.; Weiland, N.; Hamad, I.; Kempken, F.
Expression of ribonuclease A and ribonuclease N1 in the filamentous fungus Neurospora crassa
Appl. Microbiol. Biotechnol.
85
1041-1049
2010
Neurospora crassa (P09646), Neurospora crassa
brenda
Moors, S.L.; Jonckheer, A.; De Maeyer, M.; Engelborghs, Y.; Ceulemans, A.
Tryptophan conformations associated with partial unfolding in ribonuclease T1
Biophys. J.
97
1778-1786
2009
Aspergillus oryzae (P00651)
brenda
Mitkevich, V.A.; Tchurikov, N.A.; Zelenikhin, P.V.; Petrushanko, I.Y.; Makarov, A.A.; Ilinskaya, O.N.
Binase cleaves cellular noncoding RNAs and affects coding mRNAs
FEBS J.
277
186-196
2010
Bacillus intermedius (P00649), Bacillus intermedius
brenda
Chung, D.H.; Min, Z.; Wang, B.C.; Kushner, S.R.
Single amino acid changes in the predicted RNase H domain of Escherichia coli RNase G lead to complementation of RNase E deletion mutants
RNA
16
1371-1385
2010
Escherichia coli
brenda
Ulyanova, V.; Vershinina, V.; Ilinskaya, O.
Barnase and binase: twins with distinct fates
FEBS J.
278
3633-3643
2011
Bacillus amyloliquefaciens, Bacillus pumilus
brenda
Dubey, S.; Kalia, Y.N.
Electrically-assisted delivery of an anionic protein across intact skin: cathodal iontophoresis of biologically active ribonuclease T1
J. Control. Release
152
356-362
2011
Aspergillus oryzae
brenda
Song, W.S.; Lee, M.; Lee, K.
RNase G participates in processing of the 5'-end of 23S ribosomal RNA
J. Microbiol.
49
508-511
2011
Escherichia coli, Escherichia coli N3433
brenda
Beauchamp, D.L.; Khajehpour, M.
Probing the effect of water-water interactions on enzyme activity with salt gradients: a case-study using ribonuclease t1
J. Phys. Chem. B
114
16918-16928
2010
Aspergillus oryzae
brenda
Kobayashi, H.; Katsutani, T.; Hara, Y.; Motoyoshi, N.; Itagaki, T.; Akita, F.; Higashiura, A.; Yamada, Y.; Inokuchi, N.; Suzuki, M.
X-ray crystallographic structure of RNase Po1 that exhibits anti-tumor activity
Biol. Pharm. Bull.
37
968-978
2014
Pleurotus ostreatus (P81762), Pleurotus ostreatus
brenda
Kobayashi, H.; Motoyoshi, N.; Itagaki, T.; Tabata, K.; Suzuki, T.; Inokuchi, N.
The inhibition of human tumor cell proliferation by RNase Pol, a member of the RNase T1 family, from Pleurotus ostreatus
Biosci. Biotechnol. Biochem.
77
1486-1491
2013
Pleurotus ostreatus (B1Q4S7), Pleurotus ostreatus
brenda
Kobayashi, H.; Motoyoshi, N.; Itagaki, T.; Suzuki, M.; Inokuchi, N.
Effect of the replacement of aspartic acid/glutamic acid residues with asparagine/glutamine residues in RNase He1 from Hericium erinaceus on inhibition of human leukemia cell line proliferation
Biosci. Biotechnol. Biochem.
79
211-217
2015
Hericium erinaceus (B1Q4V2), Hericium erinaceus, Pleurotus ostreatus (P81762), Pleurotus ostreatus
brenda
Chao, W.C.; Shen, J.Y.; Lu, J.F.; Wang, J.S.; Yang, H.C.; Wee, K.; Lin, L.J.; Kuo, Y.C.; Yang, C.H.; Weng, S.H.; Huang, H.C.; Chen, Y.H.; Chou, P.T.
Probing water environment of Trp59 in ribonuclease T1: insight of the structure-water network relationship
J. Phys. Chem. B
119
2157-2167
2014
Aspergillus oryzae
brenda
Takahashi, K.
Structure and function studies on enzymes with a catalytic carboxyl group(s): from ribonuclease T1 to carboxyl peptidases
Proc. Jpn. Acad. Ser. B Phys. Biol. Sci.
89
201-225
2013
Aspergillus oryzae
brenda
Herbert, C.; Dzowo, Y.K.; Urban, A.; Kiggins, C.N.; Resendiz, M.J.E.
Reactivity and specificity of RNase T1, RNase A, and RNase H toward oligonucleotides of RNA containing 8-oxo-7,8-dihydroguanosine
Biochemistry
57
2971-2983
2018
Aspergillus oryzae (P00651), Aspergillus oryzae ATCC 42149 (P00651)
brenda
Chao, W.; Shen, J.; Lu, J.; Wang, J.; Yang, H.; Wee, K.; Lin, L.; Kuo, Y.; Yang, C.; Weng, S.; Huang, H.; Chen, Y.; Chou, P.
Probing water environment of trp59 in ribonuclease T1 insight of the structure-water network relationship
J. Phys. Chem. B
119
2157-2167
2015
Aspergillus oryzae (P00651), Aspergillus oryzae ATCC 42149 (P00651)
-
brenda
Gerashchenko, M.V.; Gladyshev, V.N.
Ribonuclease selection for ribosome profiling
Nucleic Acids Res.
45
e6
2017
Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, Escherichia coli, Mus musculus, Aspergillus oryzae (P00651), Saccharomyces cerevisiae BY4741, Escherichia coli BL21alpha, Caenorhabditis elegans N2, Aspergillus oryzae ATCC 42149 (P00651)
brenda
Loverix, S.; Laus, G.; Martins, J.C.; Wyns, L.; Steyaert, J.
Reconsidering the energetics of ribonuclease catalysed RNA hydrolysis
Eur. J. Biochem.
257
286-290
1998
Aspergillus oryzae
brenda
Kobayashi, H.; Sangawa, T.; Takebe, K.; Motoyoshi, N.; Itagaki, T.; Suzuki, M.
X-ray crystallographic structure of Hericium erinaceus ribonuclease, RNase He1 in complex with zinc
Biol. Pharm. Bull.
42
2054-2061
2019
Hericium erinaceus (B1Q4V2), Hericium erinaceus
brenda
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