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Information on EC 4.6.1.18 - pancreatic ribonuclease and Organism(s) Homo sapiens and UniProt Accession P07998

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IUBMB Comments
Specifically cleaves at the 3'-side of pyrimidine (uracil or cytosine) phosphate bonds in RNA. The reaction takes place in two steps, with the 2',3'-cyclic phosphodiester intermediates released from the enzyme at the completion of the first step. Hydrolysis of these cyclic compounds occurs at a much slower rate through a reversal of the first step, in which the -OH group of water substitutes for the 2'-OH group of the ribose used in the first step, and does not take place until essentially all the susceptible 3',5'-phosphodiester bonds have been cyclised. The enzyme can act as an endo- or exo ribonuclease.
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Homo sapiens
UNIPROT: P07998
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Word Map
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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an [RNA] containing cytidine
+
H2O
=
an [RNA]-3'-cytidine-3'-phosphate
+
a 5'-hydroxy-ribonucleotide-3'-[RNA]
an [RNA] containing cytidine
+
=
an [RNA]-3'-cytidine-3'-phosphate
+
a 5'-hydroxy-ribonucleotide-3'-[RNA]
an [RNA] containing uridine
+
H2O
=
an [RNA]-3'-uridine-3'-phosphate
+
a 5'-hydroxy-ribonucleotide-3'-[RNA]
an [RNA] containing uridine
+
=
an [RNA]-3'-uridine-3'-phosphate
+
a 5'-hydroxy-ribonucleotide-3'-[RNA]
Synonyms
eosinophil cationic protein, s-rnase, pancreatic ribonuclease, onconase, eosinophil-derived neurotoxin, pancreatic rnase, bovine pancreatic ribonuclease a, bs-rnase, rnase 1, rnase1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pancreatic ribonuclease
pancreatic RNase
-
alkaline ribonuclease
-
-
-
-
Ceratitis capitata alkaline ribonuclease
-
-
-
-
EC-RNase
-
-
eosinophil cationic protein
-
-
Eosinophil-derived neurotoxin
-
-
-
-
gene S glycoproteins
-
-
-
-
gene S locus-specific glycoproteins
-
-
-
-
glycoproteins, gene S locus-specific
-
-
-
-
glycoproteins, S-genotype-asssocd
-
-
-
-
glycoproteins, SLSG
-
-
-
-
glycoproteins, specific or class, gene S
-
-
-
-
glycoproteins, specific or class, SLSG (gene S locus-specific glycoprotein)
-
-
-
-
HP-RNase
-
-
nuclease, ribo-
-
-
-
-
pancreatic ribonuclease
-
-
pancreatic ribonuclease 1
-
-
pancreatic RNase
ribonuclease
-
-
-
-
ribonuclease A
-
-
-
-
ribonuclease I
-
-
-
-
Ribonuclease US
-
-
-
-
ribonuclease W1
-
-
-
-
ribonucleate 3'-pyrimidino-oligonucleotidohydrolase
-
-
-
-
ribonucleic phosphatase
-
-
-
-
RL1
-
-
-
-
RNase
-
-
-
-
RNase 1
-
-
RNase 2
-
-
RNase 3
-
-
RNase 4
-
-
RNase 5
-
-
RNase A
RNase I
-
-
-
-
RNase1
-
-
S-RNase
-
-
-
-
Seminal RNase
-
-
-
-
SLSG glycoproteins
-
-
-
-
additional information
-
the enzyme is a member of RNase A superfamily
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA]
show the reaction diagram
specifically located basic residues, together with the lack of a negative charge and/or the presence of a glycine at position 38, may contribute to make the enzymatic degradation of the polyanionic double-helical substrate more efficient
an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA]
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
RNA lyase ([RNA]-3'-cytidine/uridine-3'-phosphate and 5'-hydroxy-ribonucleotide-3'-[RNA] producing)
Specifically cleaves at the 3'-side of pyrimidine (uracil or cytosine) phosphate bonds in RNA. The reaction takes place in two steps, with the 2',3'-cyclic phosphodiester intermediates released from the enzyme at the completion of the first step. Hydrolysis of these cyclic compounds occurs at a much slower rate through a reversal of the first step, in which the -OH group of water substitutes for the 2'-OH group of the ribose used in the first step, and does not take place until essentially all the susceptible 3',5'-phosphodiester bonds have been cyclised. The enzyme can act as an endo- or exo ribonuclease.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-99-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cyclic 2',3'-cytidine monophosphate + H2O
3'-CMP
show the reaction diagram
-
-
-
?
double-stranded RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
show the reaction diagram
yeast dsRNA
-
-
?
poly (C) + H2O
3'-CMP + 3'-phospho-oligo(C)
show the reaction diagram
-
-
-
?
poly(A) + H2O
3'-AMP + 3'-oligonucleotides
show the reaction diagram
poor substrate because of Thr45 in the substrate binding site of the enzyme that sterically excludes purine bases
-
-
?
poly(A)poly(U) + H2O
?
show the reaction diagram
-
-
-
?
poly(C) + H2O
3'-CMP + 3'-phosphooligonucleotides
show the reaction diagram
-
-
-
?
poly(U) + H2O
3'-UMP + 3'-oligonucleotides
show the reaction diagram
-
-
-
?
single-stranded RNA + H2O
?
show the reaction diagram
-
-
-
?
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
show the reaction diagram
-
second step of hydrolysis is irreversible
-
-
ir
cytidine-2',3'-cyclic monophosphate + H2O
3'-CMP
show the reaction diagram
-
hydrolysis reaction
-
-
?
double-stranded poly(A)-poly(U) + H2O
3'-UMP + 3'-oligonucleotides
show the reaction diagram
-
-
-
-
?
double-stranded RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
show the reaction diagram
-
dsRNA
-
-
?
poly (C) + H2O
3'-CMP + 3'-phosphooligonucleotides
show the reaction diagram
-
-
-
-
?
poly U + H2O
3'-UMP + 3'-oligonucleotides
show the reaction diagram
poly(A)-poly(U) + H2O
?
show the reaction diagram
-
-
-
-
?
poly(A)poly(U) + H2O
?
show the reaction diagram
-
-
-
-
?
poly(C) + H2O
3'-CMP + 3'-phosphooligonucleotides
show the reaction diagram
poly(C) + H2O
?
show the reaction diagram
-
-
-
-
?
poly(U) + H2O
3'-UMP + 3'-oligonucleotides
show the reaction diagram
-
-
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
show the reaction diagram
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
show the reaction diagram
-
first step of hydrolysis is reversible
-
-
r
tRNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
show the reaction diagram
-
tRNA from yeast
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
show the reaction diagram
-
endonucleolytic cleavage to 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates, e.g. tRNA, 18S and 28S rRNA, yeast RNA,4.5S RNA
-
-
?
additional information
?
-
-
the enzyme degrades single-stranded and/or double-stranded RNA
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfate
13 sulfate anions are identified in the electrondensity map of the two dimers in the asymmetric unit of the crystal, confirming that this ion plays a fundamental role in the crystallization process. Four sulfate ions are positioned at the active sites, as typically observed in several other members of the pancreatic-like superfamily, the remaining anions are located on positive patches of the rod surface
K+
-
increases activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ribonuclease inhibitor
-
CaCl2
-
-
CuSO4
-
-
cytidine 2',3'-cyclic monophosphate
-
substrate inhibition of PE5 mutant enzyme variants at higher substrate concentration
cytosolic RNase inhibitor
-
-
-
FeSO4
-
-
H2O2
-
-
HP-RNase antibodies
-
affinity purified polyclonal antibodies against human pancreatic RNase. 94% inhibition with 50 ng
-
inhibit-Ace
-
86% inhibition at 6 U/ml
-
iodoacetate
-
-
Mg2+
-
-
ribonuclease inhibitor
RNasin
-
50 kDa protein inhibitor isolated from human placenta
-
ZnSO4
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Sodium citrate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.435 - 0.44
cyclic 2',3'-cytidine monophosphate
0.34 - 0.47
poly (C)
0.1 - 0.389
poly(A)poly(U)
-
1
cyclic 2',3'-CMP
-
-
0.0115 - 0.1059
poly(A)-poly(U)
-
0.032 - 0.16
poly(A)poly(U)
-
0.0409 - 4
poly(C)
4 - 5
tRNA
additional information
additional information
-
Michelis-Menten curves and catalytic efficiencies of HPR and its mutant variants on different substrates
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.36 - 0.45
cyclic 2',3'-cytidine monophosphate
13.3 - 16
poly (C)
1.57 - 14.71
poly(A)-poly(U)
-
0.0002 - 0.0065
poly(A)poly(U)
-
0.11 - 2833
poly(C)
additional information
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21.7 - 1067
poly(A)-poly(U)
-
15170 - 40670
poly(C)
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00042 - 0.00134
ribonuclease inhibitor
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028 - 0.029
H2O2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.017
-
pH 5.0, 37°C
10300
-
RNA
35000
-
poly(C)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
4
-
assay at
7.3 - 7.6
-
liver
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
-
pH 3.0: about 10% of activity maximum, pH 9.0: about 5% of activity maximum
7 - 7.8
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 70
-
25°C: about 5% of activity maximum, 70°C: about 45% of activity maximum
66.6
-
melting temperature of complex with human ribonuclease inhibitor
68
-
melting temperature of complex with bovine ribonuclease inhibitor
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
MGC cDNA clone
Manually annotated by BRENDA team
-
endothelial cells are the main source of serum enzyme
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
primary culture, HUVEC
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
analysis of synthesis and maturation, folding, quality control, and secretion, of pancreatic RNase in the endoplasmic reticulum of live cells, overview. Human RNase folds rapidly and is secreted mainly in glycosylated forms
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme lacks cytotoxic activity as it is inactivated by intracellular cytosolic ribonuclease inhibitor
evolution
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RNAS1_HUMAN
156
1
17644
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000 - 24000
-
fractions with one glycosylation site occupied, Asn34, SDS-PAGE
14020
-
milk, sedimentation ultracentrifugation
14750
-
mutant R4A/K6A/Q9E/D16G/S17N/T36Y/Q37R/G38W analyzed by MALDI-TOF mass spectrometry
15000
18000 - 26000
-
gel filtration
24000 - 36000
-
fractions with two or three glycosylation sites occupied, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
monomer
-
1 * 15000, pancreas, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme as dimer and tetramer after three-dimensional domain swapping, hanging-drop vapour-diffusion method, mixing of 1.6 mg/ml protein in 0.1 M sodium citrate buffer, pH 6.5, and 0.3 M NaCl, with reservoir solution containing 22% w/v PEG 8000, 0.1 M ammonium sulfate, X-ray diffraction structure determination and analysis at 2.70 A resolution
crystal structure analysis, PDB IDs 1GQV, 1QMT, 1RNF, and 1ANG
-
in complex with ribonuclease inhibitor protein, at 1.95 A resolution. Formation of 19 hydrogen bonds results in an extremely stable complex. Residues R39 and R91 are especially involved in complex stability
-
vapor-diffusion technique
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G38D
as active as wild type enzyme towards ssRNA, poly(C) and poly(U) single-stranded homopolymers. With 3fold reduction of the dsRNA degrading activity
K102A
as active as wild type enzyme towards ssRNA, poly(C) and poly(U) single-stranded homopolymers
K7A/N71A/E111A
ribonuclease inhibitor-resistant cytotoxic variant
Q28L/R31C/R32C/N34K/E111G
extremely cytotoxic
R4A
as active as wild type enzyme towards ssRNA, poly(C) and poly(U) single-stranded homopolymers
R4A/G38D/K102A
ADA variant, triple mutant. This variant shows 62% and 83% activity on poly(C) and poly(U), respectively, with respect to wild type enzyme
R4A/K6A/Q9E/D16G/S17N
more exolytic cleavage preference than parental pancreatic ribonuclease
D121A
-
Km-value for poly(C) is 2.4fold higher than wild-type value, Km-value for yeast tRNA is 1.25fold higher than wild-type value, turnover-number for poly(C) is 16.5fold lower than wild-type value, turnover-number for yeast tRNA is 1.3fold lower than wild-type value. ASp121 is crucial for the catalytic activity and may be involved in the depolymerization activity of the enzyme
G38D
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
G38R/R39G/N67R/N88R
-
20% of wild-type activity. Kd value of complex with ribonuclease inhibitor 0.032 nM
G89R/S90R
K62A
-
full catalytic activity, reduced protein stability and DNA unwinding activity
K6A
-
reduced catalytic activity on both ssRNA and dsRNA
K74A
-
altered seconday structure, reduced protein stability and DNA unwinding activity, reduced catalytic activity on both ssRNA and dsRNA
N67D/N88A/G89D/R91D
-
76% of wild-type activity. Kd value of complex with ribonuclease inhibitor 45 nM
Q28A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q28A/G38D
-
site-directed mutagenesis, the mutant shows reduced activity and thermal stability compared to the wild-type enzyme
Q28A/G38D/R39A
-
site-directed mutagenesis, the mutant shows highly reduced activity and thermal stability compared to the wild-type enzyme
Q28A/R39A
-
site-directed mutagenesis, the mutant shows reduced activity and thermal stability compared to the wild-type enzyme
Q28L
-
site-directed mutagenesis, the mutant shows enhanced activity compared to the wild-type enzyme
Q28L/R39A
-
site-directed mutagenesis, the mutant shows reduced activity and thermal stability compared to the wild-type enzyme
Q37R/R39D/K66R/N67G/G68D/G89R/S90G/R91D
-
PI5 variant
R31E/K66R/N67G/G68D/R91A
-
PE3I2 variant
R31E/Q37R/R39D/R91A
-
PE3I1 variant
R31E/R91A
-
PE3 variant
R32A
-
full catalytic activity
R39A
-
site-directed mutagenesis, the mutant shows reduced activity and thermal stability compared to the wild-type enzyme
R39A/G38D
-
site-directed mutagenesis, the mutant shows highly reduced activity and thermal stability compared to the wild-type enzyme
R39D/N67D/G89D/R91D
-
16% of wild-type activity. Kd value of complex with ribonuclease inhibitor 1000 nM
R39D/N67D/N88A/G89D
-
24% of wild-type activity. Kd value of complex with ribonuclease inhibitor 16 nM
R39D/N67D/N88A/G89D/R91D
-
30% of wild-type activity. Kd value of complex with ribonuclease inhibitor 1700 nM
R39D/N67D/N88A/R91D
-
48% of wild-type activity. Kd value of complex with ribonuclease inhibitor 278 nM
R39D/N88A/G89D/R91D
-
48% of wild-type activity. Kd value of complex with ribonuclease inhibitor 68 nM
R39L/N67L/N88A/G89L/R91L
-
143% of wild-type activity. Kd value of complex with ribonuclease inhibitor 30 nM
R4A/K6A/G89R/S90R
-
site-directed mutagenesis of mutant PE10
R4A/K6A/Q9E/D16G/S17N/G89R/S90R
-
site-directed mutagenesis, mutant PE5 is constructed from PM5 replacing Gly89 and Ser90 by Arg. PM5 codes for HP-RNase and incorporates the substitutions Arg4 and Lys6 to Ala, Gln9 to Glu, Asp16 to Gly, and Ser17 to Asn
R4A/K6A/Q9E/D16G/S17N/R31E/R91A
-
site-directed mutagenesis,mutant PE3 is constructed from PM5 replacing Arg31 and Arg91 by Glu and Ala, respectively. PM5 codes for HP-RNase and incorporates the substitutions Arg4 and Lys6 to Ala, Gln9 to Glu, Asp16 to Gly, and Ser17 to Asn
R4A/K6A/Q9E/D16G/S17N/T36Y/Q37R/G38W
-
29.6% catalytic efficiency of wild type
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32.1
-
mutant K74A, first melting temperature
51.8
-
mutant K74A, second melting temperature
53.2
-
mutant K62A, melting temperature
54
-
melting temperature, mutant R39D/N67D/G89D/R91D
54.5
-
mutant K6A, melting temperature
54.8
-
wild-type, melting temperature
55
-
mutant R32A, melting temperature
58
-
melting temperature, mutant R39D/N67D/N88A/G89D/R91D
61
-
melting temperature, mutant G38R/R39G/N67R/N88R
65
-
melting temperature, mutant R39L/N67L/N88A/G89L/R91L
70 - 80
-
immobilized enzyme retains a far greater fraction of activity at higher temperature with respect to the soluble enzyme
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilized enzyme retains 40-80% activity when incubated 30 min at 55°C with trypsin
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
at 29°C in 20% (v/v) ethanol, a significant portion of enzyme variant PM8, in which the sequence of the N-terminal domain has been substituted by that of bovine seminal ribonuclease and Pro101 has been substituted by Glu is in dimeric form without appearance of higher oligomers
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on heparin column and reversed-phase chromatography
-
gel filtration on a Mono S HR 5/5 FPLC column
-
gel filtration on SP-Sepharose column
-
of the recombinant protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli strain BL21 Codon Plus (x04DE3)-RIL
expression in CHO cells
-
expression in Escherichia coli
-
expression of wild-type and mutant enzymes in CHO-K1 cells
-
expression of wild-type and mutant enzymes in Escherichia coli
-
recombinant expression of enzyme mutants in Escherichia coli strain BL21(DE3)
-
RNase expression in CHO cells
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
a recombinant ribonuclease-resistant dimeric variant of human pancreatic ribonuclease is generated which is specifically toxic to cancer cells. Combining dimerization of pancreatic ribonuclease-inhibitor-resistance results in providing potent anti-tumor activity to human pancreatic ribonuclease. The cytotoxic variants of human pancreatic ribonuclease will be useful in designing protein therapeutics with low immunogenicity
diagnostics
-
increased N-glycosylation of Asn88 in serum pancreatic ribonuclease 1 is a diagnostic marker for pancreatic cancer. Development of an assay to specifically detect unglycosylated Asn88 in denatured RNase1, overview
drug development
-
the enzyme is an antitumor drug candidate
medicine
pharmacology
-
human antibody-pancreatic ribonuclease fusion proteins, referred to as immunoRNases, are proposed as an alternative to heterologous immunotoxins, without their immunogenicity and unspecific toxicity issue. But human pancreatic RNase and variants do not prove to be generally suitable as effector component for a therapeutic antibody drug development platform, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Anfinsen, C.B.; White, F.H.
The ribonucleases: occurence, structure and properties
The Enzymes, 2nd Ed. (Boyer, P. D. ; Lardy, H. ; Myrbck, K. , eds. )
5
95-122
1961
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
-
Manually annotated by BRENDA team
Dalaly, B.K.; Eitenmiller, R.R.; Friend, B.A.; Shahani, K.M.
Human milk ribonuclease
Biochim. Biophys. Acta
615
381-391
1980
Homo sapiens
Manually annotated by BRENDA team
Weickmann, J.L.; Elson, M.; Glitz, D.G.
Purification and characterization of human pancreatic ribonuclease
Biochemistry
20
1272-1278
1981
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Sorrentino, S.; Tucker, G.K.; Glitz, D.G.
Purification and characterization of a ribonuclease from human liver
J. Biol. Chem.
263
16125-16131
1988
Homo sapiens
Manually annotated by BRENDA team
Russo, N.; de Nigris, M.; Ciardiello, A.; Di Donato, A.; D'Alessio, G.
Expression in mammalian cells, purification and characterization of recombinant human pancreatic ribonuclease
FEBS Lett.
333
233-237
1993
Homo sapiens
Manually annotated by BRENDA team
Boix, E.; Wu, Y.; Vasandani, V.M.; Saxena, S.K.; Ardelt, W.; Ladner, J.; Youle, R.J.
Role of the N terminus in RNase A homologues: differences in catalytic activity, ribonuclease inhibitor interaction and cytotoxicity
J. Mol. Biol.
257
992-1007
1996
Bos taurus, Homo sapiens, Lithobates pipiens
Manually annotated by BRENDA team
Landre, J.B.P.; Hewett, P.W.; Olivot, J.M.; Friedl, P.; Ko, Y.; Sachinidis, A.; Moenner, M.
Human endothelial cells selectively express large amounts of pancreatic-type ribonuclease (RNase 1)
J. Cell. Biochem.
86
540-552
2002
Homo sapiens
Manually annotated by BRENDA team
Gaur, D.; Seth, D.; Batra, J.K.
Glycine 38 is crucial for the ribonucleolytic activity of human pancreatic ribonuclease on double-stranded RNA
Biochem. Biophys. Res. Commun.
297
390-395
2002
Homo sapiens
Manually annotated by BRENDA team
Sorrentino, S.; Naddeo, M.; Russo, A.; D'Alessio, G.
Degradation of double-stranded RNA by human pancreatic ribonuclease: Crucial Role of Noncatalytic Basic Amino Acid Residues
Biochemistry
42
10182-10190
2003
Homo sapiens (P07998), Homo sapiens
Manually annotated by BRENDA team
Bosch, M.; Benito, A.; Ribo, M.; Puig, T.; Beaumelle, B.; Vilanova, M.
A nuclear localization sequence endows human pancreatic ribonuclease with cytotoxic activity
Biochemistry
43
2167-2177
2004
Homo sapiens
Manually annotated by BRENDA team
Younus, H.; Owais, M.; Rao, D.N.; Saleemuddin, M.
Stabilization of pancreatic ribonuclease A by immobilization on Sepharose-linked antibodies that recognize the labile region of the enzyme
Biochim. Biophys. Acta
1548
114-120
2001
Homo sapiens
Manually annotated by BRENDA team
Peracaula, R.; Royle, L.; Tabares, G.; Mallorqui-Fernandez, G.; Barrabes, S.; Harvey, D.J.; Dwek, R.A.; Rudd, P.M.; de Llorens, R.
Glycosylation of human pancreatic ribonuclease: differences between normal and tumor states
Glycobiology
13
227-244
2003
Homo sapiens
Manually annotated by BRENDA team
Pous, J.; Canals, A.; Terzyan, S.S.; Guasch, A.; Benito, A.; Ribo, M.; Vilanova, M.; Coll, M.
Three-dimensional structure of a human pancreatic ribonuclease variant, a step forward in the design of cytotoxic ribonucleases
J. Mol. Biol.
303
49-60
2000
Homo sapiens
Manually annotated by BRENDA team
Gaur, D.; Batra, J.K.
Role of aspartic acid 121 in human pancreatic ribonuclease catalysis
Mol. Cell. Biochem.
275
95-101
2005
Homo sapiens
Manually annotated by BRENDA team
Dey, P.; Islam, A.; Ahmad, F.; Batra, J.K.
Role of unique basic residues of human pancreatic ribonuclease in its catalysis and structural stability
Biochem. Biophys. Res. Commun.
360
809-814
2007
Homo sapiens
Manually annotated by BRENDA team
Rodriguez, M.; Benito, A.; Ribo, M.; Vilanova, M.
Characterization of the dimerization process of a domain-swapped dimeric variant of human pancreatic ribonuclease
FEBS J.
273
1166-1176
2006
Homo sapiens (P07998), Homo sapiens
Manually annotated by BRENDA team
Johnson, R.J.; Lin, S.R.; Raines, R.T.
A ribonuclease zymogen activated by the NS3 protease of the hepatitis C virus
FEBS J.
273
5457-5465
2006
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Probst, J.; Brechtel, S.; Scheel, B.; Hoerr, I.; Jung, G.; Rammensee, H.; Pascolo, S.
Characterization of the ribonuclease activity on the skin surface
Genet. Vaccines Ther.
4
4
2006
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Barrabes, S.; Pages-Pons, L.; Radcliffe, C.M.; Tabares, G.; Fort, E.; Royle, L.; Harvey, D.J.; Moenner, M.; Dwek, R.A.; Rudd, P.M.; De Llorens, R.; Peracaula, R.
Glycosylation of serum ribonuclease 1 indicates a major endothelial origin and reveals an increase in core fucosylation in pancreatic cancer
Glycobiology
17
388-400
2007
Homo sapiens
Manually annotated by BRENDA team
Johnson, R.J.; McCoy, J.G.; Bingman, C.A.; Phillips, G.N.; Raines, R.T.
Inhibition of human pancreatic ribonuclease by the human ribonuclease inhibitor protein
J. Mol. Biol.
368
434-449
2007
Homo sapiens
Manually annotated by BRENDA team
Ueki, M.; Iida, R.; Fujihara, J.; Takeshita, H.; Yuasa, I.; Kominato, Y.; Yasuda, T.
Development of genotyping methods for single nucleotide polymorphism in the human pancreatic ribonuclease gene (RNASE1) and their application to population studies
Biochem. Genet.
46
145-153
2008
Homo sapiens (P07998), Homo sapiens
Manually annotated by BRENDA team
Koever, K.E.; Bruix, M.; Santoro, J.; Batta, G.; Laurents, D.V.; Rico, M.
The solution structure and dynamics of human pancreatic ribonuclease determined by NMR spectroscopy provide insight into its remarkable biological activities and inhibition
J. Mol. Biol.
379
953-965
2008
Homo sapiens (P07998), Homo sapiens
Manually annotated by BRENDA team
Torrent, G.; Ribo, M.; Benito, A.; Vilanova, M.
Bactericidal activity engineered on human pancreatic ribonuclease and onconase
Mol. Pharm.
6
531-542
2009
Homo sapiens, Lithobates pipiens
Manually annotated by BRENDA team
Merlino, A.; Avella, G.; Di Gaetano, S.; Arciello, A.; Piccoli, R.; Mazzarella, L.; Sica, F.
Structural features for the mechanism of antitumor action of a dimeric human pancreatic ribonuclease variant
Protein Sci.
18
50-57
2009
Homo sapiens (P07998), Homo sapiens
Manually annotated by BRENDA team
Geiger, R.; Gautschi, M.; Thor, F.; Hayer, A.; Helenius, A.
Folding, quality control, and secretion of pancreatic ribonuclease in live cells
J. Biol. Chem.
286
5813-5822
2011
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Rehman, M.T.; Dey, P.; Hassan, M.I.; Ahmad, F.; Batra, J.K.
Functional role of glutamine 28 and arginine 39 in double stranded RNA cleavage by human pancreatic ribonuclease
PLoS ONE
6
e17159
2011
Homo sapiens
Manually annotated by BRENDA team
Pica, A.; Merlino, A.; Buell, A.K.; Knowles, T.P.; Pizzo, E.; DAlessio, G.; Sica, F.; Mazzarella, L.
Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase
Acta Crystallogr. Sect. D
69
2116-2123
2013
Homo sapiens (P07998), Homo sapiens
Manually annotated by BRENDA team
Gagne, D.; Doucet, N.
Structural and functional importance of local and global conformational fluctuations in the RNase A superfamily
FEBS J.
280
5596-5607
2013
Gallus gallus, Homo sapiens, Danio rerio (A5HAK0), Bos taurus (P00669), Rattus norvegicus (P00684), Lithobates pipiens (P22069)
Manually annotated by BRENDA team
Schirrmann, T.; Frenzel, A.; Linden, L.; Stelte-Ludwig, B.; Willuda, J.; Harrenga, A.; Duebel, S.; Mueller-Tiemann, B.; Trautwein, M.
Evaluation of human pancreatic RNase as effector molecule in a therapeutic antibody platform
mAbs
6
367-380
2014
Homo sapiens
Manually annotated by BRENDA team
Vert, A.; Castro, J.; Ruiz-Martinez, S.; Tubert, P.; Escribano, D.; Ribo, M.; Vilanova, M.; Benito, A.
Generation of new cytotoxic human ribonuclease variants directed to the nucleus
Mol. Pharm.
9
2894-2902
2012
Homo sapiens
Manually annotated by BRENDA team
Huang, W.; Zhao, M.; Wei, N.; Wang, X.; Cao, H.; Du, Q.; Liang, Z.
Site-specific RNase A activity was dramatically reduced in serum from multiple types of cancer patients
PLoS ONE
9
e96490
2014
Homo sapiens
Manually annotated by BRENDA team
Nakata, D.
Increased N-glycosylation of Asn(88) in serum pancreatic ribonuclease 1 is a novel diagnostic marker for pancreatic cancer
Sci. Rep.
4
6715
2014
Homo sapiens
Manually annotated by BRENDA team
Attery, A.; Dey, P.; Tripathi, P.; Batra, J.K.
A ribonuclease inhibitor resistant dimer of human pancreatic ribonuclease displays specific antitumor activity
Int. J. Biol. Macromol.
107
1965-1970
2018
Homo sapiens (P07998), Homo sapiens
Manually annotated by BRENDA team