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Enzyme Nomenclature
Information on EC 3.1.27.5 - pancreatic ribonuclease
Word Map on EC 3.1.27.5
- 3.1.27.5
- asthma
- inflammation
-
allergic
- airway
-
asthmatic
- bronchial
- granule
-
ribonucleases
-
atopic
- lavage
- nasal
- ige
-
neutrophil
-
self-incompatibility
- pollen
- sputum
-
degranulation
-
inhale
- rhinitis
- eosinophilia
- histamine
- myeloperoxidase
- tryptase
-
expiratory
-
angiogenin
-
ribonucleolytic
-
bronchoalveolar
-
provocation
- solanaceae
- pistil
- dermatitis
-
hyperresponsiveness
- gametophytic
-
wheezing
- methacholine
-
rosaceae
- prunus
-
allergen-induced
- dermatophagoides
-
budesonide
-
eotaxin
-
non-self
-
exhaled
-
rnaase
-
hypereosinophilic
-
spirometry
-
interleukin-5
-
s-protein
-
prick
- diagnostics
- medicine
-
allergen-specific
- biotechnology
- agriculture
- drug development
- synthesis
- analysis
- pharmacology
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
3.1.27.5
-
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RECOMMENDED NAME
GeneOntology No.
pancreatic ribonuclease
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
-
-
-
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
the catalytic site of the enzyme is mainly composed of His12, His119, Gln11, Lys41 and Asp121. The conformation of Lys41 and Gln11 are pH dependent and their occurrence is correlated to the release of a sulfate ion from the active site at neutral pH. The sulfate anion is progressively released with pH and water molecules occupy the active site at pH 7.1. The enzyme adopts different conformational states in different pH conditions. In the protonated state, Lys41 points towards the active site both in the presence and in the absence of sulfate and acts as a general base during catalysis
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
Gly38 and Glu111 are crucial for the catalytic activity
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
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
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
two isoforms of dimeric enzyme, D-I and D-II
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
protein with 124 amino acid residues and four intra-molecular disulfide bonds. In the presence of oxidized and reduced dithiothreitol at pH 8.0 and 25ŗC, the enzyme folds through pathways involving a rapid pre-equilibrium resulting in an ensemble of three-disulfide intermediate species. Protein disulfide isomerase catalyzes the conversion of the intermediates to the native enzyme, by acting as both a chaperone and an oxidase on the on-pathway intermediate
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
the enzyme is composed of 124 amino acid residues. The amino acid residues involved in catalysis are His12, His119 and Lys41. The enzyme has six substrate binding subsites. One of them, B1, binds only to pyrimidine nucleotides and prefers to bind cytidine rather than uridine. Thr45 of the B1 subsite contributes to the enzyme substrate specificity and plays an important role in catalysis. Phe120 in the B1 subsite enhances substrate binding with the aid of its pi electron and hydrophobicity. Asn71 in the B2 subsite is responsible for productive interactions leading to efficient activity, and Glu111 in the same subsite contributes to substrate binding only in the binding of guanosine. Lys7, Arg10 and Gln11 in the P2 subsite also play an important role in catalysis. Some amino acid residues are located in the vicinity of the catalytic residues and contribute to the catalytic reaction by interacting with catalytic residues. Lys7, Arg10 and Lys66 maintain the optimum pKa of His12 and His119. Asp121 positions the proper tautomer of His119. Phe120 is responsible for the strict positioning of His119, and contributes to conformational stability. Tyr97 is involved in maintaining the correct position of Lys41. Cys65-Cys72 are located close to the catalytic and substrate binding residues and contribute to the proper spatial alignment of these residues
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
pyrimidine-specific endoribonuclease which cleaves 3',5'-phosphodiester bonds of single strand RNA via transphosphorylation and subsequent hydrolysis reactions
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
protein of 128 amino acid residues, catalyses the cleavage of RNA specifically on the 3'-side of pyrimidine bases. The catalytic triad comprises His12, Lys41 and His119. The amino acid sequence of the enzyme is longer than that of its bovine counterpart, with four extra amino acid residues at the C-terminal region
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
sequential binding of the monomeric substrate in a concentration-dependent manner makes up the active site of the enzyme
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
His12, His119 and Lys41 comprise the catalytic site, and several other amino acid residues serve as substrate binding subsites. The mutagenic replacement of Phe120 causes a positional change in His119 and that is a major cause in decreasing the activity of the enzyme. Phe120 is important in fixing the proper spatial position of His119 near the C-terminal region for efficient activity. Phe120 interacts not directly with His119, but with the hydrophobic core
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
His119 and His12 play an important structural role in active site of RNase A
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
enzymatic reaction mechanism, analysis of different versions, e.g. mechanism of Mathias and Rabin for catalysis of the hydrolysis of cytidine 2',3'-cyclic phosphate by RNase A, overview. Model of the RNase A-substrate complex, subsites of RNase A. Bn, Rn, and Rho_n are nucleobase-, ribose-, and phosphate-binding subsites, respectively
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
RNase A catalyzes a well-characterized acid-base mechanism involving two histidines (His12 and His119) and a transition state stabilizing positive charge (Lys41). The transphosphorylation of a single-stranded RNA molecule by the enzyme yields a 2',3'-cyclic phosphomonoester intermediate, which can be expelled from the active site or hydrolyzed in a microscopic reverse reaction involving the same two histidines
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
RNase A catalyzes a well-characterized acid-base mechanism involving two histidines (His12 and His119) and a transition state stabilizing positive charge (Lys41). The transphosphorylation of a single-stranded RNA molecule by the enzyme yields a 2',3'-cyclic phosphomonoester intermediate, which can be expelled from the active site or hydrolyzed in a microscopic reverse reaction involving the same two histidines
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
RNase A catalyzes a well-characterized acid-base mechanism involving two histidines (His12 and His119) and a transition state stabilizing positive charge (Lys41). The transphosphorylation of a single-stranded RNA molecule by the enzyme yields a 2',3'-cyclic phosphomonoester intermediate, which can be expelled from the active site or hydrolyzed in a microscopic reverse reaction involving the same two histidines
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
RNase A catalyzes a well-characterized acid-base mechanism involving two histidines (His12 and His119) and a transition state stabilizing positive charge (Lys41). The transphosphorylation of a single-stranded RNA molecule by the enzyme yields a 2',3'-cyclic phosphomonoester intermediate, which can be expelled from the active site or hydrolyzed in a microscopic reverse reaction involving the same two histidines
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
RNase A catalyzes a well-characterized acid-base mechanism involving two histidines (His12 and His119) and a transition state stabilizing positive charge (Lys41). The transphosphorylation of a single-stranded RNA molecule by the enzyme yields a 2',3'-cyclic phosphomonoester intermediate, which can be expelled from the active site or hydrolyzed in a microscopic reverse reaction involving the same two histidines
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
RNase A catalyzes a well-characterized acid-base mechanism involving two histidines (His12 and His119) and a transition state stabilizing positive charge (Lys41). The transphosphorylation of a single-stranded RNA molecule by the enzyme yields a 2',3'-cyclic phosphomonoester intermediate, which can be expelled from the active site or hydrolyzed in a microscopic reverse reaction involving the same two histidines
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
9001-99-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme exhibits RNase activity as well as DNA-binding properties
-
-
-
134521, 134522, 134523, 134525, 134527, 134529, 134530, 134531, 134532, 134533, 134534, 134537, 134538, 134541, 134542, 134543, 134551, 134552, 134553, 134555, 134556, 134558, 134561, 134562, 134563, 134564, 24208, 655556, 663854, 663931, 664338, 665226, 665557, 666170, 677404, 677546, 678356, 678406, 678727, 678830, 679757, 679838, 680195, 680196, 681511, 681593, 682061, 682711, 682714, 682724, 682755, 690789, 707361, 707494, 707495, 707508, 707863, 708880, 709918, 710433, 710570, 717242, 717255, 717258, 717298, 717371, 717861, 717990, 718115, 718368, 729310, 729452, 729838
-
-
-
654675, 655979, 656308, 664231, 664308, 664330, 664830, 665486, 666860, 678349, 678519, 678585, 678729, 678745, 678746, 681377, 682742, 682767, 682880, 691341, 706955, 706977, 706984, 707243, 707728, 707730, 707748, 707756, 707757, 709180, 709463, 710510, 710511, 717377, 717596, 718374, 729327
Swissprot
expression in Nicotiana tabacum as a protection against tobacco mosaic virus
Swissprot
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
-
the enzyme belongs to the pancreatic-type secretory ribonuclease superfamily; the enzyme belongs to the pancreatic-type secretory ribonuclease superfamily as a unique natively dimeric member
evolution
the enzyme belongs to the vertebrate pancreatic-like RNase A superfamily, sequence comparisons and phylogenetic analysis, overview
evolution
the enzyme belongs to the vertebrate pancreatic-like RNase A superfamily, sequence comparisons and phylogenetic analysis, overview
evolution
-
the enzyme belongs to the vertebrate pancreatic-like RNase A superfamily, sequence comparisons and phylogenetic analysis, overview
evolution
-
the enzyme belongs to the vertebrate pancreatic-like RNase A superfamily, sequence comparisons and phylogenetic analysis, overview
evolution
the enzyme belongs to the vertebrate pancreatic-like RNase A superfamily, sequence comparisons and phylogenetic analysis, overview
evolution
the enzyme belongs to the vertebrate pancreatic-like RNase A superfamily, sequence comparisons and phylogenetic analysis, overview
evolution
-
the enzyme is a member of the pancreatic ribonuclease (RNase) superfamily
evolution
-
the enzyme is one of the key models in studies of evolutionary innovation and functional diversification, evolution and the function of Caniformia RNASE1 genes, phylogenetic analysis, overview. Four independent gene duplication events in the families of superfamily Musteloidea, including Procyonidae, Ailuridae, Mephitidae and Mustelidae
malfunction
-
mechanistic model for the denaturation of bovine pancreatic ribonuclease A in urea, a direct interaction between urea and protonated histidine as the initial step for protein inactivation followed by hydrogen bond formation with polar residues, and the breaking of hydrophobic collapse as the final steps for protein denaturation
malfunction
-
RNase A tandem enzymes, in which two RNase A molecules are artificially connected by a peptide linker, and thus have a pseudodimeric structure, exhibit remarkable cytotoxic activity, but can be inhibited by the cytosolic ribonuclease inhibitor in vitro. Structure modeling, overview
physiological function
-
His12 acts mainly as a general base in the catalytic process of RNase A
physiological function
-
the enzyme has almost no anti-tumoral property in pancreatic adenocarcinoma cell lines and in nontumorigenic cells as normal control, and is largely ineffective as anti-proliferative and pro-apoptotic agent; the enzyme has good anti-tumoral property in pancreatic adenocarcinoma cell lines and in nontumorigenic cells as normal control, it stimulates a strong anti-proliferative and pro-apoptotic effect in cancer cells. The enzyme triggers Beclin1-mediated autophagic cancer cell death, providing evidence that high proliferation rate of cancer cells may render them more susceptible to autophagy by treatment with the enzyme
physiological function
-
the human isozymes have evolved additional biological activities, often linked to innate host defense, neurotoxicity, angiogenesis, and immunosuppressive and/or antibacterial/antiviral activities
physiological function
-
cytotoxic human pancreatic ribonuclease variant PE5 is able to cleave nuclear RNA, inducing the apoptosis of cancer cells and reducing the amount of P-glycoprotein in different multidrug-resistant cell lines
additional information
-
analysis of the disulfide bond formation phase in detail in the oxidative folding, as the first of two folding phases, of RNase A, overview. Comparision of folding intermediates of reduced RNase A obtained at 25°C and different pH values from pH 4.0, pH 7.0, to pH 10.0, shuffling and transformation of different intermediate types, overview. The preconformational folding phase coupled with disulfide bond formation can be divided into two distinct subphases, a kinetic (or stochastic) disulfide bond formation phase and a thermodynamic disulfide bond reshuffling phase. The transition from kinetically formed to thermodynamically stabilized disulfide bond intermediates are induced by hydrophobic nucleation as well as generation of the native interactions
additional information
-
analysis of synthesis and maturation, folding, quality control, and secretion, of pancreatic RNase in the endoplasmic reticulum of live cells, overview. In contrast to the slow in vitro refolding, the protein folds almost instantly after translation and translocation into the endoplasmatic reticulum lumen. Despite high stability of the native protein, only about half of the RNase reaches a secretion competent, monomeric form and is rapidly transported from the rough endoplasmic reticulum via the Golgi complex to the extracellular space
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
additional information
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domain swapping, the process in which a structural unit is exchanged between monomers to create a dimer containing two versions of the monomeric fold, is believed to be an important mechanism for oligomerization and the formation of amyloid fibrils. In RNase residue P114 acts as a conformational gatekeeper, regulating interconversion between monomer and domain-swapped dimer forms, with cis and trans conformation, isomerization at P114 may facilitate population of a partially unfolded intermediate or alternative structure competent for domain swapping, overview
additional information
-
arginine 39 is crucial for the dsRNA melting activity, and Gly38 is required, both these residues are not directly involved in the RNA cleavage activity
additional information
-
pancreatic ribonuclease A shows domain swapping, a type of oligomerization in which monomeric proteins exchange a structural element, resulting in oligomers whose subunits recapitulate the native, monomeric fold, under extreme conditions, such as lyophilization from acetic acid. The major domain swaps dimer form of RNase A exchanges a beta-strand at its C-terminus to form a C-terminal domain-swapped dimer, mechanism, overview. Domain swapping occurs via a local high-energy fluctuation at the C-terminus
additional information
-
very subtle structural, chemical, and potentially motional variations contribute to ligand discrimination in the enzyme
additional information
-
the enzyme performs 3D domain swapping, a process by which two or more protein molecules exchange part of their structure to form intertwined dimers or higher oligomers
additional information
RNA subsites and reaction mechanism catalyzed by RNase A, molecular interactions between the RNA substrate and residues of the catalytic groove. The following residues are known to interact with each subsite: Lys66 (P0), Thr45 and Asp83 (B1), Gln11, His12, Lys41, His119, and Asp121 (P1), Asn71 and Glu111 (B2), and Lys7 and Arg10 (P2). Structure-function relationship, overview. Potential role for catalytic base His119 in ligand discrimination and/or stabilization in addition to its critical role in catalysis, molecular dynamic simulations show that His119 adopts both rotameric positions in solution, most likely experiencing conformational exchange over the course of a catalytic reaction. Functional importance of long-range conformational rearrangements in RNase A
additional information
RNA subsites and reaction mechanism catalyzed by RNase A, molecular interactions between the RNA substrate and residues of the catalytic groove. The following residues are known to interact with each subsite: Lys66 (P0), Thr45 and Asp83 (B1), Gln11, His12, Lys41, His119, and Asp121 (P1), Asn71 and Glu111 (B2), and Lys7 and Arg10 (P2). Structure-function relationship, overview. Potential role for catalytic base His119 in ligand discrimination and/or stabilization in addition to its critical role in catalysis, molecular dynamic simulations show that His119 adopts both rotameric positions in solution, most likely experiencing conformational exchange over the course of a catalytic reaction. Functional importance of long-range conformational rearrangements in RNase A
additional information
-
RNA subsites and reaction mechanism catalyzed by RNase A, molecular interactions between the RNA substrate and residues of the catalytic groove. The following residues are known to interact with each subsite: Lys66 (P0), Thr45 and Asp83 (B1), Gln11, His12, Lys41, His119, and Asp121 (P1), Asn71 and Glu111 (B2), and Lys7 and Arg10 (P2). Structure-function relationship, overview. Potential role for catalytic base His119 in ligand discrimination and/or stabilization in addition to its critical role in catalysis, molecular dynamic simulations show that His119 adopts both rotameric positions in solution, most likely experiencing conformational exchange over the course of a catalytic reaction. Functional importance of long-range conformational rearrangements in RNase A
additional information
-
RNA subsites and reaction mechanism catalyzed by RNase A, molecular interactions between the RNA substrate and residues of the catalytic groove. The following residues are known to interact with each subsite: Lys66 (P0), Thr45 and Asp83 (B1), Gln11, His12, Lys41, His119, and Asp121 (P1), Asn71 and Glu111 (B2), and Lys7 and Arg10 (P2). Structure-function relationship, overview; RNA subsites and reaction mechanism catalyzed by RNase A, molecular interactions between the RNA substrate and residues of the catalytic groove. The following residues are known to interact with each subsite: Lys66 (P0), Thr45 and Asp83 (B1), Gln11, His12, Lys41, His119, and Asp121 (P1), Asn71 and Glu111 (B2), and Lys7 and Arg10 (P2). Structure-function relationship, overview. Potential role for catalytic base His119 in ligand discrimination and/or stabilization in addition to its critical role in catalysis, molecular dynamic simulations show that His119 adopts both rotameric positions in solution, most likely experiencing conformational exchange over the course of a catalytic reaction. Functional importance of long-range conformational rearrangements in RNase A
additional information
RNA subsites and reaction mechanism catalyzed by RNase A, molecular interactions between the RNA substrate and residues of the catalytic groove. The following residues are known to interact with each subsite: Lys66 (P0), Thr45 and Asp83 (B1), Gln11, His12, Lys41, His119, and Asp121 (P1), Asn71 and Glu111 (B2), and Lys7 and Arg10 (P2). Structure-function relationship, overview. Potential role for catalytic base His119 in ligand discrimination and/or stabilization in addition to its critical role in catalysis, molecular dynamic simulations show that His119 adopts both rotameric positions in solution, most likely experiencing conformational exchange over the course of a catalytic reaction. Functional importance of long-range conformational rearrangements in RNase A
additional information
RNA subsites and reaction mechanism catalyzed by RNase A, molecular interactions between the RNA substrate and residues of the catalytic groove. The following residues are known to interact with each subsite: Lys66 (P0), Thr45 and Asp83 (B1), Gln11, His12, Lys41, His119, and Asp121 (P1), Asn71 and Glu111 (B2), and Lys7 and Arg10 (P2). Structure-function relationship, overview. Potential role for catalytic base His119 in ligand discrimination and/or stabilization in addition to its critical role in catalysis, molecular dynamic simulations show that His119 adopts both rotameric positions in solution, most likely experiencing conformational exchange over the course of a catalytic reaction. Functional importance of long-range conformational rearrangements in RNase A
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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
5S rRNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
-
-
-
?
DNA-RNA hybrids + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
in seminal plasma
-
-
?
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
-
second step of hydrolysis is irreversible
-
-
ir
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
-
second step of hydrolysis is irreversible
24208, 134521, 134522, 134523, 134525, 134527, 134529, 134530, 134531, 134532, 134533, 134534, 134537, 134538, 134541, 134542, 134543, 134551, 134552, 134555, 134563, 134564
-
-
ir
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
-
second step of hydrolysis is irreversible
-
-
ir
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
-
second step of hydrolysis is irreversible
-
-
ir
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
Cervus capreolus
-
second step of hydrolysis is irreversible
-
-
ir
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
-
second step of hydrolysis is irreversible
-
-
ir
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
-
second step of hydrolysis is irreversible
-
-
ir
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
-
second step of hydrolysis is irreversible
-
-
ir
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
-
second step of hydrolysis is irreversible
-
-
ir
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
-
second step of hydrolysis is irreversible
-
-
ir
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
-
second step of hydrolysis is irreversible
-
-
ir
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
-
second step of hydrolysis is irreversible
-
-
ir
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
-
-
-
-
?
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
-
second step of hydrolysis is irreversible
-
-
ir
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
-
second step of hydrolysis is irreversible
-
-
ir
cytidine-2',3'-cyclic monophosphate + H2O
3'-CMP
-
hydrolysis reaction
-
-
?
cytidinyl-3',5'-adenosine + H2O
adenosine + 3'-CMP
-
CpA, transphosphorylation reaction
-
-
?
double-stranded RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
in seminal plasma
-
-
?
double-stranded RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
dsRNA
-
-
?
double-stranded RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
yeast dsRNA
-
-
?
poly (C) + H2O
3'-CMP + 3'-phosphooligonucleotides
-
-
-
-
?
poly (C) + H2O
3'-CMP + 3'-phosphooligonucleotides
-
-
-
-
?
poly(A) + H2O
3'-AMP + 3'-oligonucleotides
poor substrate because of Thr45 in the substrate binding site of the enzyme that sterically excludes purine bases
-
-
?
poly(A)-poly(U) + H2O
?
-
the enzyme dimers degrade poly(A)-poly(U) dsRNA with an activity that increases with the increase of the oligomer's basicity
-
-
?
poly(C) + H2O
3'-CMP + 3'-phosphooligonucleotides
-
35 times more active than with poly(U)
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
24208, 134521, 134522, 134523, 134525, 134527, 134529, 134530, 134531, 134532, 134533, 134534, 134537, 134538, 134541, 134542, 134543, 134551, 134552, 134555, 134556, 134563, 134564
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
high-molecular-weight yeast RNA
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
yeast RNA
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
activity against double-stranded RNA and the antitumour action increase with the size of the oligomer
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
studies on radical scavenging activities of the ribonuclease inhibitor CPRI, a scavenger of pancreatic-type ribonucleases
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
substrate yeast RNA
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
Cervus capreolus
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
not: single-stranded homopolyribonucleotides other than poly(C) and poly(U)
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
wheat germ RNA
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
yeast RNA
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
studies on application to the purification of ribonuclease of Rana catesbeiana eggs using an aqueous-aqueous polymer phase system and a small-scale cross-axis coil planet centrifuge
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
specific for pyrimidine bases
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
enzyme attacks both predicted double- and single-stranded RNA stretches, with no evident preference for specific sequences or individual bases
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
-
first step of hydrolysis is reversible
-
-
r
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
-
first step of hydrolysis is reversible
24208, 134521, 134522, 134523, 134525, 134527, 134529, 134530, 134531, 134532, 134533, 134534, 134537, 134538, 134541, 134542, 134543, 134551, 134552, 134555, 134563, 134564
-
-
r
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
-
first step of hydrolysis is reversible
-
-
r
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
-
first step of hydrolysis is reversible
-
-
r
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
Cervus capreolus
-
first step of hydrolysis is reversible
-
-
r
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
-
first step of hydrolysis is reversible
-
-
r
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
-
first step of hydrolysis is reversible
-
-
r
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
-
first step of hydrolysis is reversible
-
-
r
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
-
first step of hydrolysis is reversible
-
-
r
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
-
first step of hydrolysis is reversible
-
-
r
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
-
first step of hydrolysis is reversible
-
-
r
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
-
first step of hydrolysis is reversible
-
-
r
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
-
first step of hydrolysis is reversible
-
-
r
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
-
first step of hydrolysis is reversible
-
-
r
tRNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
-
-
?
tRNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
tRNA from yeast
-
-
?
tRNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
onconase, similar enzyme
-
-
?
tRNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
alkaline RNase, similar enzyme
-
-
?
additional information
?
-
-
removal of RNA changes the structural stability of low mobility group nonhistone protein (LMG160), in the way that the molecule tends to become self-associated
-
-
-
additional information
?
-
-
6-carboxyfluorescein-dArU(dA)2-6-carboxytetramethylrhodamine as artificial substrate
-
-
-
additional information
?
-
the enzyme degrades single-stranded and/or double-stranded RNA
-
-
-
additional information
?
-
isoform RNase1 is bactericidal with potent activities against the gramnegative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
isoform RNase1 is bactericidal with potent activities against the gramnegative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
-
isoform RNase1 is bactericidal with potent activities against the gramnegative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
isoform RNase2 is bactericidal with potent activities against the gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
isoform RNase2 is bactericidal with potent activities against the gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
-
isoform RNase2 is bactericidal with potent activities against the gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
isoform RNase3 is bactericidal with potent activities against the gramnegative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
isoform RNase3 is bactericidal with potent activities against the gramnegative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
-
isoform RNase3 is bactericidal with potent activities against the gramnegative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
the enzyme degrades single-stranded and/or double-stranded RNA
-
-
-
additional information
?
-
enzyme is both angiogenic and bactericidal. Domains II, amino acids 71-76, and III, amino acids 89-104, of RNase A-2 are both important for bactericidal activity
-
-
-
additional information
?
-
enzyme is both angiogenic and bactericidal. Domains II, amino acids 71-76, and III, amino acids 89-104, of RNase A-2 are both important for bactericidal activity
-
-
-
additional information
?
-
-
the enzyme degrades single-stranded and/or double-stranded RNA
-
-
-
additional information
?
-
-
the four extra amino acid residues in the C-terminal region of the enzyme are proposed to be responsible for a decrease in the ability to cleave poly(C)
-
-
-
additional information
?
-
-
enzyme is pyrimidine-specific and also acts on 2'-OH modified residues
-
-
-
additional information
?
-
pancreatic ribonuclease does not act randomly and shows a more endonucleolytic pattern when compared with ribonuclease A. Pancreatic ribonuclease prefers the binding and cleavage of longer substrate molecules with the phosphodiester bond that is broken 8-11 nucleotides away from at least one of the ends of substrate
-
-
-
additional information
?
-
-
the enzyme shows high activity on double stranded RNA
-
-
-
additional information
?
-
-
the enzyme degrades single-stranded and/or double-stranded RNA
-
-
-
additional information
?
-
-
analysis of the site-specificity of serum RNases on double-stranded RNA substrates cleaving predominantly at 5'-U/A-3' and 5'-C/A-3' dinucleotide sites by real-time monitoring of RNase activity by fluorescence resonance energy transfer via short double strand RNA degradation
-
-
-
additional information
?
-
-
cytidine 2',3'-cyclic monophosphate is used as substrate
-
-
-
additional information
?
-
-
enzyme is pyrimidine-specific and also acts on 2'-OH modified residues
-
-
-
additional information
?
-
-
enzyme expressed in K-562 cell is cytotoxic and cytostatic, IC50 value 0.0009 mM
-
-
-
additional information
?
-
-
predominant cleavage sites for onconase are at UG and GG residues. With the tRNA substrates studied, the predominant cleavages mapin the triplet UGG located in the context of the variable loop or the D-arm of the tRNA
-
-
-
additional information
?
-
the enzyme degrades single-stranded and/or double-stranded RNA
-
-
-
additional information
?
-
the enzyme degrades single-stranded and/or double-stranded RNA
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
24208, 134521, 134522, 134523, 134525, 134527, 134529, 134530, 134531, 134532, 134533, 134534, 134537, 134538, 134541, 134542, 134543, 134551, 134552, 134555, 134556, 134563, 134564
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
Cervus capreolus
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
P14626
-
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
-
-
?
RNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
-
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
?
-
P00669
the enzyme degrades single-stranded and/or double-stranded RNA
-
-
-
additional information
?
-
A5HAK0
isoform RNase1 is bactericidal with potent activities against the gramnegative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
A5HAK2
isoform RNase1 is bactericidal with potent activities against the gramnegative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
-
isoform RNase1 is bactericidal with potent activities against the gramnegative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
A5HAK0
isoform RNase2 is bactericidal with potent activities against the gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
A5HAK2
isoform RNase2 is bactericidal with potent activities against the gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
-
isoform RNase2 is bactericidal with potent activities against the gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
A5HAK0
isoform RNase3 is bactericidal with potent activities against the gramnegative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
A5HAK2
isoform RNase3 is bactericidal with potent activities against the gramnegative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
-
isoform RNase3 is bactericidal with potent activities against the gramnegative bacteria Escherichia coli and Pseudomonas aeruginosa but only mild effects against the gram-positive bacteria Staphylococcus aureus
-
-
-
additional information
?
-
A5HAK0
the enzyme degrades single-stranded and/or double-stranded RNA
-
-
-
additional information
?
-
Q27J90
enzyme is both angiogenic and bactericidal. Domains II, amino acids 71-76, and III, amino acids 89-104, of RNase A-2 are both important for bactericidal activity
-
-
-
additional information
?
-
Q27J91
enzyme is both angiogenic and bactericidal. Domains II, amino acids 71-76, and III, amino acids 89-104, of RNase A-2 are both important for bactericidal activity
-
-
-
additional information
?
-
-
the enzyme degrades single-stranded and/or double-stranded RNA
-
-
-
additional information
?
-
-
the enzyme degrades single-stranded and/or double-stranded RNA
-
-
-
additional information
?
-
-
enzyme expressed in K-562 cell is cytotoxic and cytostatic, IC50 value 0.0009 mM
-
-
-
additional information
?
-
P22069
the enzyme degrades single-stranded and/or double-stranded RNA
-
-
-
additional information
?
-
P00684
the enzyme degrades single-stranded and/or double-stranded RNA
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
K+
Na+
Ni2+
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(2,5-dideoxy-5-pyrrolidin-1-yl-beta-L-erythro-pentofuranosyl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-(5-deoxy-5-morpholin-4-yl-alpha-L-arabinofuranosyl)pyrimidine-2,4(1H,3H)-dione
-
-
1-(5-deoxy-5-piperidin-1-yl-alpha-L-arabinofuranosyl)pyrimidine-2,4(1H,3H)-dione
-
-
1-(5-deoxy-5-pyrrolidin-1-yl-alpha-L-arabinofuranosyl)pyrimidine-2,4(1H,3H)-dione
-
-
1-(5-deoxy-5-[4-(ethoxycarbonyl)piperidin-1-yl]-alpha-L-arabinofuranosyl)pyrimidine-2,4(1H,3H)-dione
-
-
2',3'-dideoxy-3'-L-serinylamino thymidine
-
occupies the active site of ribonuclease A and preferential perturbs the pKa value of His-119 by its free amino group as found from 1H NMR studies, compounds with polar amino acid side chains such as Ser-aT, Tyr-aT and Trp-aT (except His-aT) are more efficient inhibitors compared to those having hydrophobic side chains
2',3'-dideoxy-3'-L-tryptophanylamino thymidine
-
compounds with polar amino acid side chains such as Ser-aT, Tyr-aT and Trp-aT (except His-aT) are more efficient inhibitors compared to those having hydrophobic side chains
2',3'-dideoxy-3'-L-tyrosylamino thymidine
-
compounds with polar amino acid side chains such as Ser-aT, Tyr-aT and Trp-aT (except His-aT) are more efficient inhibitors compared to those having hydrophobic side chains
3'-TMP
-
a competitive inhibitor analogue of the 3'-CMP and 3'-UMP natural product inhibitors, the enzyme shows very high affinty and strong binding with 3'-TMP. Binding of 3'-TMP is very similar to other natural and nonnatural pyrimidine ligands, so single nucleotide affinity is independent of the presence or absence of a 2'-hydroxyl on the ribose moiety of pyrimidines
3-amino-N-[2-hydroxymethyl-5-(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-tetrahydro-furan-3-yl]-succinamic acid
-
-
3-N-piperidine-4-carboxyl-3-deoxy-ara-uridine
-
binding of two inhibitor molecules in the central cavity of enzyme
4-[2-hydroxymethyl-5-(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-tetrahydro-furan-3-ylcarbamoyl]-butyric acid
-
-
5'-phospho-2'-deoxyuridine-3-diphosphate (P-5)-adenosine-3'-phosphate
-
i.e. pdUppA-3'-p, multi-ns molecular dynamics simulations of enzyme in complex with inhibitor
ATP
-
5-ATP binds with the adenine occupying the B2 subsite in the manner of an RNA substrate but with the gamma-phosphate at the P1 subsite, crystal structure of the complex with pancreatic ribonuclease A
aurintricarboxylic acid
-
alters the three-dimensional conformation, dissociation constant of ribonuclease A with aurintricarboxylic acid is 2.33 microM
chitosan
-
molecular weight about 6 kDA, complex formation with enzyme due to establishment of 5-6 ion pairs
cytidine 2',3'-cyclic monophosphate
-
substrate inhibition of PE5 mutant enzyme variants at higher substrate concentration
Diethylpyrocarbonate
-
among the His residues of RNase A, His48 is not accessible to react with diethylpyrocarbonate
epicatechin
-
0.04 mM, 4.4% inhibition, noncompetitve, CD spectral analysis of complex with enzyme, preferred site of binding is around residues 34-39 with possible hydrogen bonding to K7 and R10
Epicatechin gallate
-
0.04 mM, 12.7% inhibition, noncompetitve, CD spectral analysis of complex with enzyme, preferred site of binding is around residues 34-39 with possible hydrogen bonding to K7 and R10
epigallocatechin
-
0.04 mM, 6.9% inhibition, noncompetitve, CD spectral analysis of complex with enzyme, preferred site of binding is around residues 34-39 with possible hydrogen bonding to K7 and R10
epigallocatechin gallate
-
0.04 mM, 18.4% inhibition, noncompetitve, CD spectral analysis of complex with enzyme, preferred site of binding is around residues 34-39 with possible hydrogen bonding to K7 and R10
HP-RNase antibodies
-
affinity purified polyclonal antibodies against human pancreatic RNase. 94% inhibition with 50 ng
-
N-[2-hydroxymethyl-5-(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-tetrahydro-furan-3-yl]-malonamic acid
-
-
N-[2-hydroxymethyl-5-(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-tetrahydro-furan-3-yl]-oxalamic acid
-
-
N-[2-hydroxymethyl-5-(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-tetrahydro-furan-3-yl]-succinamic acid
-
-
oligo(vinylsulfonic acid)
-
potent competitive inhibitor making nearly 8 favorable Coulombic interactions with the enzyme. Oligo(vinylsulfonic acid) is inexpensive and extremely stable. Accoringly oligo(vinylsulfonic acid) has the potential to be useful prophylactic in many chemical, biochemical, and biotechnical experiments involving RNA
P1,P3-bis(5'-adenosyl) triphosphate
-
crystal structure of the complex with pancreatic ribonuclease A
Pholiota nameko polysaccharide
-
linear mixed-type inhibition, noncompetitive inhibition is predominant over competitive inhibition
-
ribonuclease inhibitor CPRI
-
scavenger of pancreatic-type ribonucleases, chemiluminescence assay to determine radical scavenging activities toward different reactive oxygen species (ROS) including superoxide anion, hydroxyl radical, lipid-derived radicals and singlet oxygen
-
ribonuclease protein inhibitor
-
the native enzyme is an equilibrium mixture of two isomers, MxM and M=M. In the former the two subunits swap their N-terminal helices. In the reducing environment of the cytosol, isoform M=M dissociates into monomers, which are strongly inhibited by ribonuclease protein inhibitor, wheras isoform MxM remains as a non-covalent dimer which evades ribonuclease protein inhibitor
-
RNase inhibitor
-
RNase A, like most monomeric RNases, is strongly bound and inactivated in mammalian cells by the RNase inhibitor
-
spermidine
-
RNA-binding enzyme activity is regulated through spermidine-induced changes in the charge and structure of the RNA substrate. Spermidine transiently stabilizes RNA sub-populations by binding both specifically and nonspecifically
spermine
-
at 0.13 mM: inhibition, at 0.02 M: activity towards cyclic substrates and poly(C) is activated, not towards poly(U)
Thiocyanate
inactivation due to expansion of the enzyme surface and elongation of the catalytic center
Urea
-
mechanism of inhibition, urea inhibits ribonuclease A competitively over a concentration range from 100 mM to 4.0 M, urea with its high dipolar moment is a competitive inhibitor and a very high concentration (more than 4.0 M) of it could denature the enzyme, beginning the interaction with the protein at the active center
3'-CMP
-
strong binding by the wild-type enzyme, reduced binding by enzyme mutants T17A and T82A, kinetics, overview
cytosolic ribonuclease inhibitor
-
with CpA as substrate, both isoenzymes are fully susceptible to inhibition
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cytosolic ribonuclease inhibitor
-
protects cells against exogenous ribonucleases, variants of pancreatic ribonuclease that evade ribonuclease inhibitor are cytotoxic, molecular evolution of ribonuclease inhibitor suggests to be a means to enhance the cytotoxicity of mammalian ribonucleases
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cytosolic ribonuclease inhibitor
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RI, from Sus scrofa, binding of the RI molecule to the N-terminal RNase A entity, analysis of crystal structures of the RIRNase A complex and the SGRSGRSG-RNase A tandem enzyme, PDB-ID 1DFJ, overview
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ribonuclease inhibitor
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extremely tight complex with bovine ribonuclease inhibitor, Kd value 0.69 fM. Kd value of complex with human ribonuclease inhibitor 0.34 fM
ribonuclease inhibitor
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human placental ribonuclease inhibitor, characterization of its tryptophan residues in the complex with the enzyme. The complex formation results in a more heterogenous environment for both of the optically resolved residues W19 and W375. W19 moves slightly toward a more hydrophobic region, ant the environment of W375 becomes less solvent exposed
ribonuclease inhibitor
human placental ribonuclease inhibitor; human placental ribonuclease inhibitor
ribonuclease inhibitor
-
tight complex with human ribonuclease inhibitor, Kd value 0.34 fM. Kd value of complex with bovine ribonuclease inhibitor 35 fM
ribonuclease inhibitor
-
crystallization data of complex with enzyme, formation of 19 hydrogen bonds results in extreme stability of complex. Kd value 29 * 10-8 nM
additional information
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construction of enzyme dimer composed of monomeric units covalently linked by a single amide bond between the side-chains of residues K66 and E9 by incubation of a lyophilized preparation of enzyme under vacuum at 85°C. Dimer exhibits a twofold increase in activity over monomeric enzyme and is not inhibited by the cellular ribonuclease inhibitor protein
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additional information
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As(III) species, by avid coordination to the cysteine residues of unfolded reduced proteins, can compromise protein folding pathways, monomethylarsenous acid catalyzes the formation of amyloid-like monodisperse fibrils using reduced ribonuclease A
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additional information
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agarose gel and precipitation assays show that the spacer length and the pKa of the carboxylic group have an important role in the inhibitory capacity
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additional information
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inhibitor synthesis, molecular docking to the enzyme, interaction of inhibitors with hydrogen bonding network formation between His12 and His119 of RNase A, overview
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additional information
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enzyme-inhibitor binding and interaction analysis, kinetics, overview
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alkanediyl-alpha,omega-bis(hydroxyethyl methyl hexadecyl ammonium bromide)
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the cationic gemini surfactants slightly activate and stabilize RNase A below their critical micelle concentrations at pH 5.0. The cationic gemini surfactant with the shorter spacer interacts more efficiently with RNase A than those with longer spacers, two-transition model, UV, circular dichorism and fluorescence spectroscopies, overview
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sulfate
decreases the distance between the catalytic His residues and increases the globular compactness
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.435
cyclic 2',3'-cytidine monophosphate
mutant R4A/K6A/Q9E/D16G/S17N, 25°C, pH 5.0
additional information
CpA
-
type I and II isoenzymes, almost identical values to those of commercial enzyme, pH 5.5, 25°C
additional information
cytidine-2',3'-cyclic monophosphate
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type I and II isoenzymes, almost identical values to those of commercial enzyme, pH 5.5, 25°C
additional information
additional information
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second-order rate constants for disulfide bond formation in the oxidative folding of RNase A with DHSox as an oxidant at 25°C, overview
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additional information
additional information
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Michelis-Menten curves and catalytic efficiencies of HPR and its mutant variants on different substrates
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.45
cyclic 2',3'-cytidine monophosphate
Homo sapiens
P07998
mutant R4A/K6A/Q9E/D16G/S17N, 25°C, pH 5.0
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12
6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine
Bos taurus
-
mutant enzyme M30C/N44C
139770
1044
6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine
Bos taurus
-
mutant enzyme I107C/A122C
139770
1566
6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine
Bos taurus
-
mutant enzyme H105C/V124C
139770
3132
6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine
Bos taurus
-
mutant enzyme A4C/V118C
139770
3480
6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine
Bos taurus
-
mutant enzyme V43C/R85C
139770
4002
6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine
Bos taurus
-
mutant enzyme R10C/R33C
139770
17400
6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine
Bos taurus
-
wild-type enzyme
139770
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.229
1-(2,5-dideoxy-5-(4-carboxypiperidinyl)-beta-D-threo-pentofuranosyl)thymine
-
pH 7.5, 25°C
0.423
1-(2,5-dideoxy-5-pyrrolidin-1-yl-beta-L-erythro-pentofuranosyl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
0.179
1-(5-deoxy-5-morpholin-4-yl-alpha-L-arabinofuranosyl)pyrimidine-2,4(1H,3H)-dione
-
-
0.172
1-(5-deoxy-5-piperidin-1-yl-alpha-L-arabinofuranosyl)pyrimidine-2,4(1H,3H)-dione
-
-
0.203
1-(5-deoxy-5-pyrrolidin-1-yl-alpha-L-arabinofuranosyl)pyrimidine-2,4(1H,3H)-dione
-
-
0.077
1-(5-deoxy-5-[4-(ethoxycarbonyl)piperidin-1-yl]-alpha-L-arabinofuranosyl)pyrimidine-2,4(1H,3H)-dione
-
-
0.037
3-amino-N-[2-hydroxymethyl-5-(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-tetrahydro-furan-3-yl]-succinamic acid
-
pH 7.5, 25°C
0.25
5'-N-(4-carboxypiperidinyl)-2',3'-didehydro-3',5'-dideoxythymidine
-
pH 7.5, 25°C
0.38
N-[2-hydroxymethyl-5-(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-tetrahydro-furan-3-yl]-malonamic acid
-
-
0.132
N-[2-hydroxymethyl-5-(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-tetrahydro-furan-3-yl]-oxalamic acid
-
-
0.918
N-[2-hydroxymethyl-5-(5-methyl-2,4-dioxo-3,4-dihydro-2H-pyrimidin-1-yl)-tetrahydro-furan-3-yl]-succinamic acid
-
-
0.65
uridine 5'-diphosphate
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binds to the active site of the enzyme by anchoring two molecules connected to each other by hydrogen bonds and van der Waals interactions
4
uridine 5'-phosphate
-
binds to the active site of the enzyme by anchoring two molecules connected to each other by hydrogen bonds and van der Waals interactions
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Bos taurus
-
radical scavenging activities of CPRI indicated, measured by chemiluminescence, values shown, radical scavenging activities higher than those of tea polyphenols
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.14
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substrate poly(A)poly(U), dimethyl suberimidate-treated, monomeric RNase A, pH 7.0, 25°C
13.33
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substrate yeast RNA, cross-linked RNase A dimer, treated with dimethyl suberimidate, pH 7.0, 25°C
25.21
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substrate poly(A)poly(U), cross-linked RNase A dimer, treated with dimethyl suberimidate, pH 7.0, 25°C
49.33
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substrate yeast RNA, dimethyl suberimidate-treated, monomeric RNase A, pH 7.0, 25°C
additional information
additional information
-
type I isoform, 100% specific activity relative to commercial RNase A. Type II isoform, 53% specific activity relative to commercial enzyme
additional information
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isoenzyme D-I shows values of 88 U/mg, 382 U/mg and 6.2 U/mg with yeast RNA, poly(U) and poly(A)poly(U) as substrates, respectively. D-II isoenzyme shows values of 85 U/mg, 387 U/mg and 2.5 U/mg with yeast RNA, poly(U) and poly(A)poly(U) as substrates, respectively
additional information
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for assay conditions ribonuclease A solution prepared by dissolving 8 mg ribonuclease A in 4 ml 0.1 M NaHCO3 at pH 9.5 following by pre-cooling to 3°C
additional information
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enzymatic activities of the various RNase A monomeric and zero-length or domain-swapped oligomeric species on single-stranded yeast or double-stranded poly(A)-poly(U) RNA, overview. The dimers show higher activity compared to the monomners
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.5
7.7
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 9
-
pH 3.0: about 10% of activity maximum, pH 9.0: about 5% of activity maximum
6 - 10
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pH 6: about 15% of activity maximum, pH 10: about 10% of activity maximum
7 - 7.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 70
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25°C: about 5% of activity maximum, 70°C: about 45% of activity maximum
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
specific expression of isoform RNase9, especially in caput and corpus. Expression is andorgen-dependent
peripheral blood granulocyte; peripheral blood granulocyte
-
-
706984, 707728, 707730, 707748, 707757, 708880, 709180, 709463, 709918, 710510, 710570, 717242, 717298, 717371, 717990, 718374, 729838
-
-
134521, 134522, 134523, 134534, 134537, 134538, 134542, 134543, 134551, 134552, 134553, 134555, 134556, 134558, 134559, 134561, 134562, 134563, 134564, 654126, 654675, 654993, 655538, 655556, 655907, 655910, 655979, 656308, 656315, 656631, 657293, 663931, 664231, 664330, 665226, 677404, 677546, 678349, 678502, 678519, 678727, 678732, 678745, 678746, 678830, 680195, 680196, 681377, 681511, 681593, 681707, 682271, 682355, 682711, 682714, 682767, 682880, 682969, 690789, 706955, 707863, 717242, 717298, 717371, 717861, 717990, 718374, 729310, 729452
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-
134523, 134538, 134554, 134556, 654423, 654672, 654739, 654814, 655687, 656482, 679735, 681432, 717861, 718274, 728871
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RNase activities are significantly reduced in serum samples of patients with gastric cancer, liver cancer, pancreatic cancer, esophageal cancer, ovary cancer, cervical cancer, bladder cancer, kidney cancer and lung cancer, while only minor changes are found in serum of breast and colon cancer patients compared to healthy controls. No difference in serum RNase levels between patients with primary and metastatic colon cancer
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
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analysis of synthesis and maturation, folding, quality control, and secretion, of pancreatic RNase in the endoplasmic reticulum of live cells, overview. In contrast to the slow in vitro refolding, the protein folds almost instantly after translation and translocation into the endoplasmatic reticulum lumen. Despite high stability of the native protein, only about half of the RNase reaches a secretion competent, monomeric form and is rapidly transported from the rough endoplasmic reticulum via the Golgi complex to the extracellular space, the rest remains in the endoplasmic reticulum mainly in the form of dimers and is slowly degraded
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additional information
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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
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PDB
SCOP
CATH
ORGANISM
UNIPROT