Information on EC 3.1.27.5 - pancreatic ribonuclease

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
3.1.27.5
-
RECOMMENDED NAME
GeneOntology No.
pancreatic ribonuclease
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in Cp or Up with 2',3'-cyclic phosphate intermediates
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9001-99-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
roe deer
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Cervus capreolus
red deer
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
topi, 2 forms: A and B differ in carbohydrate
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
muskrat
-
-
Manually annotated by BRENDA team
3 forms: A, B, C: same amino acid composition, B and C: glycoproteins, A: not
-
-
Manually annotated by BRENDA team
bullfrog
SwissProt
Manually annotated by BRENDA team
enzyme exhibits RNase activity as well as DNA-binding properties
-
-
Manually annotated by BRENDA team
eland
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
18S rRNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
show the reaction diagram
-
-
-
-
?
2',3'-cCMP + H2O
3'-CMP
show the reaction diagram
-
-
-
-
?
2',3'-cCMP + H2O
?
show the reaction diagram
-
-
-
-
?
28S rRNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
show the reaction diagram
-
-
-
-
?
5S rRNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
show the reaction diagram
-
-
-
-
?
6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine + H2O
?
show the reaction diagram
6-carboxyfluorescein-dArUdGdA-6-carboxytetramethylrhodamine + H2O
?
show the reaction diagram
-
-
-
-
?
benzyl uridine + H2O
benzyl alcohol + 3'-UMP
show the reaction diagram
-
of uridine or cytidine
-
-
?
CpA + H2O
adenosine + 3'-CMP
show the reaction diagram
CpG + H2O
guanosine + 3'-CMP
show the reaction diagram
-
-
-
-
?
cyclic 2',3'-cytidine monophosphate + H2O
3'-CMP
show the reaction diagram
cyclic 2',3'-nucleoside monophosphate + H2O
3'-phosphomononucleotides
show the reaction diagram
cyclic 2',3'-uridine monophosphate + H2O
3'-UMP
show the reaction diagram
-
-
-
-
ir
cytidine 2',3'-cyclic monophosphate + H2O
cytidine 3'-phosphate
show the reaction diagram
-
-
-
-
?
cytidine-2',3'-cyclic monophosphate + H2O
3'-CMP
show the reaction diagram
cytidinyl-3',5'-adenosine + H2O
adenosine + 3'-CMP
show the reaction diagram
DNA-RNA hybrids + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
show the reaction diagram
-
in seminal plasma
-
-
?
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
pentacytidylic acid + H2O
?
show the reaction diagram
-
-
-
-
?
poly (C) + H2O
3'-CMP + 3'-phospho-oligo(C)
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
poly(A) + H2O
3'-AMP + 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'-phospho-oligo(C)
show the reaction diagram
-
-
-
-
?
poly(C) + H2O
3'-CMP + 3'-phosphooligonucleotides
show the reaction diagram
poly(C) + H2O
?
show the reaction diagram
-
-
-
-
?
poly(I)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
?
show the reaction diagram
-
-
-
-
?
RNA + H2O
cyclic 2',3'-nucleoside monophosphate
show the reaction diagram
single-stranded RNA + H2O
?
show the reaction diagram
-
-
-
?
tRNA + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
show the reaction diagram
tRNA + H2O
?
show the reaction diagram
substrate yeast tRNA
-
-
?
tRNAlys + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
show the reaction diagram
-
-
-
-
?
tRNAMet + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
show the reaction diagram
-
-
-
-
?
tRNAPhe + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
show the reaction diagram
-
-
-
-
?
tRNAVal + H2O
3'-phosphomononucleotides + 3'-phosphooligonucleotides
show the reaction diagram
-
-
-
-
?
UpA + H2O
adenosine + 3'-UMP
show the reaction diagram
-
-
-
-
?
UpG + H2O
guanosine + 3'-UMP
show the reaction diagram
UpU + H2O
3'-UMP + uridine
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
additional information
?
-
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
Zn2+
-
enhance interaction with substrate but lower stability
additional information
-
no effect of bivalent cations on enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(-)-epigallocatechin-3-gallate
-
noncompetitive
1-(2,5-dideoxy-5-(4-carboxypiperidinyl)-beta-D-threo-pentofuranosyl)thymine
-
-
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')Nucleotides
-
-
-
2',3'-dideoxy-3'-(gamma-aminobutyric acid)amino thymidine
-
-
2',3'-dideoxy-3'-D-leucylamino thymidine
-
-
2',3'-dideoxy-3'-glycylamino thymidine
-
-
2',3'-dideoxy-3'-L-alanylamino thymidine
-
-
2',3'-dideoxy-3'-L-histidinylamino thymidine
-
-
2',3'-dideoxy-3'-L-leucylamino thymidine
-
-
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
2',3'-dideoxy-3'-L-valinylamino thymidine
-
-
2'-Deoxynucleotides
-
-
-
3'-CMP
3'-deoxy-3'-[4-(ethoxycarbonyl)piperidin-1-yl] uridine
-
-
3'-deoxy-3'-[4-carboxypiperidin-1-yl] uridine
-
-
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'-UMP
-
natural product inhibitor, NMR binding analysis, overview
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'-AMP
-
-
5'-carboxyadenosine
-
-
5'-carboxythymidine
-
-
5'-deoxy-5'-N-(4-carboxypiperidinyl)thymidine
-
-
5'-deoxy-5'-N-(4-carboxypiperidinyl)uridine
-
-
5'-deoxy-5'-piperidin-1-ylthymidine
-
-
5'-GMP
-
-
5'-N-(4-carboxypiperidinyl)-2',3'-didehydro-3',5'-dideoxythymidine
-
-
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
5-aminoethyluracil
-
-
5-Nitrouracil
-
-
adenosine 5'-phosphate
-
-
arsenite
-
-
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
BeCl2
-
-
CaCl2
-
-
chitosan
-
molecular weight about 6 kDA, complex formation with enzyme due to establishment of 5-6 ion pairs
chloride
-
-
Copolymer of glutamic acid and tyrosine
-
-
-
CuSO4
-
-
cytidine
-
-
cytidine 2',3'-cyclic monophosphate
-
substrate inhibition of PE5 mutant enzyme variants at higher substrate concentration
cytidine-N3-oxide 2'-phosphate
-
-
cytosolic ribonuclease inhibitor
cytosolic RNase inhibitor
-
-
-
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
FeSO4
-
-
folic acid
-
inhibitor when 2',3'-CMP is substrate not when RNA is substrate
green tea catechins
-
noncompetitive
-
HP-RNase antibodies
-
affinity purified polyclonal antibodies against human pancreatic RNase. 94% inhibition with 50 ng
-
Hydrobenzoinphosphate
-
-
inhibit-Ace
-
86% inhibition at 6 U/ml
-
iodoacetate
liver natural inhibitor
-
-
-
Mercury hematoporphyrin
-
-
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
-
-
NADP+
-
crystal structure of the complex with pancreatic ribonuclease A
NADPH
-
crystal structure of the complex with pancreatic ribonuclease A
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
oligonucleotides
-
e.g. ApUp
P1,P3-bis(5'-adenosyl) triphosphate
-
crystal structure of the complex with pancreatic ribonuclease A
penicillin
-
-
Phenylphosphate
-
-
Pholiota nameko polysaccharide
-
linear mixed-type inhibition, noncompetitive inhibition is predominant over competitive inhibition
-
phosphate
-
-
poly(vinylsulfonic acid)
-
-
poly(vinylsulfuric acid)
-
-
Polyanions
-
natural and synthetic, free poly(A), poly(U)
-
putrescine
-
-
Pyrophosphate
-
crystal structure of the complex with pancreatic ribonuclease A
ribonuclease inhibitor
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
-
RNasin
Selenite
-
-
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
trichloroacetic acid
-
partially inactivates
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
uridine 5'-diphosphate
-
competitive inhibitor
uridine 5'-phosphate
-
competitive inhibitor
vitamin B12
-
-
VO2+
-
in complex with nucleotide monophosphate
ZnSO4
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alkanediyl-alpha,omega-bis(hydroxyethyl methyl hexadecyl ammonium bromide)
-
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
-
butanediyl-1,4-bis(hydroxyethyl methyl hexadecyl ammonium bromide)
-
-
-
Chloroquine
-
at 0.13 mM
hexanediyl-1,6-bis(hydroxyethyl methyl hexadecyl ammonium bromide)
-
-
-
pentanediyl-1,5-bis(hydroxyethyl methyl hexadecyl ammonium bromide)
-
-
-
Sodium citrate
-
-
sulfate
decreases the distance between the catalytic His residues and increases the globular compactness
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.2 - 7.5
cyclic 2 ',3'-CMP
-
-
0.46 - 7
cyclic 2',3'-CMP
0.0023 - 0.44
cyclic 2',3'-cytidine monophosphate
2.4 - 3.5
cyclic 2',3'-UMP
0.31 - 13
cytidine-2',3'-cyclic monophosphate
0.38 - 22
cytidinyl-3',5'-adenosine
0.015 - 0.038
pentacytidylic acid
0.34 - 0.47
poly (C)
0.0115 - 0.1059
poly(A)-poly(U)
0.032 - 0.389
poly(A)poly(U)
0.0409 - 4
poly(C)
0.0005 - 5
tRNA
0.79
UpA
-
-
additional information
CpA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 2.5
cyclic 2',3'-CMP
0.36 - 12
cyclic 2',3'-cytidine monophosphate
0.6 - 3.7
cyclic 2',3'-UMP
27 - 323
pentacytidylic acid
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)
35.7
RNA
Bos taurus
-
pH 7.0, 37C
0.056 - 2.6
tRNA
additional information
additional information
Homo sapiens
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12 - 17400
6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine
21.7 - 1067
poly(A)-poly(U)
15170 - 40670
poly(C)
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08124
(-)-epigallocatechin-3-gallate
-
pH 6.0
0.229
1-(2,5-dideoxy-5-(4-carboxypiperidinyl)-beta-D-threo-pentofuranosyl)thymine
-
pH 7.5, 25C
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
-
-
0.08
2',3'-dideoxy-3'-L-serinylamino thymidine
-
-
0.451
2',3'-dideoxy-3'-L-tyrosylamino thymidine
-
-
0.103
3'-deoxy-3'-[4-(ethoxycarbonyl)piperidin-1-yl] uridine
-
-
0.12
3'-deoxy-3'-[4-carboxypiperidin-1-yl] uridine
-
-
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, 25C
0.0000037
5'-AMP
-
wild-type, pH 6.0
0.067
5'-carboxyadenosine
-
pH 7.5, 25C
0.193
5'-carboxythymidine
-
pH 7.5, 25C
0.162
5'-deoxy-5'-N-(4-carboxypiperidinyl)thymidine
-
pH 7.5, 25C
0.075
5'-deoxy-5'-N-(4-carboxypiperidinyl)uridine
-
pH 7.5, 25C
0.396
5'-deoxy-5'-piperidin-1-ylthymidine
-
-
0.000067
5'-GMP
-
wild-type, pH 6.0
0.25
5'-N-(4-carboxypiperidinyl)-2',3'-didehydro-3',5'-dideoxythymidine
-
pH 7.5, 25C
0.00021 - 0.00022
chitosan
0.1063
green tea catechins
-
pH 6.0
-
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
-
-
0.000000011 - 0.0004
oligo(vinylsulfonic acid)
0.2999 - 0.545
Pholiota nameko polysaccharide
5.5 - 11
phosphate
0.00024 - 0.0039
ribonuclease inhibitor
0.65
uridine 5'-diphosphate
-
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
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028 - 0.3
H2O2
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.017
-
pH 5.0, 37C
1.14
-
substrate poly(A)poly(U), dimethyl suberimidate-treated, monomeric RNase A, pH 7.0, 25C
1.55
-
substrate poly(A)poly(U), native, monomeric RNase A, pH 7.0, 25C
2.22
-
substrate poly(A)poly(U), cross-linked RNase A dimer, pH 7.0, 25C
3
-
enzyme monomer after lyophilization
3.52
-
pH 7.0, 65C
6.08
-
enzyme dimer form I
11.67
-
enzyme dimer form I
12.15
-
substrate poly(A)poly(U), domain-swapped RNase A C-dimer pH 7.0, 25C
12.67
-
substrate yeast RNA, cross-linked RNase A dimer, pH 7.0, 25C
13.33
-
substrate yeast RNA, cross-linked RNase A dimer, treated with dimethyl suberimidate, pH 7.0, 25C
25.21
-
substrate poly(A)poly(U), cross-linked RNase A dimer, treated with dimethyl suberimidate, pH 7.0, 25C
49.33
-
substrate yeast RNA, dimethyl suberimidate-treated, monomeric RNase A, pH 7.0, 25C
53.46
-
substrate yeast RNA, domain-swapped RNase A C-dimer pH 7.0, 25C
84.55
-
substrate yeast RNA, native, monomeric RNase A, pH 7.0, 25C
1100
-
brain, poly(C)
2400
-
brain, RNA
10300
-
RNA
11300
-
pancreas, RNA
22600
-
pancreas, poly(C)
35000
-
poly(C)
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
assay at
5
-
assay at
7 - 7.5
-
-
7.3 - 7.6
-
liver
7.4
-
assay at
7.8
-
seminal plasma
9.5
-
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
6 - 10
-
pH 6: about 15% of activity maximum, pH 10: about 10% of activity maximum
7 - 7.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 70
-
25C: about 5% of activity maximum, 70C: about 45% of activity maximum
66.6
-
melting temperature of complex with human ribonuclease inhibitor
68
-
melting temperature of complex with bovine ribonuclease inhibitor
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.55
isoelectric focusing
10.1
-
calculated
10.2
isoform RNase A-1
11
isoform RNase A-2; isoform RNase A-2, calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
endothelial cells are the main source of serum enzyme
Manually annotated by BRENDA team
specific expression of isoform RNase9, especially in caput and corpus. Expression is andorgen-dependent
Manually annotated by BRENDA team
weak expression
Manually annotated by BRENDA team
peripheral blood granulocyte; peripheral blood granulocyte
Manually annotated by BRENDA team
strong expression; strong expression
Manually annotated by BRENDA team
weak expression; weak expression; weak expression
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
enzyme is bound on the acrosomal domain of sperm
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
PDB
SCOP
CATH
ORGANISM
UNIPROT