Information on EC 3.1.27.1 - ribonuclease T2

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.27.1
-
RECOMMENDED NAME
GeneOntology No.
ribonuclease T2
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric diester
-
-
hydrolysis of phosphoric ester
transphosphorylation
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
37278-25-4
-
9075-06-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
A3M929
UniProt
Manually annotated by BRENDA team
-
A3M929
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene RNASET2
-
-
Manually annotated by BRENDA team
strain CA265, rna gene
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
barley, 2 forms with different pH-optima: RNAase I, RNAase II
-
-
Manually annotated by BRENDA team
2 enzyme forms LC1 and LC2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene RNASET2
-
-
Manually annotated by BRENDA team
squid
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
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
2',3'-5-NO3-Up + H2O
?
show the reaction diagram
-
-
-
-
?
2',3'-cAMP + H2O
?
show the reaction diagram
-
-
-
-
?
2',3'-cCMP + H2O
?
show the reaction diagram
2',3'-cGMP + H2O
?
show the reaction diagram
-
-
-
-
?
2',3'-Cp + H2O
?
show the reaction diagram
-
-
-
-
?
2',3'-cUMP + H2O
?
show the reaction diagram
2',3'-cyclic NMP + H2O
3'(2')-NMP
show the reaction diagram
-
slower side reaction, intrinsic cyclic nucleotide phosphodiesterase activity
-
-
?
2',3'-Up + H2O
?
show the reaction diagram
-
-
-
-
?
5'-CCCCACCACCAUCACUU-3'
?
show the reaction diagram
-
37C, single stranded 17-mer
-
-
?
adenosine-3'-(1-naphthyl)phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
adenylyl (3'-5')uridine + H2O
?
show the reaction diagram
-
-
-
-
?
ApA + H2O
?
show the reaction diagram
ApA + H2O
AMP + adenosine
show the reaction diagram
-
-
-
-
?
ApC + H2O
?
show the reaction diagram
-
-
-
-
?
ApC + H2O
AMP + cytosine
show the reaction diagram
-
-
-
-
?
ApG + H2O
?
show the reaction diagram
ApG + H2O
AMP + guanosine
show the reaction diagram
-
-
-
-
?
ApU + H2O
?
show the reaction diagram
-
-
-
-
?
ApU + H2O
AMP + uridine
show the reaction diagram
-
-
-
-
?
CpA + H2O
?
show the reaction diagram
-
-
-
-
?
CpA + H2O
CMP + adenosine
show the reaction diagram
-
-
-
-
?
CpC + H2O
CMP + cytidine
show the reaction diagram
-
-
-
-
?
CpG + H2O
?
show the reaction diagram
-
-
-
-
?
CpG + H2O
CMP + guanosine
show the reaction diagram
-
-
-
-
?
CpU + H2O
3'-CMP + uridine
show the reaction diagram
-
-
-
-
?
CpU + H2O
?
show the reaction diagram
-
-
-
-
?
cytidylyl-3',5'-uridine
?
show the reaction diagram
37C, pH 5.5
-
-
?
GpA + H2O
GMP + adenosine
show the reaction diagram
GpC
?
show the reaction diagram
-
pH 5.0, 22C
-
-
?
GpC + H2O
GMP + cytosine
show the reaction diagram
-
-
-
-
?
GpG + H2O
?
show the reaction diagram
-
-
-
-
?
GpG + H2O
GMP + guanosine
show the reaction diagram
-
best substrate
-
-
?
GpU + H2O
?
show the reaction diagram
-
-
-
-
?
GpU + H2O
GMP + uridine
show the reaction diagram
-
-
-
-
?
IpU + H2O
?
show the reaction diagram
-
-
-
-
?
nucleotidyl-3',5'-nuceotide + H2O
2',3'-cyclic NMP + 3'(2')-NMP
show the reaction diagram
-
determination of base specificity
-
-
?
poly-8 adenylic acid
AMP + ?
show the reaction diagram
RNA
?
show the reaction diagram
-
acetate buffer pH 5.0 or Tris-HCl pH 7.5, 37 C, 5 min incubation
-
-
?
RNA + H2O
2',3'-cyclic NMP + 3'(2')-NMP
show the reaction diagram
-
high-molecular weight fraction of RNA from Torula yeast, typeII-S
2',3'-cyclic NMPs are are further hydrolyzed in a side reaction
-
?
RNA + H2O
3'-phosphomononucleotides
show the reaction diagram
RNA + H2O
5'-phosphomononucleotides
show the reaction diagram
-
hydrolyzes in 3'- to 5'-direction, hydrolyzes single stranded RNA
-
?
RNA + H2O
?
show the reaction diagram
RNA + H2O
nucleoside 3'-phosphates + 3'-phosphooligonucleotides
show the reaction diagram
RNA + H2O
nucleoside 3'-phosphates and 3'-phosphooligonucleotides
show the reaction diagram
UpA + H2O
?
show the reaction diagram
-
-
-
-
?
UpA + H2O
UMP + adenosine
show the reaction diagram
-
-
-
-
?
UpC + H2O
UMP + cytosine
show the reaction diagram
-
-
-
-
?
UpG + H2O
?
show the reaction diagram
-
-
-
-
?
UpG + H2O
UMP + guanosine
show the reaction diagram
-
-
-
-
?
UpU + H2O
?
show the reaction diagram
-
-
-
-
?
UpU + H2O
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
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
improves the activity to some extent
Ca2+
-
improves the activity to some extent
Cu2+
-
ion inhibits DNA hydrolyzing activity
CuSO4
-
activates immobilized enzyme, inhibits soluble
Hg2+
-
ion inhibits DNA hydrolyzing activity
KCl
-
enhances activity
KH2PO4
-
slight activation
NaCl
-
enhances activity
NaF
-
enhances activity
Zn2+
-
ion inhibits DNA hydrolyzing activity
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'(3')-UMP
2'-AMP
2'-CMP
2'-GMP
3'-AMP
4-chloromercuribenzoic acid
-
80% inhibition of RNase LE at 1 mM
Ag+
-
complete inhibition at 10 mM
Al3+
-
complete inhibition at 10 mM
deoxyadenosine
-
-
deoxycytidine
-
-
deoxyguanosine
-
-
deoxyuridine
-
-
diethyl dicarbonate
DNA
-
denatured
heparin
iodoacetamide
iodoacetate
iodoacetic acid
-
-
MgCl2
poliovirus RNA
-
-
-
protein Im5
-
immunity protein, in the study different mutants of Im5 are investigated
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2',5'-linked oligoadenylates
two different binding sites in the enzyme's ANK domain and a third site in the N lobe of the KH domain, sensing mechanism, structure-function analysis, overview. The KH/KH and kinase extension nuclease (KEN)/KEN interfaces are important in 2',5'-oligoadenylate-dependent enzyme activation
-
2',5'-Oligoadenylate
2',5'-oligoadenylates
-
2-5A
-
2'-5'-linked oligoadenylates
-
natural 2'-5'-linked tetraadenylates and three tetramers with 3'-end AMP units replaced with ribo-, arabino- and xylo-configured phosphonate analogues of AMP are enzyme activators with equal potency. The enzyme is activated by the binding of 2'-5'-linked oligoadenylates to the N-terminal ankyrin repeat domain, which causes the inactive monomer to form a catalytically active homodimer
-
2'-5'-oligoadenylate
-
short polyadenylate molecules that are connected by unique 2'-5' linkages, collectively referred to as 2-5A. 2-5A induces dimerization via the ANK domain and this dimerization correlates with activation of ribonuclease activity
citrate
-
25 mM sodium citrate buffer results in 170% activity compared to 100% activity in sodium acetate buffer, both pH 5.6
MgCl2
-
stimulates DNA hydrolyzing activity
phosphate
-
25 mM sodium phosphate buffer results in 153% activity compared to 100% activity in sodium acetate buffer, both pH 5.6
viral dsRNA
-
viral dsRNA provokes the synthesis of 2'-5' oligoadenylate, 2-5A, binding of 2-5A to ankyrin repeats of monomeric RNase L leads to RNase L dimerization and activation
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
2',3'-5-NO3-Up
-
-
0.23
2',3'-cAMP
-
-
0.16 - 0.4
2',3'-cCMP
6.5
2',3'-cGMP
-
-
0.025
2',3'-Cp
-
-
0.43 - 6.1
2',3'-cUMP
0.4
2',3'-mUp
-
-
0.03
2',3'-Up
-
-
0.0198 - 0.5889
adenosine 3'-(1-naphthyl)phosphate
0.0182 - 0.0203
adenylyl(3'-5')uridine
0.005 - 0.065
ApA
0.025 - 0.13
ApC
0.003 - 1.14
ApG
0.03 - 0.078
ApU
0.02 - 0.13
CpA
0.047 - 0.049
CpC
0.11 - 2.15
CpG
0.076 - 20
CpU
0.02 - 0.072
GpA
0.107 - 0.11
GpC
0.044 - 0.71
GpG
0.075 - 0.12
GpU
0.45
IpU
-
-
0.05 - 0.144
UpA
0.066 - 0.068
UpC
0.06 - 0.69
UpG
0.113 - 0.22
UpU
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00583 - 0.176
adenosine-3'-(1-naphthyl)phosphate
0.0128 - 0.0543
adenylyl (3'-5')uridine
5.37 - 13.1
CpU
2.97
GpC
Oncorhynchus keta
-
pH 5.0, 22C
0.15
RNA
Escherichia coli
-
-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.18
-
purified recombinant mutant F101K
0.7
-
purified recombinant mutant F101R
7.8
-
purified recombinant mutant F101A
8.6
-
purified recombinant mutant F101Q
22
-
purification step crude extract
60
-
purified recombinant mutant F101I
89
-
purification step acetone precipitation
110
-
purified recombinant mutant F101W
150
-
purified recombinant mutant Q32F
251
-
purification step CM-cellulose ion exchange
330
-
purified recombinant mutant Q32N
340
-
purified recombinant mutant F101L
420
-
purified recombinant mutant Q32D
426
-
purification step DEAE ion exchange
583
-
purified enzyme
620
-
purified recombinant mutant Q32V
630
-
purification step Sephadex gel filtration
968
-
purified enzyme
1250
-
purified recombinant mutant Q32E
1800
-
purified recombinant mutant Q32L
2000
-
purified recombinant mutant Q32T
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6 - 6
assay at
5 - 6
-
acidic optimum with yeast RNA as a substrate
5.7
-
RNAase I
5.8
-
DNA hydrolyzing activity assay; RNase activity assay
6 - 6.3
-
hydrolysis of various nucleoside 2',3'-cyclic phosphates, degradation of 3'-nucleotide benzyl ester
6.4
-
RNAase II
7.5
-
assay at
7.6
-
RNase assay
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 5.5
-
pH 3.5, 5.5: about 70% of activity maximum, soluble and immobilized enzyme
3.5 - 6
-
pH 3.5: 80% of activity maximum, soluble and immobilized form, pH 6: soluble form 100%, immobilized form 90% of maximum acitivity
3.5 - 6.5
-
pH 3.5: about 20% of activity maximum, 6.5: less than 10% of activity maximum
5 - 8.5
-
enzyme retains more than half of its activity
7.5 - 8.5
-
pH 7.5, pH 8.5: 85% of activity maximum
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
40
-
DNA hydrolyzing activity assay
62
-
soluble and immobilized enzyme
additional information
-
assay temperatures depending on substrate
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
-
-
25 - 30
-
RNA cleavage assay
30 - 60
-
less than 25% of maximal activity above and below
40 - 80
-
40C, 80C: less than 15% of maximal activity above and below
40 - 70
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
about, RNase LV-3, isoelectric focusing
4.9
-
about, RNase LV-1, isoelectric focusing; about, RNase LV-2, isoelectric focusing; about, RNase LX, isoelectric focusing
10
-
above
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
in all tissues; in all tissues; in all tissues
Manually annotated by BRENDA team
in all tissues; in all tissues; in all tissues
Manually annotated by BRENDA team
; low level of RNase Dre1; low level of RNase Dre1
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
; low level of RNase Dre1; low level of RNase Dre1
Manually annotated by BRENDA team
RNaseLE transcript accumulation occurs preferentially upon wounding
Manually annotated by BRENDA team
main and lateral roots
Manually annotated by BRENDA team
; low level of RNase Dre1; low level of RNase Dre1
Manually annotated by BRENDA team
additional information