BRENDA - Enzyme Database
show all sequences of 2.7.4.B2

Polyphosphate:AMP phosphotransferase as a polyphosphate-dependent nucleoside monophosphate kinase in Acinetobacter johnsonii 210A

Shiba, T.; Itoh, H.; Kameda, A.; Kobayashi, K.; Kawazoe, Y.; Noguchi, T.; J. Bacteriol. 187, 1859-1865 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene pap, construction of a cDNA library expressed in Escherichia coli, DNA and amino acid sequence determination and analysis, overexpression of pPAP2 from plasmid in Escherichia coli strain JM109
Acinetobacter johnsonii
Inhibitors
Inhibitors
Commentary
Organism
Structure
ammonium sulfate
slightly inhibitory at 50 mM
Acinetobacter johnsonii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.27
-
AMP
recombinant PAP, pH 8.0, 37°C
Acinetobacter johnsonii
0.45
-
AMP
recombinant PAP, pH 8.0, 37°C, in presence of 50 mM (NH4)2SO4
Acinetobacter johnsonii
4.4
-
GMP
recombinant PAP, pH 8.0, 37°C
Acinetobacter johnsonii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
specifically required, lowers the Km for the nucleotide substrate
Acinetobacter johnsonii
additional information
other metal ions such as Mn2+, Fe2+, Ca2+, Cu2+, Zn2+, and Co2+ cannot enhance the activity
Acinetobacter johnsonii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
55800
-
x * 55800, recombinant pPAP2, SDS-PAGE
Acinetobacter johnsonii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
AMP + [phosphate]n
Acinetobacter johnsonii
-
ADP + [phosphate]n-1
-
-
?
AMP + [phosphate]n
Acinetobacter johnsonii 210A
-
ADP + [phosphate]n-1
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Acinetobacter johnsonii
Q83XD3
gene pap, plasmid containing the pap gene, designated pPAP2
-
Acinetobacter johnsonii 210A
Q83XD3
gene pap, plasmid containing the pap gene, designated pPAP2
-
Purification (Commentary)
Commentary
Organism
recombinant pPAP2 dimer 22.1fold from Escherichia coli strain JM109 by ammonium sulfate fractionation, anion exchange and hydroxyapatite chromatography, and gel filtration
Acinetobacter johnsonii
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.48
-
crude extract of recombinant Escherichia coli strain JM109, pH 8.0, 37°C
Acinetobacter johnsonii
24.9
-
purified recombinant PAP tetramer, pH 8.0, 37°C
Acinetobacter johnsonii
54.9
-
purified recombinant PAP dimer, pH 8.0, 37°C
Acinetobacter johnsonii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
AMP + [phosphate]n
-
722513
Acinetobacter johnsonii
ADP + [phosphate]n-1
-
-
-
?
AMP + [phosphate]n
best substrate
722513
Acinetobacter johnsonii
ADP + [phosphate]n-1
-
-
-
?
AMP + [phosphate]n
-
722513
Acinetobacter johnsonii 210A
ADP + [phosphate]n-1
-
-
-
?
AMP + [phosphate]n
best substrate
722513
Acinetobacter johnsonii 210A
ADP + [phosphate]n-1
-
-
-
?
CMP + [phosphate]n
0.09% of the activity with AMP
722513
Acinetobacter johnsonii
CDP + [phosphate]n-1
-
-
-
?
CMP + [phosphate]n
0.09% of the activity with AMP
722513
Acinetobacter johnsonii 210A
CDP + [phosphate]n-1
-
-
-
?
dAMP + [phosphate]n
18% of the activity with AMP
722513
Acinetobacter johnsonii
dADP + [phosphate]n-1
-
-
-
?
dCMP + [phosphate]n
0.008% of the activity with AMP
722513
Acinetobacter johnsonii
dCDP + [phosphate]n-1
-
-
-
?
dGMP + [phosphate]n
2.6% of the activity with AMP
722513
Acinetobacter johnsonii
dGDP + [phosphate]n-1
-
-
-
?
GMP + [phosphate]n
10% of the activity with AMP
722513
Acinetobacter johnsonii
GDP + [phosphate]n-1
-
-
-
?
GMP + [phosphate]n
10% of the activity with AMP
722513
Acinetobacter johnsonii 210A
GDP + [phosphate]n-1
-
-
-
?
IMP + [phosphate]n
2.2% of the activity with AMP
722513
Acinetobacter johnsonii
IDP + [phosphate]n-1
-
-
-
?
additional information
PAP acts as a poly(P)-dependent NMP kinase, activity for AMP by PAP is about 10times greater than that for GMP and 770 and about 1100times greater than that for UMP and CMP. ATP production by the coupled reactions of recombinant PAP and purified Escherichia coli poly(P) kinases from AMP. The purified recombinant PAP enzyme has not only strong PAP activity but also shows poly(P)-dependent nucleoside monophosphate kinase activity, by which it converts ribonucleoside monophosphates and deoxyribonucleoside monophosphates into ribonucleoside diphosphates and deoxyribonucleoside diphosphates, respectively
722513
Acinetobacter johnsonii
?
-
-
-
-
additional information
PAP acts as a poly(P)-dependent NMP kinase, activity for AMP by PAP is about 10times greater than that for GMP and 770 and about 1100times greater than that for UMP and CMP. ATP production by the coupled reactions of recombinant PAP and purified Escherichia coli poly(P) kinases from AMP. The purified recombinant PAP enzyme has not only strong PAP activity but also shows poly(P)-dependent nucleoside monophosphate kinase activity, by which it converts ribonucleoside monophosphates and deoxyribonucleoside monophosphates into ribonucleoside diphosphates and deoxyribonucleoside diphosphates, respectively
722513
Acinetobacter johnsonii 210A
?
-
-
-
-
TMP + [phosphate]n
0.012% of the activity with AMP
722513
Acinetobacter johnsonii
TDP + [phosphate]n-1
-
-
-
?
UMP + [phosphate]n
0.13% of the activity with AMP
722513
Acinetobacter johnsonii
UDP + [phosphate]n-1
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 55800, recombinant pPAP2, SDS-PAGE
Acinetobacter johnsonii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
recombinant enzyme
Acinetobacter johnsonii
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
30
50
the level of activity at 50°C is 3.2fold and 1.8fold higher than that at 30°C and 37°C, respectively
Acinetobacter johnsonii
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
45
-
purified recombinant PAP, 10 min, 40% activity remaining without polyphosphate, 85% activity remaining in presence of 10 mM polyphosphate
Acinetobacter johnsonii
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
35
-
GMP
recombinant PAP, pH 8.0, 37°C
Acinetobacter johnsonii
151.7
-
AMP
recombinant PAP, pH 8.0, 37°C, in presence of 50 mM (NH4)2SO4
Acinetobacter johnsonii
166.7
-
AMP
recombinant PAP, pH 8.0, 37°C
Acinetobacter johnsonii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
9
recombinant enzyme
Acinetobacter johnsonii
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
7
11
purified recombinant enzyme, stable at
Acinetobacter johnsonii
Cloned(Commentary) (protein specific)
Commentary
Organism
gene pap, construction of a cDNA library expressed in Escherichia coli, DNA and amino acid sequence determination and analysis, overexpression of pPAP2 from plasmid in Escherichia coli strain JM109
Acinetobacter johnsonii
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ammonium sulfate
slightly inhibitory at 50 mM
Acinetobacter johnsonii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.27
-
AMP
recombinant PAP, pH 8.0, 37°C
Acinetobacter johnsonii
0.45
-
AMP
recombinant PAP, pH 8.0, 37°C, in presence of 50 mM (NH4)2SO4
Acinetobacter johnsonii
4.4
-
GMP
recombinant PAP, pH 8.0, 37°C
Acinetobacter johnsonii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
specifically required, lowers the Km for the nucleotide substrate
Acinetobacter johnsonii
additional information
other metal ions such as Mn2+, Fe2+, Ca2+, Cu2+, Zn2+, and Co2+ cannot enhance the activity
Acinetobacter johnsonii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
55800
-
x * 55800, recombinant pPAP2, SDS-PAGE
Acinetobacter johnsonii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
AMP + [phosphate]n
Acinetobacter johnsonii
-
ADP + [phosphate]n-1
-
-
?
AMP + [phosphate]n
Acinetobacter johnsonii 210A
-
ADP + [phosphate]n-1
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant pPAP2 dimer 22.1fold from Escherichia coli strain JM109 by ammonium sulfate fractionation, anion exchange and hydroxyapatite chromatography, and gel filtration
Acinetobacter johnsonii
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.48
-
crude extract of recombinant Escherichia coli strain JM109, pH 8.0, 37°C
Acinetobacter johnsonii
24.9
-
purified recombinant PAP tetramer, pH 8.0, 37°C
Acinetobacter johnsonii
54.9
-
purified recombinant PAP dimer, pH 8.0, 37°C
Acinetobacter johnsonii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
AMP + [phosphate]n
-
722513
Acinetobacter johnsonii
ADP + [phosphate]n-1
-
-
-
?
AMP + [phosphate]n
best substrate
722513
Acinetobacter johnsonii
ADP + [phosphate]n-1
-
-
-
?
AMP + [phosphate]n
-
722513
Acinetobacter johnsonii 210A
ADP + [phosphate]n-1
-
-
-
?
AMP + [phosphate]n
best substrate
722513
Acinetobacter johnsonii 210A
ADP + [phosphate]n-1
-
-
-
?
CMP + [phosphate]n
0.09% of the activity with AMP
722513
Acinetobacter johnsonii
CDP + [phosphate]n-1
-
-
-
?
CMP + [phosphate]n
0.09% of the activity with AMP
722513
Acinetobacter johnsonii 210A
CDP + [phosphate]n-1
-
-
-
?
dAMP + [phosphate]n
18% of the activity with AMP
722513
Acinetobacter johnsonii
dADP + [phosphate]n-1
-
-
-
?
dCMP + [phosphate]n
0.008% of the activity with AMP
722513
Acinetobacter johnsonii
dCDP + [phosphate]n-1
-
-
-
?
dGMP + [phosphate]n
2.6% of the activity with AMP
722513
Acinetobacter johnsonii
dGDP + [phosphate]n-1
-
-
-
?
GMP + [phosphate]n
10% of the activity with AMP
722513
Acinetobacter johnsonii
GDP + [phosphate]n-1
-
-
-
?
GMP + [phosphate]n
10% of the activity with AMP
722513
Acinetobacter johnsonii 210A
GDP + [phosphate]n-1
-
-
-
?
IMP + [phosphate]n
2.2% of the activity with AMP
722513
Acinetobacter johnsonii
IDP + [phosphate]n-1
-
-
-
?
additional information
PAP acts as a poly(P)-dependent NMP kinase, activity for AMP by PAP is about 10times greater than that for GMP and 770 and about 1100times greater than that for UMP and CMP. ATP production by the coupled reactions of recombinant PAP and purified Escherichia coli poly(P) kinases from AMP. The purified recombinant PAP enzyme has not only strong PAP activity but also shows poly(P)-dependent nucleoside monophosphate kinase activity, by which it converts ribonucleoside monophosphates and deoxyribonucleoside monophosphates into ribonucleoside diphosphates and deoxyribonucleoside diphosphates, respectively
722513
Acinetobacter johnsonii
?
-
-
-
-
additional information
PAP acts as a poly(P)-dependent NMP kinase, activity for AMP by PAP is about 10times greater than that for GMP and 770 and about 1100times greater than that for UMP and CMP. ATP production by the coupled reactions of recombinant PAP and purified Escherichia coli poly(P) kinases from AMP. The purified recombinant PAP enzyme has not only strong PAP activity but also shows poly(P)-dependent nucleoside monophosphate kinase activity, by which it converts ribonucleoside monophosphates and deoxyribonucleoside monophosphates into ribonucleoside diphosphates and deoxyribonucleoside diphosphates, respectively
722513
Acinetobacter johnsonii 210A
?
-
-
-
-
TMP + [phosphate]n
0.012% of the activity with AMP
722513
Acinetobacter johnsonii
TDP + [phosphate]n-1
-
-
-
?
UMP + [phosphate]n
0.13% of the activity with AMP
722513
Acinetobacter johnsonii
UDP + [phosphate]n-1
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 55800, recombinant pPAP2, SDS-PAGE
Acinetobacter johnsonii
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
50
-
recombinant enzyme
Acinetobacter johnsonii
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
30
50
the level of activity at 50°C is 3.2fold and 1.8fold higher than that at 30°C and 37°C, respectively
Acinetobacter johnsonii
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
45
-
purified recombinant PAP, 10 min, 40% activity remaining without polyphosphate, 85% activity remaining in presence of 10 mM polyphosphate
Acinetobacter johnsonii
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
35
-
GMP
recombinant PAP, pH 8.0, 37°C
Acinetobacter johnsonii
151.7
-
AMP
recombinant PAP, pH 8.0, 37°C, in presence of 50 mM (NH4)2SO4
Acinetobacter johnsonii
166.7
-
AMP
recombinant PAP, pH 8.0, 37°C
Acinetobacter johnsonii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
9
recombinant enzyme
Acinetobacter johnsonii
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
7
11
purified recombinant enzyme, stable at
Acinetobacter johnsonii
General Information
General Information
Commentary
Organism
additional information
PAP contains two putative phosphate-binding motifs, P-loops. The similarity between PAP and the PPK2 homologues indicates that there is a common mechanism by which these enzymes use poly(P) for phosphorylation of nucleosides. The C-terminal region of PAP, including one P-loop (amino acids 286 to 292), is thought to be essential for poly(P)-dependent nucleotide phosphorylation. An additional P-loop in the N-terminal region (amino acids 45 to 51) of PAP may play a crucial role in binding with nucleoside monophosphate
Acinetobacter johnsonii
General Information (protein specific)
General Information
Commentary
Organism
additional information
PAP contains two putative phosphate-binding motifs, P-loops. The similarity between PAP and the PPK2 homologues indicates that there is a common mechanism by which these enzymes use poly(P) for phosphorylation of nucleosides. The C-terminal region of PAP, including one P-loop (amino acids 286 to 292), is thought to be essential for poly(P)-dependent nucleotide phosphorylation. An additional P-loop in the N-terminal region (amino acids 45 to 51) of PAP may play a crucial role in binding with nucleoside monophosphate
Acinetobacter johnsonii
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
7.83
-
GMP
recombinant PAP, pH 8.0, 37°C
Acinetobacter johnsonii
333.3
-
AMP
recombinant PAP, pH 8.0, 37°C, in presence of 50 mM (NH4)2SO4
Acinetobacter johnsonii
616.7
-
AMP
recombinant PAP, pH 8.0, 37°C
Acinetobacter johnsonii
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
7.83
-
GMP
recombinant PAP, pH 8.0, 37°C
Acinetobacter johnsonii
333.3
-
AMP
recombinant PAP, pH 8.0, 37°C, in presence of 50 mM (NH4)2SO4
Acinetobacter johnsonii
616.7
-
AMP
recombinant PAP, pH 8.0, 37°C
Acinetobacter johnsonii
Other publictions for EC 2.7.4.B2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
737499
Motomura
A new subfamily of polyphospha ...
Meiothermus ruber, Meiothermus ruber NBRC 106122
Appl. Environ. Microbiol.
80
2602-2608
2014
1
-
1
-
2
-
-
-
-
2
2
6
-
2
-
-
1
-
-
-
6
-
11
1
1
1
1
-
1
-
-
-
-
-
-
1
-
1
-
-
2
-
-
-
-
-
-
2
2
6
-
-
-
1
-
-
6
-
11
1
1
1
1
-
1
-
-
-
-
3
3
-
-
-
738411
Jyoti Roy
-
Polyphosphate kinase from Leis ...
Leishmania donovani, Leishmania donovani MHOM/IN/83/AG83
Int. J. Drug Develop. Res.
6
159-164
2014
-
-
-
-
-
-
-
-
-
1
-
3
-
2
-
-
-
-
-
1
3
-
5
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
1
3
-
5
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
720887
Zhang
Inorganic polyphosphate in the ...
Myxococcus xanthus
Proc. Natl. Acad. Sci. USA
102
13416-13420
2005
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
722513
Shiba
Polyphosphate:AMP phosphotrans ...
Acinetobacter johnsonii, Acinetobacter johnsonii 210A
J. Bacteriol.
187
1859-1865
2005
-
-
1
-
-
-
1
3
-
2
1
2
-
6
-
-
1
-
-
-
3
-
16
1
1
1
1
3
1
-
1
-
-
-
-
-
-
1
-
-
-
-
-
1
-
3
-
2
1
2
-
-
-
1
-
-
3
-
16
1
1
1
1
3
1
-
1
-
-
1
1
-
3
3
720949
Shi
Inorganic polyphosphate in Bac ...
Bacillus cereus
Proc. Natl. Acad. Sci. USA
49
17061-17065
2004
-
-
-
-
-
-
-
-
-
-
-
1
-
6
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
722511
Itoh
Polyphosphate synthetic activi ...
Acinetobacter johnsonii, Acinetobacter johnsonii 210A
J. Bacteriol.
186
5178-5181
2004
-
-
-
-
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7
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In vitro ATP regeneration from ...
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Ishige
Inorganic polyphosphate kinase ...
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Purification and properties of ...
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Polyphosphate-dependent enzyme ...
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Polyphosphate-degrading enzyme ...
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