BRENDA - Enzyme Database
show all sequences of 3.5.1.48
Other publictions for EC 3.5.1.48
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
Synonyms
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)
752780
Shinsky
Polyamine deacetylase structu ...
Danio rerio, Homo sapiens
Biochemistry
57
3105-3114
2018
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2
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2
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2
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2
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6
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2
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4
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6
6
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754843
Hai
Histone deacetylase 10 struct ...
Danio rerio, Homo sapiens
Nat. Commun.
8
15368
2017
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2
1
5
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2
37
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2
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2
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8
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2
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27
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6
2
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37
2
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2
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2
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1
5
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2
2
37
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2
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2
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2
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27
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2
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37
2
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2
2
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35
35
733494
Decroos
Synthesis and evaluation of N8 ...
Mycoplana ramosa
Bioorg. Med. Chem.
21
4530-4540
2013
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1
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1
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35
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1
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5
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7
1
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1
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1
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1
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35
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7
1
1
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1
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172047
Wang
Effect of N8-acetylspermidine ...
Mus musculus
Biochem. Pharmacol.
57
1095-1103
1999
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2
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1
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1
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172048
Menezes
Differentiation of PC 12 cells ...
Rattus sp.
Proc. West. Pharmacol. Soc.
36
21-24
1993
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1
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172049
Huang
Inhibition of N8-acetylspermid ...
Rattus sp.
J. Med. Chem.
35
2414-2418
1992
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10
1
1
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3
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9
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9
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172046
Suzuke
-
Acetylspermidine deacetylase a ...
Homo sapiens
Med. Sci. Res.
15
675-676
1987
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12
1
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1
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8
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3
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1
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12
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1
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8
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3
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1
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172050
Marchant
N1-Acetylspermidine is not a s ...
Rattus sp.
Biochim. Biophys. Acta
881
297-299
1986
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2
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1
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1
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172051
Manneh
-
Inhibitor studies on the chara ...
Rattus sp.
Proc. West. Pharmacol. Soc.
28
255-258
1985
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7
1
1
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6
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7
6
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1
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1
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1
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172052
Libby
Acetylspermidine deacetylase ( ...
Rattus sp.
Methods Enzymol.
94
329-331
1983
1
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3
2
1
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1
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1
1
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3
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4
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1
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1
1
1
3
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1
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172053
Santacroce
Inhibition of acetylspermidine ...
Rattus sp.
Proc. West. Pharmacol. Soc.
25
113-118
1982
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7
1
1
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1
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1
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6
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9
6
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1
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172054
Blankenship
Deacetylation of N8-acetylsper ...
Rattus sp.
Arch. Biochem. Biophys.
189
20-27
1978
1
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1
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8
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8
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1
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1
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172055
Libby
Properties of an acetylspermid ...
Rattus sp.
Arch. Biochem. Biophys.
188
360-363
1978
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3
1
1
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3
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1
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1
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1
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1
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3
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1
1
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1
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1
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3
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1
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