BRENDA - Enzyme Database show
show all sequences of 3.5.3.11

The first archaeal agmatinase from anaerobic hyperthermophilic archaeon Pyrococcus horikoshii: cloning, expression, and characterization

Goda, S.; Sakuraba, H.; Kawarabayasi, Y.; Ohshima, T.; Biochim. Biophys. Acta 1748, 110-115 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli. Mainly obtained as inactive inclusion body in Escherichia coli
Pyrococcus horikoshii
Inhibitors
Inhibitors
Commentary
Organism
Structure
putrescine
-
Pyrococcus horikoshii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.53
-
agmatine
50C, pH 11.3
Pyrococcus horikoshii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
Pyrococcus horikoshii
Co2+
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
Pyrococcus horikoshii
Mg2+
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
Pyrococcus horikoshii
Mn2+
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
Pyrococcus horikoshii
Zn2+
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
Pyrococcus horikoshii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
31000
-
4 * 31000, SDS-PAGE
Pyrococcus horikoshii
145000
-
gel filtration
Pyrococcus horikoshii
Organic Solvent Stability
Organic Solvent
Commentary
Organism
dimethyl sulfoxide
10%, no loss of activity at 50C
Pyrococcus horikoshii
Ethanol
10%, no loss of activity at 50C
Pyrococcus horikoshii
Methanol
10%, no loss of activity at 50C
Pyrococcus horikoshii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pyrococcus horikoshii
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant
Pyrococcus horikoshii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
agmatine + H2O
-
664200
Pyrococcus horikoshii
putrescine + urea
-
-
-
?
additional information
no activity with arginine
664200
Pyrococcus horikoshii
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
tetramer
4 * 31000, SDS-PAGE
Pyrococcus horikoshii
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
100
-
-
Pyrococcus horikoshii
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
80
-
10 min, stable
Pyrococcus horikoshii
90
-
10 min, 53% loss of activity
Pyrococcus horikoshii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
11
-
-
Pyrococcus horikoshii
pH Range
pH Minimum
pH Maximum
Commentary
Organism
9.5
12.5
pH 9.5: about 50% of maximal activity, pH 12.5: about 85% of maximal activity
Pyrococcus horikoshii
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.8
-
putrescine
50C, pH 11.3
Pyrococcus horikoshii
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli. Mainly obtained as inactive inclusion body in Escherichia coli
Pyrococcus horikoshii
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
putrescine
-
Pyrococcus horikoshii
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.8
-
putrescine
50C, pH 11.3
Pyrococcus horikoshii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.53
-
agmatine
50C, pH 11.3
Pyrococcus horikoshii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
Pyrococcus horikoshii
Co2+
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
Pyrococcus horikoshii
Mg2+
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
Pyrococcus horikoshii
Mn2+
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
Pyrococcus horikoshii
Zn2+
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
Pyrococcus horikoshii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
31000
-
4 * 31000, SDS-PAGE
Pyrococcus horikoshii
145000
-
gel filtration
Pyrococcus horikoshii
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
dimethyl sulfoxide
10%, no loss of activity at 50C
Pyrococcus horikoshii
Ethanol
10%, no loss of activity at 50C
Pyrococcus horikoshii
Methanol
10%, no loss of activity at 50C
Pyrococcus horikoshii
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant
Pyrococcus horikoshii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
agmatine + H2O
-
664200
Pyrococcus horikoshii
putrescine + urea
-
-
-
?
additional information
no activity with arginine
664200
Pyrococcus horikoshii
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 31000, SDS-PAGE
Pyrococcus horikoshii
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
100
-
-
Pyrococcus horikoshii
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
80
-
10 min, stable
Pyrococcus horikoshii
90
-
10 min, 53% loss of activity
Pyrococcus horikoshii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
11
-
-
Pyrococcus horikoshii
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
9.5
12.5
pH 9.5: about 50% of maximal activity, pH 12.5: about 85% of maximal activity
Pyrococcus horikoshii
Other publictions for EC 3.5.3.11
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)
737576
Prunetti
Deciphering the translation in ...
Haloferax volcanii, Haloferax volcanii DSM 3757
Archaea
2016
7316725
2016
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1
1
-
-
-
727122
Wang
Arginine decarboxylase and agm ...
Ovis aries
Biol. Reprod.
90
84
2014
-
-
-
-
-
-
-
-
-
-
-
1
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2
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2
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1
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1
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2
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1
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-
-
-
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-
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-
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1
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-
1
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-
734651
Burnat
Inactivation of agmatinase exp ...
Anabaena sp., Anabaena sp. PCC 7120
MicrobiologyOpen
3
777-792
2014
-
-
-
-
-
-
-
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1
2
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5
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1
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1
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4
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2
1
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-
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718561
Madai
Synaptic localisation of agmat ...
Rattus norvegicus
Amino Acids
43
1399-1403
2012
-
-
-
-
-
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1
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3
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720553
Bernstein
Agmatinase, an inactivator of ...
Homo sapiens
Neuropharmacology
62
237-246
2012
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1
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1
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1
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-
726980
Miller
A new subfamily of agmatinases ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
Biochemistry
51
3067-3078
2012
1
-
1
-
4
-
4
5
-
2
2
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4
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1
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1
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2
1
1
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5
1
1
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1
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1
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4
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4
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5
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2
2
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1
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1
-
2
1
1
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-
5
1
1
-
-
-
-
-
-
5
5
710833
Bernstein
The agmatine-degrading enzyme ...
Homo sapiens, Rattus norvegicus
Amino Acids
40
453-465
2010
-
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2
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4
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2
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712119
Mella
Expression and localization of ...
Rattus norvegicus
Histochem. Cell Biol.
134
137-144
2010
-
-
-
-
-
-
-
-
-
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1
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5
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5
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1
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1
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1
1
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712287
Chattopadhyay
Polyamines are not required fo ...
Escherichia coli
J. Bacteriol.
191
5549-5552
2009
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1
1
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695474
Haenisch
Regulatory mechanisms underlyi ...
Homo sapiens
Am. J. Physiol. Gastrointest. Liver Physiol.
295
G1104-G1110
2008
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4
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686646
Alarcon
Mutational analysis of substra ...
Homo sapiens
FEBS J.
273
5625-5631
2006
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1
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1
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663534
Kim
Expression, crystallization an ...
Homo sapiens
Acta Crystallogr. Sect. F
61
889-891
2005
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1
1
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3
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664200
Goda
The first archaeal agmatinase ...
Pyrococcus horikoshii
Biochim. Biophys. Acta
1748
110-115
2005
-
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1
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1
1
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5
2
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3
6
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1
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2
1
1
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2
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1
1
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1
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1
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1
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1
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649495
Carvajal
Kinetic studies and site-direc ...
Escherichia coli
Arch. Biochem. Biophys.
430
185-190
2004
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2
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663483
Lee
Crystallization and preliminar ...
Deinococcus radiodurans
Acta Crystallogr. Sect. D
60
1890-1892
2004
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1
1
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5
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665228
Dallmann
Human agmatinase is diminished ...
Homo sapiens
Int. J. Cancer
108
342-347
2004
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6
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6
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665590
Ahn
Crystal structure of agmatinas ...
Deinococcus radiodurans
J. Biol. Chem.
279
50505-50513
2004
-
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1
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1
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665940
Salas
Studies on the interaction of ...
Escherichia coli
J. Inorg. Biochem.
98
1032-1036
2004
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2
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1
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1
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3
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