BRENDA - Enzyme Database show
show all sequences of 3.5.3.11

A new subfamily of agmatinases present in methanogenic Archaea is Fe(II) dependent

Miller, D.; Xu, H.; White, R.H.; Biochemistry 51, 3067-3078 (2012)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
dithiothreitol
the enzyme requires the presence of dithiothreitol for maximum activity
Methanocaldococcus jannaschii
Cloned(Commentary)
Commentary
Organism
overexpression in Escherichia coli
Methanocaldococcus jannaschii
Engineering
Amino acid exchange
Commentary
Organism
C136A
mutant has 90% of the activity compared to wild type in the presence of Fe(II). As the wild-type enzyme the mutant enzyme requires dithiothreitol for activity
Methanocaldococcus jannaschii
C151S
mutant has 6% of the activity compared to wild type in the presence of Fe(II). When dithiothreitol is present in the reaction the mutant shows 24% of the wild type activity
Methanocaldococcus jannaschii
C229A
mutant has 92% of the activity compared to wild type in the presence of Fe(II)
Methanocaldococcus jannaschii
C71S
mutant has 4% of the activity compared to wild type in the presence of Fe(II). When dithiothreitol is present in the reaction the mutant shows 24% of the wild type activity
Methanocaldococcus jannaschii
Inhibitors
Inhibitors
Commentary
Organism
Structure
iodoacetic acid
the enzyme is rendered inactive when the purified enzyme is incubated with dithiothreitol followed by excess iodoacetic acid
Methanocaldococcus jannaschii
L-arginine
44% inhibition at at 16.7 mM
Methanocaldococcus jannaschii
N-ethylmaleinimide
the enzyme is rendered inactive when the purified enzyme is incubated with dithiothreitol followed by excess N-ethylmaleimide
Methanocaldococcus jannaschii
putrescine
43% inhibition at 8.3 mM, 60% inhibition at 16.7 mM
Methanocaldococcus jannaschii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.4
-
agmatine
pH 7.5, 70°C, wild-type enzyme
Methanocaldococcus jannaschii
5.8
-
agmatine
pH 7.5, 70°C, mutant enzyme C229A
Methanocaldococcus jannaschii
6.2
-
agmatine
pH 7.5, 70°C, mutant enzyme C151S
Methanocaldococcus jannaschii
9.2
-
agmatine
pH 7.5, 70°C, mutant enzyme C136A
Methanocaldococcus jannaschii
11
-
agmatine
pH 7.5, 70°C, mutant enzyme C71S
Methanocaldococcus jannaschii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
Fe(II)-dependent agmatinase. Requires the presence of 4 equivalents of Fe(II) for maximum activity
Methanocaldococcus jannaschii
Mn2+
supports activity at 15% of the activation by Fe2+
Methanocaldococcus jannaschii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
x * 40000, SDS-PAGE
Methanocaldococcus jannaschii
190000
-
gel filtration
Methanocaldococcus jannaschii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanocaldococcus jannaschii
Q57757
-
-
Methanocaldococcus jannaschii DSM 2661
Q57757
-
-
Purification (Commentary)
Commentary
Organism
wild-type and mutant enzymes
Methanocaldococcus jannaschii
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.45
-
pH 7.5, 70°C
Methanocaldococcus jannaschii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
agmatine + H2O
-
726980
Methanocaldococcus jannaschii
putrescine + urea
-
-
-
?
agmatine + H2O
-
726980
Methanocaldococcus jannaschii DSM 2661
putrescine + urea
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 40000, SDS-PAGE
Methanocaldococcus jannaschii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
assay at
Methanocaldococcus jannaschii
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0075
-
agmatine
pH 7.5, 70°C, mutant enzyme C71S
Methanocaldococcus jannaschii
0.0095
-
agmatine
pH 7.5, 70°C, mutant enzyme C151S
Methanocaldococcus jannaschii
0.023
-
agmatine
pH 7.5, 70°C, mutant enzyme C136A
Methanocaldococcus jannaschii
0.032
-
agmatine
pH 7.5, 70°C, wild-type enzyme
Methanocaldococcus jannaschii
0.041
-
agmatine
pH 7.5, 70°C, mutant enzyme C229A
Methanocaldococcus jannaschii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Methanocaldococcus jannaschii
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6.5
10
no activity is detected at pH 6.5 and the measured activity steadily increases to pH 10.0. Higher pH values are tested but the observation of activity is dependent on the buffer used and are not reported here. Agmatine shows no hydrolysis in the pH 10 and 11 buffers and assay conditions used
Methanocaldococcus jannaschii
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
dithiothreitol
the enzyme requires the presence of dithiothreitol for maximum activity
Methanocaldococcus jannaschii
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpression in Escherichia coli
Methanocaldococcus jannaschii
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C136A
mutant has 90% of the activity compared to wild type in the presence of Fe(II). As the wild-type enzyme the mutant enzyme requires dithiothreitol for activity
Methanocaldococcus jannaschii
C151S
mutant has 6% of the activity compared to wild type in the presence of Fe(II). When dithiothreitol is present in the reaction the mutant shows 24% of the wild type activity
Methanocaldococcus jannaschii
C229A
mutant has 92% of the activity compared to wild type in the presence of Fe(II)
Methanocaldococcus jannaschii
C71S
mutant has 4% of the activity compared to wild type in the presence of Fe(II). When dithiothreitol is present in the reaction the mutant shows 24% of the wild type activity
Methanocaldococcus jannaschii
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
iodoacetic acid
the enzyme is rendered inactive when the purified enzyme is incubated with dithiothreitol followed by excess iodoacetic acid
Methanocaldococcus jannaschii
L-arginine
44% inhibition at at 16.7 mM
Methanocaldococcus jannaschii
N-ethylmaleinimide
the enzyme is rendered inactive when the purified enzyme is incubated with dithiothreitol followed by excess N-ethylmaleimide
Methanocaldococcus jannaschii
putrescine
43% inhibition at 8.3 mM, 60% inhibition at 16.7 mM
Methanocaldococcus jannaschii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.4
-
agmatine
pH 7.5, 70°C, wild-type enzyme
Methanocaldococcus jannaschii
5.8
-
agmatine
pH 7.5, 70°C, mutant enzyme C229A
Methanocaldococcus jannaschii
6.2
-
agmatine
pH 7.5, 70°C, mutant enzyme C151S
Methanocaldococcus jannaschii
9.2
-
agmatine
pH 7.5, 70°C, mutant enzyme C136A
Methanocaldococcus jannaschii
11
-
agmatine
pH 7.5, 70°C, mutant enzyme C71S
Methanocaldococcus jannaschii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
Fe(II)-dependent agmatinase. Requires the presence of 4 equivalents of Fe(II) for maximum activity
Methanocaldococcus jannaschii
Mn2+
supports activity at 15% of the activation by Fe2+
Methanocaldococcus jannaschii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
x * 40000, SDS-PAGE
Methanocaldococcus jannaschii
190000
-
gel filtration
Methanocaldococcus jannaschii
Purification (Commentary) (protein specific)
Commentary
Organism
wild-type and mutant enzymes
Methanocaldococcus jannaschii
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.45
-
pH 7.5, 70°C
Methanocaldococcus jannaschii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
agmatine + H2O
-
726980
Methanocaldococcus jannaschii
putrescine + urea
-
-
-
?
agmatine + H2O
-
726980
Methanocaldococcus jannaschii DSM 2661
putrescine + urea
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 40000, SDS-PAGE
Methanocaldococcus jannaschii
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
assay at
Methanocaldococcus jannaschii
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0075
-
agmatine
pH 7.5, 70°C, mutant enzyme C71S
Methanocaldococcus jannaschii
0.0095
-
agmatine
pH 7.5, 70°C, mutant enzyme C151S
Methanocaldococcus jannaschii
0.023
-
agmatine
pH 7.5, 70°C, mutant enzyme C136A
Methanocaldococcus jannaschii
0.032
-
agmatine
pH 7.5, 70°C, wild-type enzyme
Methanocaldococcus jannaschii
0.041
-
agmatine
pH 7.5, 70°C, mutant enzyme C229A
Methanocaldococcus jannaschii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Methanocaldococcus jannaschii
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6.5
10
no activity is detected at pH 6.5 and the measured activity steadily increases to pH 10.0. Higher pH values are tested but the observation of activity is dependent on the buffer used and are not reported here. Agmatine shows no hydrolysis in the pH 10 and 11 buffers and assay conditions used
Methanocaldococcus jannaschii
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00069
-
agmatine
pH 7.5, 70°C, mutant enzyme C71S
Methanocaldococcus jannaschii
0.0015
-
agmatine
pH 7.5, 70°C, mutant enzyme C151S
Methanocaldococcus jannaschii
0.0025
-
agmatine
pH 7.5, 70°C, mutant enzyme C136A
Methanocaldococcus jannaschii
0.0077
-
agmatine
pH 7.5, 70°C, mutant enzyme C229A
Methanocaldococcus jannaschii
0.013
-
agmatine
pH 7.5, 70°C, wild-type enzyme
Methanocaldococcus jannaschii
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00069
-
agmatine
pH 7.5, 70°C, mutant enzyme C71S
Methanocaldococcus jannaschii
0.0015
-
agmatine
pH 7.5, 70°C, mutant enzyme C151S
Methanocaldococcus jannaschii
0.0025
-
agmatine
pH 7.5, 70°C, mutant enzyme C136A
Methanocaldococcus jannaschii
0.0077
-
agmatine
pH 7.5, 70°C, mutant enzyme C229A
Methanocaldococcus jannaschii
0.013
-
agmatine
pH 7.5, 70°C, wild-type enzyme
Methanocaldococcus jannaschii
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
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727122
Wang
Arginine decarboxylase and agm ...
Ovis aries
Biol. Reprod.
90
84
2014
-
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-
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1
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1
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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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2
1
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718561
Madai
Synaptic localisation of agmat ...
Rattus norvegicus
Amino Acids
43
1399-1403
2012
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-
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-
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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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726980
Miller
A new subfamily of agmatinases ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
Biochemistry
51
3067-3078
2012
1
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1
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4
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4
5
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2
2
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4
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1
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1
1
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5
1
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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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5
5
710833
Bernstein
The agmatine-degrading enzyme ...
Homo sapiens, Rattus norvegicus
Amino Acids
40
453-465
2010
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712119
Mella
Expression and localization of ...
Rattus norvegicus
Histochem. Cell Biol.
134
137-144
2010
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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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686646
Alarcon
Mutational analysis of substra ...
Homo sapiens
FEBS J.
273
5625-5631
2006
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663534
Kim
Expression, crystallization an ...
Homo sapiens
Acta Crystallogr. Sect. F
61
889-891
2005
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
664200
Goda
The first archaeal agmatinase ...
Pyrococcus horikoshii
Biochim. Biophys. Acta
1748
110-115
2005
-
-
1
-
-
-
1
1
-
5
2
-
3
6
-
-
1
-
-
-
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2
1
1
-
2
-
1
1
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1
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1
1
1
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5
2
-
3
-
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1
-
-
-
-
2
1
1
-
2
-
1
1
-
-
-
-
-
-
-
-
649495
Carvajal
Kinetic studies and site-direc ...
Escherichia coli
Arch. Biochem. Biophys.
430
185-190
2004
-
-
-
-
1
-
2
2
-
-
-
-
-
2
-
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
663483
Lee
Crystallization and preliminar ...
Deinococcus radiodurans
Acta Crystallogr. Sect. D
60
1890-1892
2004
-
-
1
1
-
-
-
-
-
-
-
-
-
5
-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
665228
Dallmann
Human agmatinase is diminished ...
Homo sapiens
Int. J. Cancer
108
342-347
2004
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
6
-
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6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
665590
Ahn
Crystal structure of agmatinas ...
Deinococcus radiodurans
J. Biol. Chem.
279
50505-50513
2004
-
-
-
1
-
-
1
-
-
-
-
-
-
4
-
-
-
-
-
-
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1
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
665940
Salas
Studies on the interaction of ...
Escherichia coli
J. Inorg. Biochem.
98
1032-1036
2004
-
-
-
-
2
-
1
-
-
1
-
-
-
3
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
651139
Salas
Insights into the reaction mec ...
Escherichia coli
Eur. J. Biochem.
269
5522-5526
2002
-
-
-
-
2
-
-
-
-
1
-
-
-
2
-
-
-
-
-
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246676
Carvajal
Evidence that histidine-163 is ...
Escherichia coli
Biochem. Biophys. Res. Commun.
264
196-200
1999
-
-
-
-
-
-
2
-
-
1
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
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-
-
-
-
2
-
-
-
1
-
1
-
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-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246685
Carvajal
Manganese is essential for cat ...
Escherichia coli
Biochem. Biophys. Res. Commun.
258
808-811
1999
-
-
-
-
-
-
4
-
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246682
Sastre
Agmatinase activity in rat bra ...
Rattus norvegicus
J. Neurochem.
67
1761-1765
1995
-
-
-
-
-
-
-
1
1
-
-
1
-
2
-
-
-
-
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
246683
Szumanski
Influence of cyclic AMP, agmat ...
Escherichia coli
J. Bacteriol.
174
758-764
1992
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
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-
-
-
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1
-
-
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-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246684
Szumanski
Analysis and sequence of the s ...
Escherichia coli
J. Bacteriol.
172
538-547
1990
-
-
-
-
-
-
-
-
-
-
2
-
-
5
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246681
Satishchandran
Purification and properties of ...
Escherichia coli
J. Bacteriol.
165
843-848
1986
-
-
-
-
-
-
4
1
-
-
3
-
-
2
-
-
1
-
-
-
-
1
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
1
-
-
3
-
-
-
-
1
-
-
-
1
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
246680
Shaibe
Metabolic pathway for the util ...
Escherichia coli
J. Bacteriol.
163
933-937
1985
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246678
Legaz
Endogenous inactivators of arg ...
Evernia prunastri
Plant Physiol.
71
300-302
1983
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
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-
-
-
-
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-
-
-
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-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246679
White Tabor
Cloning of the Escherichia col ...
Escherichia coli
Methods Enzymol.
94
117-121
1983
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246677
Vicente
-
Purification and properties of ...
Evernia prunastri
Physiol. Plant.
55
335-339
1982
3
-
-
-
-
-
3
1
-
-
1
1
-
1
-
-
1
-
-
1
-
-
1
-
1
-
2
-
1
-
-
-
-
-
-
3
-
-
-
-
-
-
-
3
-
1
-
-
1
1
-
-
-
1
-
1
-
-
1
-
1
-
2
-
1
-
-
-
-
-
-
-
-
-
246674
Friedrich
Enzymes of agmatine degradatio ...
Klebsiella aerogenes
J. Bacteriol.
137
1127-1133
1979
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
246675
Boldt
-
Metabolism of agmatine in frui ...
Lentinus tigrinus
Phytochemistry
10
731-738
1971
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
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1
-
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