BRENDA - Enzyme Database show
show all sequences of 3.5.3.11

Expression, crystallization and preliminary X-ray crystallographic analysis of human agmatinase

Kim, K.H.; Ahn, H.J.; Kim, D.J.; Lee, H.H.; Ha, J.Y.; Kim, H.K.; Yoon, H.J.; Suh, S.W.; Acta Crystallogr. Sect. F 61, 889-891 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
residues Ala36-Val352 overexpressed as a fusion with both N- and C-terminal purification tags in Escherichia coli
Homo sapiens
Crystallization (Commentary)
Crystallization
Organism
hanging-drop vapour-diffusion method, agmatinase (residues Ala36-Val352) overexpressed as a fusion with both N- and C-terminal purification tags in Escherichia coli and crystallized in the presence of Mn2+ and 1,6-diaminohexane at 297 K using polyethylene glycol 4000 as a precipitant. X-ray diffraction data are collected at 100 K to 2.49 A from a flash-frozen crystal. The crystals are tetragonal, belonging to space group P4(2), with unit-cell parameters a = b = 114.54 A, c =125.65A, alpha = beta = gamma = 90°. Three monomers are likely to be present in the asymmetric unit, giving a crystal volume per protein weight of 3.66A
Homo sapiens
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Purification (Commentary)
Commentary
Organism
-
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
residues Ala36-Val352 overexpressed as a fusion with both N- and C-terminal purification tags in Escherichia coli
Homo sapiens
Crystallization (Commentary) (protein specific)
Crystallization
Organism
hanging-drop vapour-diffusion method, agmatinase (residues Ala36-Val352) overexpressed as a fusion with both N- and C-terminal purification tags in Escherichia coli and crystallized in the presence of Mn2+ and 1,6-diaminohexane at 297 K using polyethylene glycol 4000 as a precipitant. X-ray diffraction data are collected at 100 K to 2.49 A from a flash-frozen crystal. The crystals are tetragonal, belonging to space group P4(2), with unit-cell parameters a = b = 114.54 A, c =125.65A, alpha = beta = gamma = 90°. Three monomers are likely to be present in the asymmetric unit, giving a crystal volume per protein weight of 3.66A
Homo sapiens
Purification (Commentary) (protein specific)
Commentary
Organism
-
Homo sapiens
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 ...
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Archaea
2016
7316725
2016
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727122
Wang
Arginine decarboxylase and agm ...
Ovis aries
Biol. Reprod.
90
84
2014
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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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Madai
Synaptic localisation of agmat ...
Rattus norvegicus
Amino Acids
43
1399-1403
2012
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720553
Bernstein
Agmatinase, an inactivator of ...
Homo sapiens
Neuropharmacology
62
237-246
2012
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726980
Miller
A new subfamily of agmatinases ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
Biochemistry
51
3067-3078
2012
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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
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5549-5552
2009
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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
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649495
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Kinetic studies and site-direc ...
Escherichia coli
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663483
Lee
Crystallization and preliminar ...
Deinococcus radiodurans
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1890-1892
2004
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665228
Dallmann
Human agmatinase is diminished ...
Homo sapiens
Int. J. Cancer
108
342-347
2004
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665590
Ahn
Crystal structure of agmatinas ...
Deinococcus radiodurans
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279
50505-50513
2004
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665940
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Studies on the interaction of ...
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651139
Salas
Insights into the reaction mec ...
Escherichia coli
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5522-5526
2002
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Evidence that histidine-163 is ...
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246685
Carvajal
Manganese is essential for cat ...
Escherichia coli
Biochem. Biophys. Res. Commun.
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808-811
1999
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246682
Sastre
Agmatinase activity in rat bra ...
Rattus norvegicus
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67
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1995
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246683
Szumanski
Influence of cyclic AMP, agmat ...
Escherichia coli
J. Bacteriol.
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758-764
1992
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246684
Szumanski
Analysis and sequence of the s ...
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1990
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246681
Satishchandran
Purification and properties of ...
Escherichia coli
J. Bacteriol.
165
843-848
1986
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4
1
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3
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1
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1
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246680
Shaibe
Metabolic pathway for the util ...
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