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Information on EC 3.5.3.11 - agmatinase
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3.5.3.11 agmatinaseSpecify your search results
Word Map
- 3.5.3.11
- putrescine
- polyamine
- ornithine
-
imidazoline
- speb
- arcaine
- proclavaminate
-
idazoxan
- slc7a1
-
efaroxan
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
agmatinase, agmatine ureohydrolase, agmat, agm-1, agmatinase-like protein, agmatine amidinohydrolase, alr2310, proclavaminic acid amidino hydrolase, mj0309, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AGMAT
agmatinase
agmatine ureohydrolase
Alr2310
AUH
-
-
-
-
HVO_2299
MJ0309
Proclavaminic acid amidino hydrolase
-
-
-
-
SpeB
agmatine ureohydrolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
agmatine + H2O = putrescine + urea
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amidine hydrolysis
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
agmatine amidinohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
37289-16-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
agmatine + H2O
putrescine + urea
-
the N130D mutant of arginase type I is able to cleave not only arginine but also agmatine (1-amino-4-guanidinobutane)
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
Fe2+
Fe(II)-dependent agmatinase. Requires the presence of 4 equivalents of Fe(II) for maximum activity
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
Mn2+
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
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
Mn2+
-
the enzyme contains one Mn2+ per subunit after purification. Adding extra Mn2+ leads to a further increase in activity. Incubation in the presence of Mn2+ at 60 °C for up to 20 min results in a significant activation in all ALP variants. The activation of the H206A and H435A mutants is comparable to wild-type enzyme (about 4fold increase), while for the remaining mutants (H65A, H127A, H394A) the increase is less significant. His206 is likely to interact with a Mn2+ bound to a high affinity site. His65 and possibly His435 are important for binding of a secondMn2+ to a lower affinity site
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,6-diaminohexane
-
inhibition arises from the displacement of the metal-bridging water
iodoacetic acid
the enzyme is rendered inactive when the purified enzyme is incubated with dithiothreitol followed by excess iodoacetic acid
N-ethylmaleinimide
the enzyme is rendered inactive when the purified enzyme is incubated with dithiothreitol followed by excess N-ethylmaleimide
EDTA
-
incubation with 50 mM EDTA (pH 7.5) and subsequent dialysis to remove the chelating agent results in the loss of agmatinase activity
putrescine
43% inhibition at 8.3 mM, 60% inhibition at 16.7 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
the enzyme requires the presence of dithiothreitol for maximum activity
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma of Lung
Agmatinase promotes the lung adenocarcinoma tumorigenesis by activating the NO-MAPKs-PI3K/Akt pathway.
Asthma
Functionally Important Role for Arginase 1 in the Airways Hyperresponsiveness of Asthma.
Carcinogenesis
Agmatinase promotes the lung adenocarcinoma tumorigenesis by activating the NO-MAPKs-PI3K/Akt pathway.
Carcinoma, Renal Cell
Human agmatinase is diminished in the clear cell type of renal cell carcinoma.
Hepatitis
Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus.
Hepatitis B
Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus.
Malaria
Structural metal dependency of the arginase from the human malaria parasite Plasmodium falciparum.
Mania
Evaluation of plasma agmatine level and its metabolic pathway in patients with bipolar disorder during manic episode and remission period.
Neoplasms
Agmatinase promotes the lung adenocarcinoma tumorigenesis by activating the NO-MAPKs-PI3K/Akt pathway.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
9.5 - 12.5
-
pH 9.5: about 50% of maximal activity, pH 12.5: about 85% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
agmatinase is localised pre- and postsynaptically, to dendritic spines, spine and non-spine terminals, and dendritic profiles. In dendritic spines, labelling displayed a tendency towards the postsynaptic density
brenda
the enzyme is localized in the apical and subapical region of mature hyphae, localizing at the Spitzenkörper and at the endocytic collar closely resembling the F-actin population
brenda
-
in glial cells and arcuate nucleus neurons of the hypothalamus
brenda
-
agmatinase in normal kidneys is restricted to tubulus epithelial cells, while in tumors activity is low and heterogeneous
brenda
-
agmatinase in normal kidneys is restricted to tubulus epithelial cells, while in tumors activity is low and heterogeneous
brenda
additional information
-
the protein is not detected in brain cortex
brenda
the protein is present at significantly lower levels in heterocysts than in vegetative cells
brenda
-
the protein is present at significantly lower levels in heterocysts than in vegetative cells
-
brenda
-
agmatinase protein is detected in a subset of hippocampal interneurons. The protein is localized to perikarya, neurites and putative nerve endings contacting hippocampal pyramidal neurons and dentate gyrus granule cells. The number and the numerical density of agmatinase-immunopositive cell bodies are strongly elevated in depressive patients
brenda
-
agmatinase is predominantly detected in distinct populations of neurons, especially cortical interneurons. Principal neurons in limbic regions like the habenula and in the cerebellum robustly express agmatinase protein
brenda
-
agmatinase is predominantly detected in distinct populations of neurons, especially cortical interneurons. Principal neurons in limbic regions like the habenula and in the cerebellum robustly express agmatinase protein
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
in vivo knockdown of translation of both ODC1 and AGMAT RNAs resulted in over-expression of genes related to synthesis and transport of polyamines in ovine conceptuses during the peri-implantation period of pregnancy
malfunction
the role in the agmatinase-like protein (AGM-1) in the alternative pathway to produce polyamines is not its main function since only a slight reduction of polyamines concentration is detected in the DELTAagm-1 het strain. The null mutant DELTAagm-1 (homokaryon strain) is unable to grow and the deficiency of agm-1 in the heterokaryon strain provokes a decrease in elongation rate, conidia and biomass production, despite of having constitutive pathway via the ornithine decarboxylase. Mature hyphae of the DELTAagm-1 het strain presented unusual apical branching and a disorganized Spitzenkörper
metabolism
-
the gene agmatine ureohydrolase is involved in polyamine biosynthesis
metabolism
the role in the agmatinase-like protein (AGM-1) in the alternative pathway to produce polyamines is not its main function since only a slight reduction of polyamines concentration is detected in the DELTAagm-1 het strain. In Neurospora crassa AGM-1 has a close association with the F-actin population via its substrate agmatine, playing an essential role during cell development
metabolism
utilization of L-arginine in Stichopus japonicus is conducted by three enzymes: nitric oxide synthase, arginase and agmatinase. Balance of the production of these three enzymes is regulated by multiple transcription factors, such as CREB, NF-kappaB/Rel and STAT5, as well as their substrate L-arginine. Stimulation of pathogen LPS disrupts this balance and subsequently influences the immune response conducted by NO
physiological function
-
agmatinase-like protein plays a role in the regulation of intracellular concentrations of the neurotransmitter/neuromodulator agmatine
physiological function
the gene is essential, its deletion failed even in the presence of 1 mM putrescine
physiological function
-
the gene is essential, its deletion failed even in the presence of 1 mM putrescine
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65700
x * 65700, enzyme fused to a tetra-glycine linker peptide, and the green fluorescent protein, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 65700, enzyme fused to a tetra-glycine linker peptide, and the green fluorescent protein, SDS-PAGE
?
-
x * 65700, enzyme fused to a tetra-glycine linker peptide, and the green fluorescent protein, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of Mn2+ -free, Mn2+ -bound, and Mn2+ -1,6-diaminohexane(inhibitor)-bound forms
-
hangimg-drop vapor-diffusion method, crystallized at 297 K using polyethylene glycol 3000 as a precipitant. X-ray diffraction data are collected to 1.8 A from a crystal grown in the presence of Mn2+ and 1,6-hexanediamine. The crystals are orthorhombic, belonging to the space group P2(1)2(1)2(1), with unit-cell parameters a = 81.77 A, b = 131.44 A, c = 168.85 A, alpha = beta = gamma = 90°. A hexameric molecule is likely to be present in the asymmetric unit
-
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
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H126N
H151N
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
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
C229A
mutant has 92% of the activity compared to wild type in the presence of Fe(II)
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
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
-
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
-
C229A
-
mutant has 92% of the activity compared to wild type in the presence of Fe(II)
-
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
-
H127A
-
Km-value for agmatine is 2.3fold lower than the Km-value for the wild-type enzyme. kcat is 1.7fold higher as compared to the wild-type enzyme
H206A
-
Km-value for agmatine is 2.1fold lower than the Km-value for the wild-type enzyme. kcat is 90% compared to the wild-type value
H394A
-
Km-value for agmatine is 2.3fold higher than the Km-value for the wild-type enzyme. kcat ist identical to wild-type enzyme
H435A
-
Km-value for agmatine is 1.5fold higher than the Km-value for the wild-type enzyme. kcat ist 70% compared to the wild-type value
H65A
-
incubation of the mutant with 50 mM EDTA (pH 7.5) and subsequent dialysis to remove the chelating agent results in the loss of agmatinase activity. Even in the presence of Mn2+ only about 20% of the activity of the mutant enzyme is recovered. Km-value for agmatine is 1.44fold higher than the Km-value for the wild-type enzyme. kcat is 1.1fold higher as compared to the wild-type enzyme
H126N
-
51% of wild-type activity with Mn2+-activated mutant enzyme. Interaction with the required Mn2+ is significantly altered. Mutation is not accompanied by change in Km-value, Ki-value for putrescine inhibition, molecular weight, tryptophan fluorescence properties or CD spectra of the enzyme
H151N
-
30% of wild-type activity with Mn2+-activated mutant enzyme. Interaction with the required Mn2+ is significantly altered. Mutation is not accompanied by change in Km-value, Ki-value for putrescine inhibition, molecular weight, tryptophan fluorescence properties or CD spectra of the enzyme
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme appears to be active in the mono and binuclear form, with binding of the second metal ion increasing both reactivity and stability
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as a fusion protein with the C-terminal eight-residue His-tag
-
expression in Escherichia coli. Mainly obtained as inactive inclusion body in Escherichia coli
-
residues Ala36-Val352 overexpressed as a fusion with both N- and C-terminal purification tags in Escherichia coli
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
agmatinase expression is up-regulated in hippocampal interneurons of patients with mood disorders
-
protein expression increases more than 2fold in morpholino antisense oligonucleotide-ornithine decarboxylase 1-knockdown conceptuses and uteri
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Friedrich, B.; Magasanik, B.
Enzymes of agmatine degradation and the control of their synthesis in Klebsiella aerogenes
J. Bacteriol.
137
1127-1133
1979
Klebsiella aerogenes
brenda
Boldt, A.; Miersch, J.; Reinbothe, H.
Metabolism of agmatine in fruit-bodies of the fungus Panus tigrinus (bull. ex. fr.) sing.
Phytochemistry
10
731-738
1971
Lentinus tigrinus
-
brenda
Carvajal, N.; Olate, J.; Salas, M.; Lopez, V.; Cerpa, J.; Herrera, P.; Uribe, E.
Evidence that histidine-163 is critical for catalytic activity, but not for substrate binding to Escherichia coli agmatinase
Biochem. Biophys. Res. Commun.
264
196-200
1999
Escherichia coli
brenda
Vicente, C.; Legaz, M.E.
Purification and properties of agmatine amidinohydrolase of Evernia prunastri
Physiol. Plant.
55
335-339
1982
Evernia prunastri
-
brenda
Legaz, M.E.; Vicente, C.
Endogenous inactivators of arginase, L-arginine decarboxylase, and agmatine amidinohydrolase in Evernia prunastri thallus
Plant Physiol.
71
300-302
1983
Evernia prunastri
brenda
White Tabor, C.; Tabor, H.; Hafner, E.W.; Markham, G.D.; Boyle, S.M.
Cloning of the Escherichia coli genes for the biosynthetic enzymes fo polyamines
Methods Enzymol.
94
117-121
1983
Escherichia coli
brenda
Shaibe, E.; Metzer, E.; Halpern, Y.S.
Metabolic pathway for the utilization of L-arginine, L-ornithine, agmatine, and putrescine as nitrogen sources in Escherichia coli K-12
J. Bacteriol.
163
933-937
1985
Escherichia coli
brenda
Satishchandran, C.; Boyle S.M.
Purification and properties of agmatine ureohydrolase, a putrescine biosynthetic enzyme in Escherichia coli
J. Bacteriol.
165
843-848
1986
Escherichia coli
brenda
Sastre, M.; Regunathan, S.; Galea, E.; Reis, D.J.
Agmatinase activity in rat brain: a metabolic pathway for the degradation of agmatine
J. Neurochem.
67
1761-1765
1995
Rattus norvegicus
brenda
Szumanski, M.B.W.; Boyle, S.M.
Influence of cyclic AMP, agmatine and a novel protein encoded by a flanking gene on speB (agmatine ureohydrolase) in Escherichia coli
J. Bacteriol.
174
758-764
1992
Escherichia coli
brenda
Szumanski, M.B.W.; Boyle, S.M.
Analysis and sequence of the speB gene encoding agmatine ureohydrolase, a putrescine biosynthetic enzyme in Escherichia coli
J. Bacteriol.
172
538-547
1990
Escherichia coli
brenda
Carvajal, N.; Lopez, V.; Salas, M.; Uribe, E.; Herrera, P.; Cerpa, J.
Manganese is essential for catalytic activity of Escherichia coli Agmatinase
Biochem. Biophys. Res. Commun.
258
808-811
1999
Escherichia coli
brenda
Carvajal, N.; Orellana, M.S.; Salas, M.; Enriquez, P.; Alarcon, R.; Uribe, E.; Lopez, V.
Kinetic studies and site-directed mutagenesis of Escherichia coli agmatinase. A role for Glu274 in binding and correct positioning of the substrate guanidinium group
Arch. Biochem. Biophys.
430
185-190
2004
Escherichia coli
brenda
Salas, M.; Rodriguez, R.; Lopez, N.; Uribe, E.; Lopez, V.; Carvajal, N.
Insights into the reaction mechanism of Escherichia coli agmatinase by site-directed mutagenesis and molecular modelling
Eur. J. Biochem.
269
5522-5526
2002
Escherichia coli
brenda
Lee, J.A.; Ahn, H.J.; Ha, J.Y.; Shim, S.M.; Kim, K.H.; Kim, H.K.; Suh, S.W.
Crystallization and preliminary X-ray crystallographic analysis of a putative agmatinase from Deinococcus radiodurans
Acta Crystallogr. Sect. D
60
1890-1892
2004
Deinococcus radiodurans
brenda
Kim, K.H.; Ahn, H.J.; Kim, D.J.; Lee, H.H.; Ha, J.Y.; Kim, H.K.; Yoon, H.J.; Suh, S.W.
Expression, crystallization and preliminary X-ray crystallographic analysis of human agmatinase
Acta Crystallogr. Sect. F
61
889-891
2005
Homo sapiens
brenda
Goda, S.; Sakuraba, H.; Kawarabayasi, Y.; Ohshima, T.
The first archaeal agmatinase from anaerobic hyperthermophilic archaeon Pyrococcus horikoshii: cloning, expression, and characterization
Biochim. Biophys. Acta
1748
110-115
2005
Pyrococcus horikoshii
brenda
Dallmann, K.; Junker, H.; Balabanov, S.; Zimmermann, U.; Giebel, J.; Walther, R.
Human agmatinase is diminished in the clear cell type of renal cell carcinoma
Int. J. Cancer
108
342-347
2004
Homo sapiens
brenda
Ahn, H.J.; Kim, K.H.; Lee, J.; Ha, J.Y.; Lee, H.H.; Kim, D.; Yoon, H.J.; Kwon, A.R.; Suh, S.W.
Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily
J. Biol. Chem.
279
50505-50513
2004
Deinococcus radiodurans
brenda
Salas, M.; Lopez, V.; Uribe, E.; Carvajal, N.
Studies on the interaction of Escherichia coli agmatinase with manganese ions: structural and kinetic studies of the H126N and H151N variants
J. Inorg. Biochem.
98
1032-1036
2004
Escherichia coli
brenda
Alarcon, R.; Orellana, M.S.; Neira, B.; Uribe, E.; Garcia, J.R.; Carvajal, N.
Mutational analysis of substrate recognition by human arginase type I -agmatinase activity of the N130D variant
FEBS J.
273
5625-5631
2006
Homo sapiens
brenda
Haenisch, B.; von Kuegelgen, I.; Boenisch, H.; Goethert, M.; Sauerbruch, T.; Schepke, M.; Marklein, G.; Hoefling, K.; Schroeder, D.; Molderings, G.J.
Regulatory mechanisms underlying agmatine homeostasis in humans
Am. J. Physiol. Gastrointest. Liver Physiol.
295
G1104-G1110
2008
Homo sapiens (Q9BSE5), Homo sapiens
brenda
Bernstein, H.G.; Derst, C.; Stich, C.; Pruess, H.; Peters, D.; Krauss, M.; Bogerts, B.; Veh, R.W.; Laube, G.
The agmatine-degrading enzyme agmatinase: a key to agmatine signaling in rat and human brain?
Amino Acids
40
453-465
2010
Homo sapiens, Rattus norvegicus
brenda
Mella, C.; Martinez, F.; de Los Angeles Garcia, M.; Nualart, F.; Castro, V.; Bustos, P.; Carvajal, N.; Uribe, E.
Expression and localization of an agmatinase-like protein in the rat brain
Histochem. Cell Biol.
134
137-144
2010
Rattus norvegicus
brenda
Chattopadhyay, M.K.; Tabor, C.W.; Tabor, H.
Polyamines are not required for aerobic growth of Escherichia coli: preparation of a strain with deletions in all of the genes for polyamine biosynthesis
J. Bacteriol.
191
5549-5552
2009
Escherichia coli
brenda
Madai, V.I.; Poller, W.C.; Peters, D.; Berger, J.; Paliege, K.; Bernard, R.; Veh, R.W.; Laube, G.
Synaptic localisation of agmatinase in rat cerebral cortex revealed by virtual pre-embedding
Amino Acids
43
1399-1403
2012
Rattus norvegicus
brenda
Bernstein, H.G.; Stich, C.; Jaeger, K.; Dobrowolny, H.; Wick, M.; Steiner, J.; Veh, R.; Bogerts, B.; Laube, G.
Agmatinase, an inactivator of the putative endogenous antidepressant agmatine, is strongly upregulated in hippocampal interneurons of subjects with mood disorders
Neuropharmacology
62
237-246
2012
Homo sapiens
brenda
Miller, D.; Xu, H.; White, R.H.
A new subfamily of agmatinases present in methanogenic Archaea is Fe(II) dependent
Biochemistry
51
3067-3078
2012
Methanocaldococcus jannaschii (Q57757), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57757)
brenda
Wang, X.; Ying, W.; Dunlap, K.A.; Lin, G.; Satterfield, M.C.; Burghardt, R.C.; Wu, G.; Bazer, F.W.
Arginine decarboxylase and agmatinase: an alternative pathway for de novo biosynthesis of polyamines for development of mammalian conceptuses
Biol. Reprod.
90
84
2014
Ovis aries (W5PHZ9)
brenda
Burnat, M.; Flores, E.
Inactivation of agmatinase expressed in vegetative cells alters arginine catabolism and prevents diazotrophic growth in the heterocyst-forming cyanobacterium Anabaena
MicrobiologyOpen
3
777-792
2014
Anabaena sp. (Q8YUM9), Anabaena sp., Anabaena sp. PCC 7120 (Q8YUM9)
brenda
Prunetti, L.; Graf, M.; Blaby, I.K.; Peil, L.; Makkay, A.M.; Starosta, A.L.; Papke, R.T.; Oshima, T., Wilson, D.N.; de Crcy-Lagard, V.
Deciphering the translation initiation factor 5A modification pathway in halophilic Archaea
Archaea
2016
7316725
2016
Haloferax volcanii (D4GWG4), Haloferax volcanii DSM 3757 (D4GWG4)
brenda
Lenis, Y.Y.; Elmetwally, M.A.; Tang, W.; Satterfield, C.; Dunlap, K.; Wu, G.; Bazer, F.W.
Functional roles of agmatinase during the peri-implantation period of pregnancy in sheep
Amino Acids
50
293-308
2018
Ovis aries (W5PHZ9), Ovis aries
brenda
Shao, Y.; Li, C.; Zhang, W.; Xu, W.; Duan, X.; Li, Y.; Qiu, Q.; Jin, C.
Cloning and comparative analysis the proximal promoter activities of arginase and agmatinase genes in Apostichopus japonicus
Dev. Comp. Immunol.
65
299-308
2016
Apostichopus japonicus (A0A146AXJ2), Apostichopus japonicus
brenda
Perez-Mozqueda, L.L.; Vazquez-Duhalt, R.; Castro-Longoria, E.
Role and dynamics of an agmatinase-like protein (AGM-1) in Neurospora crassa
Fungal Genet. Biol.
132
103264
2019
Neurospora crassa (Q1K7T0), Neurospora crassa
brenda
Quinones, M.; Cofre, J.; Benitez, J.; Garcia, D.; Romero, N.; Gonzalez, A.; Carvajal, N.; Garcia, M.; Lopez, V.; Schenk, G.; Uribe, E.
Insight on the interaction of an agmatinase-like protein with Mn(2+) activator ions
J. Inorg. Biochem.
145
65-69
2015
Rattus norvegicus
brenda
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Release 2023.1 (January 2023)
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