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Information on EC 3.5.3.11 - agmatinase and Organism(s) Homo sapiens and UniProt Accession Q9BSE5

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.3 In linear amidines
                3.5.3.11 agmatinase
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Homo sapiens
UNIPROT: Q9BSE5 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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agmatine
+
H2O
=
putrescine
+
urea
+
=
+
Synonyms
agmatinase, agmatine ureohydrolase, agmat, agm-1, agmatinase-like protein, agmatine amidinohydrolase, alr2310, proclavaminic acid amidino hydrolase, mj0309, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agmatinase
-
-
agmatine ureohydrolase
-
-
-
-
AUH
-
-
-
-
N130D variant of arginase type I
-
-
Proclavaminic acid amidino hydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
agmatine amidinohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37289-16-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
agmatine + H2O
putrescine + urea
show the reaction diagram
-
-
-
?
agmatine + H2O
putrescine + urea
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
agmatine + H2O
putrescine + urea
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
totally dependent on Mn2+ for catalytic activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
putrescine
-
linear competitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
agmatine
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
agmatine
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
putrescine
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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
Manually annotated by BRENDA team
-
agmatinase in normal kidneys is restricted to tubulus epithelial cells, while in tumors activity is low and heterogeneous
Manually annotated by BRENDA team
-
agmatinase in normal kidneys is restricted to tubulus epithelial cells, while in tumors activity is low and heterogeneous
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SPEB_HUMAN
352
0
37660
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
-
SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain JM109
-
residues Ala36-Val352 overexpressed as a fusion with both N- and C-terminal purification tags in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
agmatinase expression is up-regulated in hippocampal interneurons of patients with mood disorders
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team