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Information on EC 4.1.1.19 - arginine decarboxylase and Organism(s) Homo sapiens
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4.1.1.19 arginine decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 4.1.1.19
- polyamine
- putrescine
- ornithine
- spermidine
- s-adenosylmethionine
- arginase
-
diamine
- samdc
- decarboxylases
- agmatinase
- deiminase
- alpha-difluoromethylornithine
- cadaverine
-
imidazoline
- d-arginine
- pao
-
3.5.3.1
-
iminohydrolase
-
arginine-dependent
-
scots
-
ureohydrolase
- difluoromethylornithine
-
pyrogenic
- drug development
- agriculture
- hyoscyamine
- trifoliata
- poncirus
- speb
-
tropane
- dl-alpha-difluoromethylornithine
- antizyme
- datura
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
arginine decarboxylase, spea2, argdc, spea1, biosynthetic arginine decarboxylase, ppadc, l-arginine decarboxylase, pyruvoyl-dependent arginine decarboxylase, atadc2, ptadc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADC
ARGDC
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-
-
-
bADC
-
-
-
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Biosynthetic arginine decarboxylase
-
-
-
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dADC
-
-
-
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Decarboxylase, arginine
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-
-
-
L-Arginine decarboxylase
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-
-
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Synthetic arginine decarboxylase
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-
-
-
ADC
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-arginine carboxy-lyase (agmatine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
9024-77-5
-
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
additional information
?
-
-
human ornithine decarboxylase paralogue (ODCp) is not an arginine decarboxylase
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibition by 1 mM alpha-difluoromethylornithine
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme activity and agmatine levels in human sputum peak during cystic fibrosis illness, decrease with treatment, and is positively correlated with inflammatory cytokines. Bacterial pathways of agmatine metabolism are able to impact the agmatine levels within the lung during infection
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
agmatine is synthesized by the arginine decarboxylase pathway, but is essentially undetectable if the aguBA operon is left intact
physiological function
physiological function
higher level of hexahistidine tagged human ADC transgene expression completely trigger the endogenous agmatine synthesis during H2O2 injury thus protecting NIH3T3 cells against cytotoxicity
physiological function
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agmatine, an endogenous polyamine catalyzed from L-arginine by arginine decarboxylase (ADC), is a neuromodulator that protects neurons/glia against various injuries. Agmatine, is naturally found in the mammalian central nervous system (CNS) and acts as a multifunctional neuromodulator. It is packed into synaptic vesicles and released from synaptosomes by neuronal depolarization. Agmatine can stimulate alpha2-adrenergic and imidazoline receptors. Retroviral expression of human arginine decarboxylase reduces oxidative stress injury in mouse cortical astrocytes
physiological function
-
human ornithine decarboxylase paralogue (ODC-like protein, ODCp or ODC paralogue), which has been suggested to function either as mammalian arginine decarboxylase, ADC, or ornithine decarboxylase, ODC, is actually an antizyme inhibitor but not an arginine or ornithine decarboxylase. Human ODCp has no intrinsic ADC activity. ODCp acts as a regulator of ODC activity and inhibits its proteasomal degradation. ODCp is degraded by ubiquitination like AZI (AZ inhibitor)
physiological function
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in humans, enzyme-produced agmatine is a neurotransmitter with affinities towards alpha2-adrenoreceptors, serotonin receptors, and may inhibit nitric oxide synthase. Agmatine is at the center of a competing metabolism in the human lung during airways infections and is influenced by the metabolic phenotypes of the infecting pathogens, e.g. Pseudomonas aeruginosa
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
agmatine-producing mouse cortical astrocytes were developed through transduction of the transformed heterologous human ADC gene
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ADC, functional overexpression from retroviral vector hADC pLXSN in murine cortical astrocytes leading to and astrocyte-protective effect of human arginine decarboxylase transduction against oxygen-glucose deprivation (OGD), overview
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the hexahistidine tagged human ADC gene is delivered into mouse fibroblast cell line (NIH3T3) using retroviral vector and transfected into the PT-67 cell line
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme activity and agmatine levels in human sputum peak during cystic fibrosis illness, decrease with treatment, and is positively correlated with inflammatory cytokines
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhu, M.Y.; Iyo, A.; Piletz, J.E.; Regunathan, S.
Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine
Biochim. Biophys. Acta
1670
156-164
2004
Homo sapiens (Q96A70), Homo sapiens
Kanerva, K.; Makitie, L.T.; Pelander, A.; Heiskala, M.; Andersson, L.C.
Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor but not an arginine decarboxylase
Biochem. J.
409
187-192
2008
Homo sapiens
Moon, S.U.; Kwon, K.H.; Kim, J.H.; Bokara, K.K.; Park, K.A.; Lee, W.T.; Lee, J.E.
Recombinant hexahistidine arginine decarboxylase (hisADC) induced endogenous agmatine synthesis during stress
Mol. Cell. Biochem.
345
53-60
2010
Homo sapiens (Q96A70), Homo sapiens
Kanerva, K.; Maekitie, L.T.; Pelander, A.; Heiskala, M.; Andersson, L.C.
Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor but not an arginine decarboxylase
Biochem. J.
409
187-192
2008
Homo sapiens
Hong, S.; Son, M.R.; Yun, K.; Lee, W.T.; Park, K.A.; Lee, J.E.
Retroviral expression of human arginine decarboxylase reduces oxidative stress injury in mouse cortical astrocytes
BMC Neurosci.
15
99
2014
Homo sapiens
Paulson, N.B.; Gilbertsen, A.J.; Dalluge, J.J.; Welchlin, C.W.; Hughes, J.; Han, W.; Blackwell, T.S.; Laguna, T.A.; Williams, B.J.
The arginine decarboxylase pathways of host and pathogen interact to impact inflammatory pathways in the lung
PLoS ONE
9
e111441
2014
Homo sapiens, Mus musculus, Pseudomonas aeruginosa (Q9HUX1), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 (Q9HUX1)
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