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Information on EC 4.1.1.17 - ornithine decarboxylase and Organism(s) Mus musculus and UniProt Accession P00860
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4.1.1.17 ornithine decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 4.1.1.17
- polyamine
- spermidine
- alpha-difluoromethylornithine
- carcinogenesis
- antizyme
-
chemopreventive
- 12-o-tetradecanoylphorbol-13-acetate
-
phorbol
- mucosa
- difluoromethylornithine
-
diamine
- decarboxylases
-
n1-acetyltransferase
- hyperplasia
- arginase
- c-myc
-
antiproliferative
-
tpa-induced
- prostaglandin
- testosterone
-
3hthymidine
- tumorigenesis
-
mitogen
- cycloheximide
- c-fos
- methylglyoxal
-
tpa-treated
- 1,2-dimethylhydrazine
- isoproterenol
- hairless
- degrons
-
12-o-tetradecanoyl
-
hepatectomy
- cadaverine
- s-adenosyl-l-methionine
- drug development
- azoxymethane
-
protooncogene
- papilloma
-
7,12-dimethylbenzaanthracene
- agmatine
- phorbol-13-acetate
- medicine
-
tumor-promoting
- food industry
- diagnostics
- nitrilotriacetate
- pharmacology
- prolactin
-
crypt
- trypanothione
-
12-o-tetradecanoylphorbol
-
ester-induced
- actinomycin
- mezerein
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
odc, ornithine decarboxylase, ldodc, lysine/ornithine decarboxylase, s-adenosylmethionine decarboxylase/ornithine decarboxylase, ldc/odc, ddodc, odc-paralogue, xodc2, adometdc/odc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bODC
-
-
-
-
Decarboxylase, ornithine
-
-
-
-
ODC
ODC-paralogue
-
-
-
-
XODC1
-
-
-
-
XODC2
-
-
-
-
ODC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
SYSTEMATIC NAME
IUBMB Comments
L-ornithine carboxy-lyase (putrescine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
9024-60-6
-
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
L-lysine
cadaverine + CO2
-
L-lysine is a poor substrate for ODC, with a Km approximately 100fold higher than that of L-ornithine
-
-
?
L-ornithine
putrescine + CO2
the enzyme is involved in polyamine biosynthesis, and is regulated mainly by posttranscriptional mechanisms, influence of polyamine deprivation on catecholamine and corticoid levels, sexual dimorphism of the enzyme in the adrenal gland resulting in sex-related differences in prevalent diseases and stress responses, overview
-
-
?
L-ornithine
putrescine + CO2
-
-
677508, 680214, 680257, 697094, 708244, 708546, 708797, 709519, 709568, 710340, 713681, 713718, 713733, 714920, 749065
-
-
?
L-ornithine
putrescine + CO2
-
enzyme regulation, overview, ODC initiates the polyamine biosynthetic pathway, rapid turnover of ODC is brought about by the 26S proteasome, the structure of the COOH-terminal region needed for rapid degradation, ubiquitination is not required for this degradation, antizyme increases the degradation of ODC by enhancing its interaction with the proteasome but does not increase the rate of proteasomal processing, role of ODC and antizyme in carcinogenesis, overview
-
-
?
L-ornithine
putrescine + CO2
-
first enzyme in polyamine biosynthesis, the unique and tight regulation of the enzyme occurs at the levels of transcription, translation and protein degradation, dysregulation of ornithine decarboxylase during oncogenic transformation, mechanisms and therapeutic potential, overview, ODC induction as a necessary step in MEK-induced tumorigenesis, enzyme inhibition reduces tumor growth, synergistic or additive effects with vindesine or doxorubicin, overview
-
-
?
L-ornithine
putrescine + CO2
-
Cys360 plays an essential role in ensuring correct protonation of the decarboxylated reaction intermediate at Calpha
-
-
?
L-ornithine
putrescine + CO2
-
key rate-limiting enzyme in polyamine biosynthesis, elevated levels of ODC and polyamines stimulate proliferation of keratinocytes
-
-
?
additional information
?
-
circadian variations in ODC activity in female and male mice, influence of sex hormones, overview
-
-
?
additional information
?
-
-
circadian variations in ODC activity in female and male mice, influence of sex hormones, overview
-
-
?
additional information
?
-
mouse ODC is quickly degraded by the 26S proteasome in an ubiquitin-dependent manner in mammalian and fungal cells. Within cODC, Cys441 functions as a proteasome association element, while the C-terminal end of cODC initiates entry into the proteasome
-
-
?
additional information
?
-
-
mouse ODC is quickly degraded by the 26S proteasome in an ubiquitin-dependent manner in mammalian and fungal cells. Within cODC, Cys441 functions as a proteasome association element, while the C-terminal end of cODC initiates entry into the proteasome
-
-
?
additional information
?
-
-
the Raf/MEK/ERK pathway is involved in the regulation of ODC during skin tumorigenesis, overview
-
-
?
additional information
?
-
-
NAD(P)H quinone oxidoreductase binds to the enzyme and stabilizes it, this interaction is disrupted with dicoumarol, it sensitizes ODC monomers to degradation by the 20S proteasome in a manner independent of both antizyme and ubiquitin, overview
-
-
?
additional information
?
-
-
role of ornithine decarboxylase antizyme inhibitor in vivo, ODC antizyme inhibitor, AZI, plays an important role in regulating the levels of ODC, putrescine and spermidine in mice, and is essential for the survival of mice, overview
-
-
?
additional information
?
-
-
small functional upstream ORF, uORF, often performing a regulatory role, precedes the translation start site for the main products. The murine AUG-less uORF present in mouse antizyme inhibitor, one of the ornithine decarboxylase homologs in mammals, mediates polyamine-induced repression of the downstream main ORF, this repression is part of an autoregulatory circuit, and one of its sensors is the AUU codon, murine uORF-M regulates the expression of the main ORF. Translation initiation codon identity is likely used for regulation in eukaryotes, overview
-
-
?
additional information
?
-
-
the enzyme induces phosphorylation of ataxia telangiectasia mutated and its substrate p53, which are significantly induced both in Ker/ODC and in K6/ODC transgenic skin, overview
-
-
?
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
L-ornithine
putrescine + CO2
the enzyme is involved in polyamine biosynthesis, and is regulated mainly by posttranscriptional mechanisms, influence of polyamine deprivation on catecholamine and corticoid levels, sexual dimorphism of the enzyme in the adrenal gland resulting in sex-related differences in prevalent diseases and stress responses, overview
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
enzyme regulation, overview, ODC initiates the polyamine biosynthetic pathway, rapid turnover of ODC is brought about by the 26S proteasome, the structure of the COOH-terminal region needed for rapid degradation, ubiquitination is not required for this degradation, antizyme increases the degradation of ODC by enhancing its interaction with the proteasome but does not increase the rate of proteasomal processing, role of ODC and antizyme in carcinogenesis, overview
-
-
?
L-ornithine
putrescine + CO2
-
first enzyme in polyamine biosynthesis, the unique and tight regulation of the enzyme occurs at the levels of transcription, translation and protein degradation, dysregulation of ornithine decarboxylase during oncogenic transformation, mechanisms and therapeutic potential, overview, ODC induction as a necessary step in MEK-induced tumorigenesis, enzyme inhibition reduces tumor growth, synergistic or additive effects with vindesine or doxorubicin, overview
-
-
?
L-ornithine
putrescine + CO2
-
key rate-limiting enzyme in polyamine biosynthesis, elevated levels of ODC and polyamines stimulate proliferation of keratinocytes
-
-
?
additional information
?
-
circadian variations in ODC activity in female and male mice, influence of sex hormones, overview
-
-
?
additional information
?
-
-
circadian variations in ODC activity in female and male mice, influence of sex hormones, overview
-
-
?
additional information
?
-
mouse ODC is quickly degraded by the 26S proteasome in an ubiquitin-dependent manner in mammalian and fungal cells. Within cODC, Cys441 functions as a proteasome association element, while the C-terminal end of cODC initiates entry into the proteasome
-
-
?
additional information
?
-
-
mouse ODC is quickly degraded by the 26S proteasome in an ubiquitin-dependent manner in mammalian and fungal cells. Within cODC, Cys441 functions as a proteasome association element, while the C-terminal end of cODC initiates entry into the proteasome
-
-
?
additional information
?
-
-
the Raf/MEK/ERK pathway is involved in the regulation of ODC during skin tumorigenesis, overview
-
-
?
additional information
?
-
-
role of ornithine decarboxylase antizyme inhibitor in vivo, ODC antizyme inhibitor, AZI, plays an important role in regulating the levels of ODC, putrescine and spermidine in mice, and is essential for the survival of mice, overview
-
-
?
additional information
?
-
-
small functional upstream ORF, uORF, often performing a regulatory role, precedes the translation start site for the main products. The murine AUG-less uORF present in mouse antizyme inhibitor, one of the ornithine decarboxylase homologs in mammals, mediates polyamine-induced repression of the downstream main ORF, this repression is part of an autoregulatory circuit, and one of its sensors is the AUU codon, murine uORF-M regulates the expression of the main ORF. Translation initiation codon identity is likely used for regulation in eukaryotes, overview
-
-
?
additional information
?
-
-
the enzyme induces phosphorylation of ataxia telangiectasia mutated and its substrate p53, which are significantly induced both in Ker/ODC and in K6/ODC transgenic skin, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
the PLP cofactor is bound in a Schiff base linkage to Lys69
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-difluoromethylornithine
DFMO, is used in therapy combined with MQT 1426, a polyamine transport inhibitor, for treatment of squamous cell carcinoma in a mouse model, K6/ODC
testosterone
29% decrease in activity in female mice, more important chnage in female compared to male mice, overview
testosterone propionate
decreases ODC activity by 56% in adrenal gland of castrated male mice, not in female mice
alpha-difluoromethylornithine
-
i.e. DFMO, irreversible inactivator, antitumor action of ODC inhibition using DFMO, chemopreventive effects, DFMO provides significant protection against N-butyl-N(4-hydroxybutyl)-nitrosamine-induced bladder cancer, overview
alpha-difluoromethylornithine
-
the enzyme is inhibited in the combination therapy with 2-difluoromethylornithine and a polyamine transport inhibitor MQT 1426, i.e. D-Lys-spermine, against squamous cell carcinoma, the apoptotic index of the cells is transiently increased by combination therapy but not by DFMO alone, a K6/ODC mouse model, overview
alpha-DL-difluoromethylornithine
-
experimental interruption of pregnancy in the mouse
antizyme
-
an important endogenous regulator of ODC and polyamine homeostasis, overview, the wild type form of ODC has an extremely short half life of 20-30 min, and its degradation is mediated by antizyme, which binds to the monomeric form of ODC, preventing formation of the enzymatically active homodimer, and then targets ODC for degradation
-
antizyme
-
there are multiple antizyme genes with at least four members, all members, which are localized in different compartments or tissue, inhibit ODC activity, overview, the antizyme inhibitor blocks the effects of antizyme on the enzyme, overview
-
antizyme
-
role of ornithine decarboxylase antizyme inhibitor in vivo, ODC antizyme inhibitor, AZI, regulates ODC activity in cell cultures
-
additional information
MQT 1426 has no inhibitory effect on squamous cell carcinoma ODC activity nor does it enhance the inhibition by 2-difluoromethylornithine, but it reduces the polyamine levels in squamous cell carcinoma cells
-
additional information
-
enzyme activity is not affected in secondary cell lines exposed to 872 MHz RF radiation, overview
-
additional information
-
inhibition of ODC activity reverts the transformation of cells in vitro and reduces tumor growth
-
additional information
-
enzyme degradation is enhanced by antizyme, a polyamine-induced protein, this is prevented by ODCp, a brain- and testis-specific ornithine decarboxylase paralogue, overview
-
additional information
-
hemin reduces the 12-O-tetradecanoylphorobl-13-acetate-induced expression of ODC, and hemin suppresses the 12-O-tetradecanoylphorobl-13-acetate-induced activation of extracellular signal-regulated protein kinase and p38 MAPK
-
additional information
-
radiation at 5 W/kg does not affect the enzyme activity or cell proliferation and caspase-3 activity in L-929 cells
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
ODC induction, e.g. in response to the tumor promoter 12-O-tetradecanoylphorbol-13-acetate, is a necessary step in MEK-induced tumorigenesis, ODC is induced during carcinogenesis by a variety of oncogenic stimuli, overview
-
additional information
-
12-O-tetradecanoylphorobl-13-acetate induces expression of ODC
-
additional information
-
radiation at 5 W/kg does not affect the enzyme activity or cell proliferation and caspase-3 activity in L-929 cells
-
additional information
-
antizyme inhibitor has the ability to bind antizyme with higher affinity than ODC, in this manner, it prevents antizyme from binding and inhibiting ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
in the adult prostate, ornithine decarboxylase activity is androgen-dependent
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
circadian variations in ODC activity in female and male mice, overview
additional information
-
circadian variations in ODC activity in female and male mice, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
CD11b+ myeloid cells and CD11b- nonmyeloid cells from the gastric lamina propria of mice infected with Helicobacter pylori premouse Sydney strain 1 (PMSS1) for 48 h
-
ornithine decarboxylase protein is expressed in the urogenital sinus (UGS) epithelium of the male and female embryo prior to prostate development, and expression continues in prostatic epithelial buds as they emerge from the UGS
-
ornithine decarboxylase protein is expressed in the epithelium of the ventral, dorsolateral and anterior lobes of the adult mouse prostate
additional information
-
epidermal cell line, induction of enzyme by 12-O-tetradecanoylphorbol-13-acetate. Induction is suppressed by polysaccharides from soybean and soybeans fermented with Phellinus igniarius or Agrocybe cylindracea
-
of testosterone treated mouse. 13fold higher activity in male mice than that in females
-
hyperplastic and hypertrophic kidney, 80- to 1000fold increase in enzyme activity
-
overexpression of constitutively active Ras12V results in up to 20fold increase of enzyme activity due to increase in enzyme transcription and translation
additional information
adrenal weight, ODC activity, immunoreactivity, and corticosterone and aldosterone secretion are higher in female than in male mice, while orchidectomy brings the male parameters closer to the values of females, overview
additional information
-
adrenal weight, ODC activity, immunoreactivity, and corticosterone and aldosterone secretion are higher in female than in male mice, while orchidectomy brings the male parameters closer to the values of females, overview
additional information
-
immunocytochemical localization of ornithine decarboxylase
additional information
-
ornithine decarboxylase co-localizes with vimentin in the developing urogenital sinus. Immunohistochemic localization analysis, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
metabolism
physiological function
additional information
enzyme residue Cys441 takes part in functionally significant side-chain interactions with an amino acid in this local neighbourhood. Cys441 is intolerant of positional change. Cys441 does not form an intramolecular disulfide bond
malfunction
myeloid-specific deletion of Odc (OdcDELTAmye) provokes a marked increase in the response of mouse bone marrow-derived macrophages to M1 stimuli including Helicobacter pylori, Citrobacter rodentium, or lipopolysaccharides plus IFN-gamma, and to increased expression of M1 genes
malfunction
myeloid-specific Odc deletion significantly increases gastric and colonic inflammation, respectively, and enhances M1 activation. Add-back of putrescine, the product of ODC, reverses the increased macrophage activation, indicating that ODC and putrescine are regulators of macrophage function. Odc-deficient macrophages have increased histone 3, lysine 4 (H3K4) monomethylation, and H3K9 acetylation, accompanied by decreased H3K9 di/trimethylation both in vivo and ex vivo in primary macrophages. These alterations in chromatin structure directly result in upregulated gene transcription, especially M1 gene expression. OdcDELTAmye mice have significantly increased histologic gastritis, but significantly decreased Helicobacter pylori burden after chronic infection. ODC deletion augments proinflammatory cytokine and chemokine production in vivo. ODC deletion in macrophages also enhances NLRP3-inflammasome activation. ODC deletion promotes histone modifications leading to euchromatin formation and transcription
metabolism
murine ODC (ornithine decarboxylase) is quickly degraded by the 26S proteasome in mammalian and fungal cells. Its degradation is independent of ubiquitin but requires a degradation signal composed of residues 425-461 at the ODC C-terminus, cODC (the last 37 amino acids of the ODC C-terminus). The presence of two essential elements in the degradation signal: the first consists of cysteine and alanine at residues 441 and 442 respectively, the second element is the C-terminus distal to residue 442. It has little or no sequence specificity, but is intolerant of insertions or deletions that alter its span. Reducing conditions, which preclude all well-characterized chemical reactions of the Cys441 thiol, are essential for in vitro degradation. The degradative function of Cys441 does not involve its participation in chemical reaction, instead, it functions within a structural element for recognition by the 26S proteasome. Rattus norvegicus AZ1-stimulated ODC degradation is conducted in reticulocyte lysate. the thiol group of Cys441 must be maintained in a reduced state to act as a recognition signal for the 26S proteasome, and does not act as a bonding partner with other residues. Within cODC, Cys441 functions as a proteasome association element, while the C-terminal end of cODC initiates entry into the proteasome
metabolism
ornithine decarboxylase (ODC) is the rate-limiting enzyme for polyamine biosynthesis
physiological function
enzyme ODC is involved in polyamine biosynthesis and squamous cell carcinoma proliferation
physiological function
ornithine decarboxylase (ODC) is the rate-limiting enzyme in polyamine metabolism. Ornithine decarboxylase regulates M1 macrophage activation and mucosal inflammation via histone modifications. Macrophage-derived ODC is a critical regulator of M1 macrophage activation during both Helicobacter pylori and Citrobacter rodentium infection. ODC in macrophages tempers antimicrobial, M1 macrophage responses during bacterial infections through histone modifications and altered euchromatin formation, leading to the persistence and pathogenesis of these organisms. ODC-driven histone modifications are essential for alterations in M1 macrophage activation
physiological function
ornithine decarboxylase (ODC) is the regulatory enzyme in polyamine biosynthesis. Elevated ornithine decarboxylase activity promotes skin tumorigenesis by stimulating the recruitment of bulge stem cells but not via toxic polyamine catabolic metabolites (reactive oxygen species)
physiological function
polyamine biosynthesis begins with the production of the biogenic amine, putrescine, which is produced by the enzyme ornithine decarboxylase (ODC1). Ornithine decarboxylase (ODC) is the rate-limiting enzyme for polyamine biosynthesis and restricts M1 macrophage activation in gastrointestinal infections. Ornithine decarboxylase in macrophages exacerbates colitis and promotes colitis-associated colon carcinogenesis by impairing M1 immune responses, role of macrophage ODC in colonic epithelial-driven inflammation, overview. ODC regulates the mucosal pro-inflammatory response during acute colitis, contribution of epithelial-derived ODC to the development of dextran sulfate sodium-induced colitis
malfunction
-
inhibition of ODC activity in C2C12 myoblasts by alpha-difluoromethylornithine decreases myoblast number by 40% and 66% following 48 and 72 h of treatment, respectively
malfunction
-
ODC inhibition is associated with an abnormal morphology of the actin cytoskeleton during cell spreading and migration
malfunction
-
inhibiting ornithine decarboxylase using DL-alpha-difluromethylornithine in urogenital sinus (UGS) organ culture blocks the induction of prostatic buds by androgens, and significantly decreases expression of key prostate transcription factor, Nkx3.1, by androgens. DL-alpha-Difluromethylornithine also significantly decreases the expression of developmental regulatory gene Notch1. Other genes implicated in prostatic development, including Sox9, Wif1 and Srd5a2, are unaffected by the inhibitor. Inhibiting ornithine decarboxylase using pharmacologic agents such as alpha-difluromethylornithine or ablating Odc1 using a genetic approach renders pregnant mice unable to carry pups to term
metabolism
-
ornithine decarboxylase catalyzes the first and rate-limiting step in polyamine synthesis
physiological function
-
ornithine decarboxylase is able to boost the metabolic flux to the downstream scopolamine and enhance the overexpression of polyamine biosynthetic genes for enhanced production of scopolamine
physiological function
-
ornithine decarboxylase promotes myoblast proliferation and delays differentiation. Overexpression of Odc1 in C2C12 myoblasts results in a 27% increase in cell number vs. control when cells are grown under differentiation conditions for 96 h
physiological function
-
overexpression of ornithine decarboxylase decreases ventricular systolic function during induction of cardiac hypertrophy
physiological function
-
unperturbed ODC activity is a requirement for proper microvessel sprouting
physiological function
-
the first and rate-limiting step in polyamine synthesis is catalyzed by the enzyme ornithine decarboxylase which is encoded by the gene Odc1. Ornithine decarboxylase catalyzes the conversion of L-ornithine to putrescine. Ornithine decarboxylase activity is required for prostatic budding in the developing mouse prostate. Odc1 and polyamines are required for androgens to exert their effect in mediating prostatic bud induction, and are required for the expression of a subset of prostatic developmental regulatory genes including Notch1 and Nkx3.1. Testosterone administered to castrated male mice restores prostate secretory activity, whereas administering testosterone and the ornithine decarboxylase inhibitor DL-alpha-difluromethylornithine (DFMO) to castrated males does not restore prostate secretory activity, suggesting that polyamines are required for androgens to exert their effects
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). DCOR_MOUSE
461
0
51177
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
-
1 * 50000, SDS-PAGE, the enzyme exists as monomer at high salt concentrations and in polymeric form at low salt concentrations
53000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
-
1 * 50000, SDS-PAGE, the enzyme exists as monomer at high salt concentrations and in polymeric form at low salt concentrations
dimer
-
antizyme binds to the monomeric form of ODC, preventing formation of the enzymatically active homodimer, and then targets ODC for degradation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
murine ODC (ornithine decarboxylase) is quickly degraded by the 26S proteasome in mammalian and fungal cells. Its degradation is independent of ubiquitin but requires a degradation signal composed of residues 425-461 at the ODC C-terminus, cODC (the last 37 amino acids of the ODC C-terminus). The presence of two essential elements in the degradation signal: the first consists of cysteine and alanine at residues 441 and 442 respectively, the second element is the C-terminus distal to residue 442. It has little or no sequence specificity, but is intolerant of insertions or deletions that alter its span. Reducing conditions, which preclude all well-characterized chemical reactions of the Cys441 thiol, are essential for in vitro degradation. The degradative function of Cys441 does not involve its participation in chemical reaction, instead, it functions within a structural element for recognition by the 26S proteasome. Rattus norvegicus AZ1-stimulated ODC degradation is conducted in reticulocyte lysate. The thiol group of Cys441 must be maintained in a reduced state to act as a recognition signal for the 26S proteasome, and does not act as a bonding partner with other residues
additional information
-
degradation of enzyme is accelerated antizyme extract as well as by Selenomonas ruminantium P22 protein, which is a counterpart of antizyme. Degradation occurs via 26S proteasome
additional information
-
rapid turnover of ODC is brought about by the 26S proteasome, the structure of the COOH-terminal region needed for rapid degradation, ubiquitination is not required for this degradation, antizyme increases the degradation of ODC by enhancing its interaction with the proteasome but does not increase the rate of proteasomal processing, NAD(P)H quinone oxidoreductase binds to the enzyme and stabilizes it, this interaction is disrupted with dicoumarol, it sensitizes ODC monomers to degradation by the 20S proteasome in a manner independent of both antizyme and ubiquitin, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of truncated ODC at 1.6 A resolution, 0.01 mM of silica hydrogel on a microbridge, sitting within a 3.25 ml well containing 1 ml 10% polyethylene glycol is gently covered with 0.01 ml 26% polyethylene glycol 3350, the microbridge is transferred to a well containing 1 ml 26% polyethylene glycol 3350, protein solution containing 12 mg/ml ODC, 2.5 mM dithiothreitol, 1 mM EDTA is added to the microbridge and the well is sealed with tape, plate is left undisturbed in the dark at room temperature for 2 weeks
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A457W
C441A
C441A/A442C
site-directed mutagenesis, swapping the cysteine residue with either of the two adjacent residues stabilizes ODC, reducing degradation from 25% to less than 5% in each case
S440C/C441S
site-directed mutagenesis, swapping the cysteine residue with either of the two adjacent residues stabilizes ODC, reducing degradation from 25% to less than 5% in each case. The stabilization of ODC by the C441S mutation implies that the hydroxy group cannot replicate the functional properties of the thiol of Cys441
S456A
A123S
-
mutation in a conserved residue of the antizyme-binding region, mutant is somehow more resistant to degradation than wild-type. About 130% of wild-type activity
C360A
C441S
-
the isosteric alteration of the enzyme completely stabilizes ODC even in the presence of excess antizyme
E138A
-
mutation in a conserved residue of the antizyme-binding region, mutant is degraded as efficientlyas wild-type. Almost complete loss of activity. Mutation diminishes the formation of enzyme dimers
E138A/L139S
-
mutation prevents the degradation by the proteasome, complete loss of activity. Mutation diminishes the formation of enzyme dimers
K115A
-
mutation in a conserved residue of the antizyme-binding region. About 30 of wild-type activity. Mutation diminishes the formation of enzyme dimers
K115A/K141A
-
degradation by the proteasome occurs with similar efficiency as for wild-type. About 10% of wild-type activity. Mutation diminishes the formation of enzyme dimers
K141A
-
mutation in a conserved residue of the antizyme-binding region. About 25% of wild-type activity
K69A
-
mutant enzyme K69A shows a changed spectrum and a 550fold decrease in the turnover/Km value
L139A
-
mutation in a conserved residue of the antizyme-binding region, mutant is resistant to degradation. About 15% of wild-type activity. Mutation diminishes the formation of enzyme dimers
L139S
-
mutation in a conserved residue of the antizyme-binding region, mutant is resistant to degradation. Almost complete loss of activity
additional information
A457W
site-directed mutagenesis, the mutation does not stabilize the enzyme
C441A
construction of a duplicated cODC, from fusing ODC to a tandem cODC-cODCC441A at its C-terminus, with the first ODC copy being wild-type including a wild-type Cys441, and the distal C-terminal copy of cODC carrying mutation C441A
C441A
site-directed mutagenesis, the mutation stabilizes the enzyme but also profoundly reduces its activity
S456A
site-directed mutagenesis, the mutation does not stabilize the enzyme
C360A
-
mutation C360A 26fold reduces the specificity constant and 2fold decreases the Km
C360A
-
mutant enzyme C360A is completely resistant to inactivation by (R,R)-delta-methyl-alpha-acetylenicputrescine and is much less sensitive than the wild type enzyme to alpha-monofluoromethyldehydromethylornithine
additional information
construction of several truncated enzyme mutants, mutant protein stabilities, overview
additional information
-
construction of several truncated enzyme mutants, mutant protein stabilities, overview
additional information
construction of myeloid-specific Odc deletion mutant mice (OdcDELTAmye). Increased mRNA expression of Nos2, Tnfa, Il1b, Il12a, Ccl5 and Cxcl10 is demonstrated in dextran sulfate sodium-treated OdcDELTAmye versus Odcfl/fl mice, while expression levels of the M2 markers, Arg1 and Chil3, are comparable in colonic tissues of dextran sulfate sodium-treated Odcfl/fl and OdcDELTAmye mice. OdcDELTAmye mice are protected from colitis-associated carcinogenesis
additional information
in ODC-ER transgenic mice, in which an involucrin promoter directs the expression of the inducible ODC cDNA fused in frame to a 4-hydroxytamoxifen (4OHT)-responsive mutant estrogen receptor ligand binding domain to the suprabasal epidermis, elevated expression of ornithine decarboxylase (ODC), the regulatory enzyme in polyamine biosynthesis, targeted to the epidermis is sufficient to promote skin tumor development following a single subthreshold dose of dimethylbenz(a)anthracene (DMBA). ODC-ER transgenic mice and their normal littermates have been backcrossed into either the FVB or C57Bl/6 background for at least 10 generations. An inducible Cre-activated bi-transgenic mouse system is used to track hair follicle bulge stem cells and their progeny. K15-CrePR1 transgenic mice, that express CrePR1 under the control of a keratin 15 (K15) promoter, are generated to target expression of genes to the adult epidermal stem cells located in the hair follicle bulge cells. K15-CrePR1 transgenic mice are crossed with Cre-responsive R26R transgenic mice, that express lacZ under the control of a ubiquitous promoter, after Cre-mediated removal of an inactivating sequence. The resulting K15-CrePR1-R26R bitransgenic mice are treated topically with RU486 to induce expression of lacZ in the bulge stem cells of the skin. Polyamine oxidase inhibitor MDL72527 is applied. MDL72527 treatment increases skin tumor growth and conversion to carcinomas in DMBA-initiated ODC-ER mice, overview
additional information
-
in ODC-ER transgenic mice, in which an involucrin promoter directs the expression of the inducible ODC cDNA fused in frame to a 4-hydroxytamoxifen (4OHT)-responsive mutant estrogen receptor ligand binding domain to the suprabasal epidermis, elevated expression of ornithine decarboxylase (ODC), the regulatory enzyme in polyamine biosynthesis, targeted to the epidermis is sufficient to promote skin tumor development following a single subthreshold dose of dimethylbenz(a)anthracene (DMBA). ODC-ER transgenic mice and their normal littermates have been backcrossed into either the FVB or C57Bl/6 background for at least 10 generations. An inducible Cre-activated bi-transgenic mouse system is used to track hair follicle bulge stem cells and their progeny. K15-CrePR1 transgenic mice, that express CrePR1 under the control of a keratin 15 (K15) promoter, are generated to target expression of genes to the adult epidermal stem cells located in the hair follicle bulge cells. K15-CrePR1 transgenic mice are crossed with Cre-responsive R26R transgenic mice, that express lacZ under the control of a ubiquitous promoter, after Cre-mediated removal of an inactivating sequence. The resulting K15-CrePR1-R26R bitransgenic mice are treated topically with RU486 to induce expression of lacZ in the bulge stem cells of the skin. Polyamine oxidase inhibitor MDL72527 is applied. MDL72527 treatment increases skin tumor growth and conversion to carcinomas in DMBA-initiated ODC-ER mice, overview
additional information
Odc knockdown in myeloid cells, generation of mutant mice with a myeloid-specific deletion of gene Odc, by crossing C57BL/6 Odcfl/fl mice with myeloid-specific LysMcre/cre driver mice, yielding the OdcDELTAmye mice
additional information
purified [35S]methionine-labeled recombinant His6-TEV (tobacco etch virus)-FLAG-ODC is generated and degraded in vitro
additional information
-
construction of enzyme overexpressing and enzyme-deficient transgenic mice, deletion of the 5 terminal residues 457-461 also stabilizes ODC but to a lesser extent than removing the terminal 37 residues or mutation of Cys441
additional information
-
transgenic mice overexpressing ODC in hair follicle keratinocytes using keratin promotors are much more sensitive than littermate controls to DMBA-induced carcinogenesis, and do not require treatment with a tumor promoter to develop tumors, overview
additional information
-
construction of ODC-overexpressing K6/ODC transgenic mice in which a keratin 6 promoter directs the expression of ODC to the outer root sheath cells of hair follicles in the skin. Although elevated levels of ODC and polyamines stimulate proliferation of keratinocytes, mutant Ker/ODC cells undergo apoptotic cell death within days of primary culture unlike wild-type Ker/Norm cells that continue to proliferate. Ker/ODC also displays increased generation of H2O2, acroleinlysine conjugates, and protein oxidation products as well as polyamine-dependent DNA damage, phenotype, overview
additional information
-
establishment of an embryonic stem cell clone with disrupted Azin1 gene by the gene trap technique, construction of a mutant mouse line using these trapped embryonic stem cells. Homozygous mutant mice die at P0 with abnormal liver morphology, deletion of Azin1 in homozygous mice results in the degradation of ODC, and reduced the biosynthesis of putrescine and spermidine, genotype and phenotype, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
mouse ODC is quickly degraded by the 26S proteasome in mammalian and fungal cells
ODC initiates the polyamine biosynthetic pathway, rapid turnover of ODC is brought about by the 26S proteasome, ubiquitination is not required for this degradation, antizyme increases the degradation of ODC by enhancing its interaction with the proteasome but does not increase the rate of proteasomal processing
-
the wild type form of ODC has an extremely short half life of 20-30 min, and its degradation is mediated by antizyme, which binds to the monomeric form of ODC, preventing formation of the enzymatically active homodimer, and then targets ODC for degradation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-40°C, 25 mM Tris-HCl, pH 7.5, 0.1 mM EDTA, 2.5 mM dithiothreitol, 0.02% Brij 35
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type an dmutant enzymes from Escherichia coli
enzyme occurs mainly in an inactivated form and is activated during purification
-
Q Sepharose column chromatography, HiTrap Q column chromatography, and Sephadex R75 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Odc1, site-directed mutated ODC is in vitro transcribed and translated in reticulocyte lysate, recombinant expression of His-tagged wild-type enzyme, point mutants, and mutant His6-TEV (tobacco etch virus)-FLAG-ODC construct in Escherichia coli
mutated ODC is in vitro transcribed and translated in reticulocyte lysate, expression of His-tagged ODC fused to the human dihydrofolate reductase, DHFR, in Escherichia coli
Myc plays a role in transcription of ODC, transcriptional regulation, overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
determination of Odc mRNA levels in CD11b+ myeloid cells and CD11b- nonmyeloid cells from the gastric lamina propria of mice infected with Helicobacter pylori premouse Sydney strain 1 (PMSS1) for 48 h. Odc is not induced in CD11b- cells or gastric epithelial cells, and Odc mRNA levels are not altered in these cells derived from the Odcfl/fl and OdcDELTAmye mice
ODC activity shows no significant alteration after exposure at an SAR of 2.5 W/kg for 1 h, no alteration of ODC activity is detected when L-929 cells are exposed to 217 Hz modulated GSM-900 MHz (wire-patch antenna) or GSM-1800 MHz (waveguides)
-
ODC induction occurs irrespective of the endospores' germination capabilities and is more prominent in macrophages exposed to Bacillus anthracis endospores lacking lethal toxin
-
Odc1 expression is decreased more than 60% in muscle from male muscle-specific androgen receptor knockout mice
-
ornithine decarboxylase is upregulated by the androgen receptor in skeletal muscle. Muscle of adult male mice expresses high levels of Odc1 compared with age-matched females and younger males. Dihydrotestosterone increases Odc1 levels 2.7 and 1.6fold in skeletal muscle cell myoblasts after 12 and 24 h of treatment, respectively
-
ornithine decarboxylase mRNA increases in the prostate upon administration of androgens
-
single topical application of argemone oil (0.05-0.4 ml/mouse) or sanguinarine alkaloid (0.0015-0.012 mM/mouse) affords significant increase in ornithine decarboxylase activity and protein expression, the maximum induction of ODC activity (335%) occurs at 4 h with argemone oil, which comes down to 56% after 8h exposure time. Sanguinarine alkaloid shows 213% and 233% induction of ODC activity after 2 and 4 h, respectively. Maximum induction of ODC activity (7fold) occurs at 4 h after application of 12-O-tetradecanoyl phorbol myristate acetate and by 8 h the activity returns to the control level
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
targeting both polyamine biosynthesis via ODC through 2-difluoromethylornithine and polyamine transport through MQT 1426 from the tumor microenvironment enhances the efficacy of polyamine-based therapy in this mouse model of squamous cell carcinoma, overview
medicine
-
after induction of regenerative hyperplasia or renal hypertrophy by administration of folates or testosterone resp., enzyme activity increases 80- to 1000fold in enzyme activity
pharmacology
-
the enzyme is a target in the combination therapy with 2-difluoromethylornithine and a polyamine transport inhibitor MQT 1426, i.e. D-Lys-spermine, against murine squamous cell carcinoma, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Katz, A.; Kahana, C.
Isolation and characterization of the mouse ornithine decarboxylase gene
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263
7604-7609
1988
Mus musculus
Kitani, T.; Fujisawa, H.
Molecular properties of ornithine decarboxylase from mouse kidney. Detailed comparison with those of the enzyme from rat liver
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103
547-553
1988
Mus musculus, Rattus norvegicus
O'Brien, T.G.; Madara, T.; Pyle, J.A.; Holmes, M.
Ornithine decarboxylase from mouse epidermis and epidermal papillomas: differences in enzymatic properties and structure
Proc. Natl. Acad. Sci. USA
83
9448-9452
1986
Mus musculus
Laitinen, P.H.; Hietala, O.A.; Pulkka, A.E.; Pajunen, A.E.I.
Purification of mouse brain ornithine decarboxylase reveals its presence as an inactive complex with antizyme
Biochem. J.
236
613-616
1986
Mus musculus
Seely, J.E.; Persson, L.; Sertich, G.J.; Pegg, A.E.
Comparison of ornithine decarboxylase from rat liver, rat hepatoma and mouse kidney
Biochem. J.
226
577-586
1985
Mus musculus, Rattus norvegicus
Seely, J.E.; Pegg, A.E.
Ornithine decarboxylase (mouse kidney)
Methods Enzymol.
94
158-161
1983
Mus musculus
Isomaa, V.V.; Pajunen, A.E.I.; Bardin, C.W.; Jaenne, O.A.
Ornithine decarboxylase in mouse kidney. Purification, characterization, and radioimmunological determination of the enzyme protein
J. Biol. Chem.
258
6735-6740
1983
Mus musculus
Poulin, R.; Lu, L.; Ackermann, B.; Bey, P.; Pegg, A.E.
Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by a alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites
J. Biol. Chem.
267
150-158
1992
Mus musculus
Coleman, C.S.; Stanley, B.A.; Pegg, A.E.
Effect of mutations at active site residues on the activity of ornithine decarboxylase and its inhibition by active site-directed irreversible inhibitors
J. Biol. Chem.
268
24572-24579
1993
Mus musculus
Baby, T.G.; Hayashi, S.
Hepatic ornithine decarboxylase from the frog, Rana negromaculata: dietary induction, purification and some properties
Comp. Biochem. Physiol. B
99
151-156
1991
Mus musculus, Pelophylax nigromaculatus
Fozard, J.R.; Part, M.L.
Methods for the study of the experimental interruption of pregnancy by ornithine decarboxylase inhibitors
Methods Enzymol.
94
213-216
1983
Mus musculus
Persson, L.; Rosengren, E.; Sundler, F.; Uddman, R.
Immunocytochemical localization of ornithine decarboxylase
Methods Enzymol.
94
166-169
1983
Mus musculus, Rattus norvegicus
Zagon, I.S.; Seely, J.E.; Pegg, A.E.
Autoradiographic localization of ornithine decarboxylase
Methods Enzymol.
94
169-176
1983
Mus musculus
Shantz, L.M.; Guo, Y.; Sawicki, J.A.; Pegg, A.E.; O'Brien, T.G.
Overexpression of a dominant-negative ornithine decarboxylase in mouse skin: effect on enzyme activity and papilloma formation
Carcinogenesis
23
657-664
2002
Mus musculus
Svechnikov, K.; Ritzen, E.M.; Holst, M.
Androgen and estrogen stimulation of ornithine decarboxylase activity in mouse kidney
J. Steroid Biochem. Mol. Biol.
75
329-333
2001
Mus musculus
Kern, A.D.; Oliveira, M.A.; Coffino, P.; Hackert, M.L.
Structure of mammalian ornithine decarboxylase at 1.6 A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases
Structure Fold. Des.
7
567-581
1999
Mus musculus
Shantz, L.M.
Transcriptional and translational control of ornithine decarboxylase during Ras transformation
Biochem. J.
377
257-264
2004
Mus musculus
Shon, Y.H.; Nam, K.S.
Inhibition of cytochrome P450 isozymes and ornithine decarboxylase activities by polysaccharides from soybeans fermented with Phellinus igniarius or Agrocybe cylindracea
Biotechnol. Lett.
26
159-163
2004
Mus musculus
Fogel, W.A.; Dudkowska, M.; Wagner, W.; Grzelakowska-Sztabert, B.; Manteuffel-Cymborowska, M.
Ornithine and histidine decarboxylase: Activities in hypertrophic and hyperplastic mouse kidney
Inflamm. Res.
54
S62-S63
2005
Mus musculus
-
Yamaguchi, Y.; Takatsuka, Y.; Matsufuji, S.; Murakami, Y.; Kamio, Y.
Characterization of a counterpart to mammalian ornithine decarboxylase antizyme in prokaryotes
J. Biol. Chem.
281
3995-4001
2005
Mus musculus
Bastida, C.M.; Cremades, A.; Castells, M.T.; Lopez-Contreras, A.J.; Lopez-Garcia, C.; Sanchez-Mas, J.; Penafiel, R.
Sexual dimorphism of ornithine decarboxylase in the mouse adrenal: influence of polyamine deprivation on catecholamine and corticoid levels
Am. J. Physiol. Endocrinol. Metab.
292
E1010-E1017
2007
Mus musculus (P00860), Mus musculus
Shantz, L.M.; Levin, V.A.
Regulation of ornithine decarboxylase during oncogenic transformation: mechanisms and therapeutic potential
Amino Acids
33
213-223
2007
Homo sapiens, Mus musculus, Rattus norvegicus
Chen, Y.; Weeks, R.S.; Burns, M.R.; Boorman, D.W.; Klein-Szanto, A.; OBrien, T.G.
Combination therapy with 2-difluoromethylornithine and a polyamine transport inhibitor against murine squamous cell carcinoma
Int. J. Cancer
118
2344-2349
2006
Mus musculus, Mus musculus FVB/N
Hoeytoe, A.; Juutilainen, J.; Naarala, J.
Ornithine decarboxylase activity is affected in primary astrocytes but not in secondary cell lines exposed to 872 MHz RF radiation
Int. J. Radiat. Biol.
83
367-374
2007
Homo sapiens, Mus musculus, Rattus norvegicus
Pegg, A.E.
Regulation of ornithine decarboxylase
J. Biol. Chem.
281
14529-14532
2006
Mus musculus
Takeuchi, J.; Chen, H.; Hoyt, M.A.; Coffino, P.
Structural elements of the ubiquitin-independent proteasome degron of ornithine decarboxylase
Biochem. J.
410
401-407
2008
Mus musculus (P00860), Mus musculus
Snapir, Z.; Keren-Paz, A.; Bercovich, Z.; Kahana, C.
ODCp, a brain- and testis-specific ornithine decarboxylase paralogue, functions as an antizyme inhibitor, although less efficiently than AzI1
Biochem. J.
410
613-619
2008
Homo sapiens, Mus musculus
Wei, G.; DeFeo, K.; Hayes, C.S.; Woster, P.M.; Mandik-Nayak, L.; Gilmour, S.K.
Elevated ornithine decarboxylase levels activate ataxia telangiectasia mutated-DNA damage signaling in normal keratinocytes
Cancer Res.
68
2214-2222
2008
Mus musculus
Tang, H.; Ariki, K.; Ohkido, M.; Murakami, Y.; Matsufuji, S.; Li, Z.; Yamamura, K.
Role of ornithine decarboxylase antizyme inhibitor in vivo
Genes Cells
14
79-87
2009
Mus musculus
Hoeytoe, A.; Sokura, M.; Juutilainen, J.; Naarala, J.
Radiofrequency radiation does not significantly affect ornithine decarboxylase activity, proliferation, or caspase-3 activity of fibroblasts in different physiological conditions
Int. J. Radiat. Biol.
84
727-733
2008
Mus musculus
Park, J.H.; Lee, C.K.; Hwang, Y.S.; Park, K.K.; Chung, W.Y.
Hemin inhibits cyclooxygenase-2 expression through nuclear factor-kappa B activation and ornithine decarboxylase expression in 12-O-tetradecanoylphorbol-13-acetate-treated mouse skin
Mutat. Res.
642
68-73
2008
Mus musculus
Ivanov, I.P.; Loughran, G.; Atkins, J.F.
uORFs with unusual translational start codons autoregulate expression of eukaryotic ornithine decarboxylase homologs
Proc. Natl. Acad. Sci. USA
105
10079-10084
2008
Mus musculus
Bera, S.; Wallimann, T.; Ray, S.; Ray, M.
Enzymes of creatine biosynthesis, arginine and methionine metabolism in normal and malignant cells
FEBS J.
275
5899-5909
2008
Mus musculus
Porasuphatana, S.; Cao, G.L.; Tsai, P.; Tavakkoli, F.; Huwar, T.; Baillie, L.; Cross, A.S.; Shapiro, P.; Rosen, G.M.
Bacillus anthracis endospores regulate ornithine decarboxylase and inducible nitric oxide synthase through ERK1/2 and p38 mitogen-activated protein kinases
Curr. Microbiol.
61
567-573
2010
Mus musculus
Ansari, K.M.; Das, M.
Skin tumor promotion by argemone oil/alkaloid in mice: evidence for enhanced cell proliferation, ornithine decarboxylase, cyclooxygenase-2 and activation of MAPK/NF-kappaB pathway
Food Chem. Toxicol.
48
132-138
2010
Mus musculus
Billaudel, B.; Taxile, M.; Ruffie, G.; Veyret, B.; Lagroye, I.
Effects of exposure to DAMPS and GSM signals on ornithine decarboxylase (ODC) activity: I. L-929 mouse fibroblasts
Int. J. Radiat. Biol.
85
510-518
2009
Mus musculus
Cohavi, O.; Tobi, D.; Schreiber, G.
Docking of antizyme to ornithine decarboxylase and antizyme inhibitor using experimental mutant and double-mutant cycle data
J. Mol. Biol.
390
503-515
2009
Mus musculus
Ivanov, I.P.; Firth, A.E.; Atkins, J.F.
Recurrent emergence of catalytically inactive ornithine decarboxylase homologous forms that likely have regulatory function
J. Mol. Evol.
70
289-302
2010
Aedes aegypti, Ancylostoma ceylanicum, Anopheles gambiae, Aspergillus clavatus, Aspergillus fischeri, Aspergillus fumigatus, Aspergillus terreus, Bos taurus, Botrytis cinerea, Branchiostoma floridae, Caenorhabditis briggsae, Caenorhabditis elegans, Meyerozyma guilliermondii, Canis lupus familiaris, Gallus gallus, Ciona intestinalis, Coccidioides immitis, Culex pipiens, Dictyostelium discoideum, Drosophila melanogaster, Fusarium oxysporum, Fusarium verticillioides, Homo sapiens, Hydra vulgaris, Mus musculus, Neurospora crassa, Rattus norvegicus, Takifugu rubripes, Trypanosoma brucei, Xenopus laevis, Petromyzon marinus, Parastagonospora nodorum, Uncinocarpus reesii, Tetraodon nigroviridis, Dugesia japonica, Gasterosteus aculeatus, Anolis carolinensis, Schmidtea mediterranea, Nasonia vitripennis
Tokuhiro, K.; Isotani, A.; Yokota, S.; Yano, Y.; Oshio, S.; Hirose, M.; Wada, M.; Fujita, K.; Ogawa, Y.; Okabe, M.; Nishimune, Y.; Tanaka, H.
OAZ-t/OAZ3 is essential for rigid connection of sperm tails to heads in mouse
PLoS Genet.
5
e1000712
2009
Mus musculus
Singh, A.; Nirala, N.; Das, S.; Narula, A.; Rajam, M.; Srivastava, P.
Overexpression of odc (ornithine decarboxylase) in Datura innoxia enhances the yield of scopolamine
Acta Physiol. Plant.
2011
1-7
2011
Mus musculus
-
Lee, N.K.; Skinner, J.P.; Zajac, J.D.; MacLean, H.E.
Ornithine decarboxylase is upregulated by the androgen receptor in skeletal muscle and regulates myoblast proliferation
Am. J. Physiol. Endocrinol. Metab.
301
E172-E179
2011
Mus musculus
Giordano, E.; Hillary, R.A.; Vary, T.C.; Pegg, A.E.; Sumner, A.D.; Caldarera, C.M.; Zhang, X.Q.; Song, J.; Wang, J.; Cheung, J.Y.; Shantz, L.M.
Overexpression of ornithine decarboxylase decreases ventricular systolic function during induction of cardiac hypertrophy
Amino Acids
42
507-518
2012
Mus musculus
Kucharzewska, P.; Welch, J.E.; Svensson, K.J.; Belting, M.
Ornithine decarboxylase and extracellular polyamines regulate microvascular sprouting and actin cytoskeleton dynamics in endothelial cells
Exp. Cell Res.
316
2683-2691
2010
Homo sapiens, Mus musculus
Ramos-Molina, B.; Lambertos, A.; Lopez-Contreras, A.J.; Penafiel, R.
Mutational analysis of the antizyme-binding element reveals critical residues for the function of ornithine decarboxylase
Biochim. Biophys. Acta
1830
5157-5165
2013
Mus musculus
Hayes, C.; DeFeo-Mattox, K.; Woster, P.; Gilmour, S.
Elevated ornithine decarboxylase activity promotes skin tumorigenesis by stimulating the recruitment of bulge stem cells but not via toxic polyamine catabolic metabolites
Amino Acids
46
543-552
2014
Mus musculus (P00860), Mus musculus, Mus musculus C57BL/6 (P00860)
Takeuchi, J.; Chen, H.; Hoyt, M.A.; Coffino, P.
Structural elements of the ubiquitin-independent proteasome degron of ornithine decarboxylase
Biochem. J.
410
401-407
2008
Mus musculus (P00860)
Singh, K.; Coburn, L.A.; Asim, M.; Barry, D.P.; Allaman, M.M.; Shi, C.; Washington, M.K.; Luis, P.B.; Schneider, C.; Delgado, A.G.; Piazuelo, M.B.; Cleveland, J.L.; Gobert, A.P.; Wilson, K.T.
Ornithine decarboxylase in macrophages exacerbates colitis and promotes colitis-associated colon carcinogenesis by impairing M1 immune responses
Cancer Res.
78
4303-4315
2018
Mus musculus (P00860), Homo sapiens (P11926), Homo sapiens
Chen, Y.; Weeks, R.S.; Burns, M.R.; Boorman, D.W.; Klein-Szanto, A.; O'Brien, T.G.
Combination therapy with 2-difluoromethylornithine and a polyamine transport inhibitor against murine squamous cell carcinoma
Int. J. Cancer
118
2344-2349
2006
Mus musculus (P00860), Mus musculus C57BL/6J (P00860)
-
Gamat, M.; Malinowski, R.L.; Parkhurst, L.J.; Steinke, L.M.; Marker, P.C.
Ornithine decarboxylase activity is required for prostatic budding in the developing mouse prostate
PLoS ONE
10
e0139522
2015
Mus musculus, Mus musculus C57/BL6
Hardbower, D.M.; Asim, M.; Luis, P.B.; Singh, K.; Barry, D.P.; Yang, C.; Steeves, M.A.; Cleveland, J.L.; Schneider, C.; Piazuelo, M.B.; Gobert, A.P.; Wilson, K.T.
Ornithine decarboxylase regulates M1 macrophage activation and mucosal inflammation via histone modifications
Proc. Natl. Acad. Sci. USA
114
E751-E760
2017
Mus musculus (P00860)
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