Information on EC 4.1.1.17 - ornithine decarboxylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
4.1.1.17
-
RECOMMENDED NAME
GeneOntology No.
ornithine decarboxylase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-ornithine = putrescine + CO2
show the reaction diagram
-
-
-
-
L-ornithine = putrescine + CO2
show the reaction diagram
mechanism, reaction proceeds via formation of a Schiff base intermediate
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
decarboxylation
-
-
decarboxylation
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
putrescine biosynthesis III
-
-
putrescine biosynthesis IV
-
-
superpathway of ornithine degradation
-
-
polyamine pathway
-
-
Arginine and proline metabolism
-
-
Glutathione metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
L-ornithine carboxy-lyase (putrescine-forming)
A pyridoxal-phosphate protein.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
AdoMetDC/ODC
-
-
bODC
-
-
-
-
Decarboxylase, ornithine
-
-
-
-
dODC
-
degradative ornithine decarboxylase
lysine/ornithine decarboxylase
-
-
ODC
-
-
-
-
ODC
Entamoeba histolytica HM 1:IMSS
-
-
-
ODC
Lactobacillus gasseri DSM 20243
Q040G7
-
-
ODC
Leishmania donovani LdBob
-
-
-
ODC
Mus musculus K6/ODC
-
-
-
ODC
Phytomonas sp. Jma, Phytomonas sp. T274
-
-
-
ODC
Serratia liquefaciens IFI65
-
-
ODC
-
-
ODC-paralogue
-
-
-
-
ornithine decarboxylase
-
-
ornithine decarboxylase
-
-
ornithine decarboxylase
-
-
ornithine decarboxylase
-
-
ornithine decarboxylase
-
-
ornithine decarboxylase
Thalassobius aestuarii JC2049
-
-
-
PfAdoMetDC-ODC
-
-
PfODC/AdoMetDC
-
-
S-adenosylmethionine decarboxylase/ornithine decarboxylase
-
-
XODC1
-
-
-
-
XODC2
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-60-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
an endosymbiont-containing trypanosomatid
-
-
Manually annotated by BRENDA team
cultivar Columbia, Landsberg erecta
-
-
Manually annotated by BRENDA team
exogenous polyamines spermine, spermidine or putrescine lead to decrease in enzyme activity due to decrease in enzyme synthesis
-
-
Manually annotated by BRENDA team
up to 4fold increase in activity after beginning of growth period
Swissprot
Manually annotated by BRENDA team
strain HM-1:IMSS
-
-
Manually annotated by BRENDA team
strain HM-1:IMSS clone 6
UniProt
Manually annotated by BRENDA team
strain HM1: IMSS
-
-
Manually annotated by BRENDA team
Entamoeba histolytica HM 1:IMSS
strain HM1: IMSS
-
-
Manually annotated by BRENDA team
gene odc
-
-
Manually annotated by BRENDA team
patients suffering from Helicobacter pylori-infected gastritis
-
-
Manually annotated by BRENDA team
patients with chronic superficial gastritis, chronic atrophic gastritis with and without intestinal metaplasia, gastric dysplasia, and gastric cancer
-
-
Manually annotated by BRENDA team
patients with colorectal adenoma and adenocarcinoma
-
-
Manually annotated by BRENDA team
-
Q040G7
UniProt
Manually annotated by BRENDA team
Lactobacillus gasseri DSM 20243
-
Q040G7
UniProt
Manually annotated by BRENDA team
Lactobacillus saerimneri 30a ATCC 33222
-
UniProt
Manually annotated by BRENDA team
a trypanosomatid parasite causing visceral leishmaniasis, constitutive enzyme
-
-
Manually annotated by BRENDA team
strain LdBob
-
-
Manually annotated by BRENDA team
Leishmania donovani LdBob
strain LdBob
-
-
Manually annotated by BRENDA team
a trypanosomatid parasite causing cutaneous leishmaniasis, constitutive enzyme
-
-
Manually annotated by BRENDA team
low expression level of enzyme
Swissprot
Manually annotated by BRENDA team
two isozymes encoded by genes speC and speF
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
female ICR mice
-
-
Manually annotated by BRENDA team
K6/ODC mice
-
-
Manually annotated by BRENDA team
Ker/Norm wild-type mice and K6/ODC transgenic mice
-
-
Manually annotated by BRENDA team
MEK mutant K14-MEK mice
-
-
Manually annotated by BRENDA team
ODC1; Swiss CD1 mice
SwissProt
Manually annotated by BRENDA team
wild type and mutant enzymes C360A, K69A and C70S
-
-
Manually annotated by BRENDA team
Mus musculus K6/ODC
K6/ODC mice
-
-
Manually annotated by BRENDA team
cv. Wisconsin 38
-
-
Manually annotated by BRENDA team
no activity in Loktanella hongkongensis
-
-
-
Manually annotated by BRENDA team
no activity in Marinovum algicola
-
-
-
Manually annotated by BRENDA team
no activity in Marinovum algicola ATCC 51442
-
-
-
Manually annotated by BRENDA team
no activity in Phaeobacter gallaeciensis BS107
-
-
-
Manually annotated by BRENDA team
no activity in Raoultella ornithinolytica
-
-
-
Manually annotated by BRENDA team
no activity in Thalassobius mediterraneus
-
-
-
Manually annotated by BRENDA team
no activity in Thalassobius mediterraneus XSM19
-
-
-
Manually annotated by BRENDA team
no activity in Thalassococcus halodurans
-
-
-
Manually annotated by BRENDA team
no activity in Thalassococcus halodurans UST050418-052
-
-
-
Manually annotated by BRENDA team
Oenococcus oeni IOEB 89006
-
UniProt
Manually annotated by BRENDA team
subline M3C
-
-
Manually annotated by BRENDA team
strain Jma
-
-
Manually annotated by BRENDA team
strain T274
-
-
Manually annotated by BRENDA team
Phytomonas sp. Jma
strain Jma
-
-
Manually annotated by BRENDA team
Phytomonas sp. T274
strain T274
-
-
Manually annotated by BRENDA team
bifunctional S-adenosylmethionine decarboxylase/ornithine decarboxylase
SwissProt
Manually annotated by BRENDA team
strain FCR 3TC
-
-
Manually annotated by BRENDA team
Plasmodium falciparum FCR 3TC
strain FCR 3TC
-
-
Manually annotated by BRENDA team
Pseudomonas syringae pv. phaseolicola
-
-
-
Manually annotated by BRENDA team
diverse strains, overview
-
-
Manually annotated by BRENDA team
estrogenized female rats and castrated male and female rats
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
wild-type strain BY4741
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae WDHT668
-
-
-
Manually annotated by BRENDA team
strain IFI65, isolated from a spoiled Spanish dry-cured ham, gene speF
SwissProt
Manually annotated by BRENDA team
Serratia liquefaciens IFI65
strain IFI65, isolated from a spoiled Spanish dry-cured ham, gene speF
SwissProt
Manually annotated by BRENDA team
strain B006, ATCC PTA-7961
-
-
Manually annotated by BRENDA team
Staphylococcus pseudolugdunensis B006
strain B006, ATCC PTA-7961
-
-
Manually annotated by BRENDA team
Thalassobius aestuarii JC2049
JC2049
-
-
Manually annotated by BRENDA team
ssp. gambiense causing the West African form of sleeping sickness
-
-
Manually annotated by BRENDA team
a trypanosomatid causing Chagas disease, constitutive enzyme
-
-
Manually annotated by BRENDA team
ground squirrel
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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. ODC inhibition in endothelial cells results in increased Cdc42 activation
malfunction
-
ODC inhibition is associated with an abnormal morphology of the actin cytoskeleton during cell spreading and migration
metabolism
-
ornithine decarboxylase is the rate-limiting enzyme of polyamine synthesis
metabolism
-
ODC is the rate-limiting enzyme in polyamine biosynthesis
physiological function
-
ornithine decarboxylase regulates the activity and localization of rhoA via polyamination, ODC activity is needed for the maintenance of rhoA at the plasma membrane
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 ex vivo as well as the migration of primary human endothelial cells
physiological function
-
unperturbed ODC activity is a requirement for proper microvessel sprouting
physiological function
ornithine decarboxylase from Lactobacillus brevis is coupled to an ornithine/putrescine transmembrane exchanger. Their combined activities results in the extracellular release of putrescine
physiological function
ornithine decarboxylase system of Lacobacillus casei is composed of a decarboxylase active on ornithine and L-2,4-diaminobutyric acid and a transporter that mediates unidirectional transport of ornithine into the cytoplasm
physiological function
Q040G7
ornithine decarboxylase system of Lacobacillus gasseri is composed of a decarboxylase active on ornithine and L-2,4-diaminobutyric acid and a transporter that mediates unidirectional transport of ornithine into the cytoplasm
physiological function
ornithine decarboxylase from Oenococcus oeni is coupled to an ornithine/putrescine transmembrane exchanger. Their combined activities results in the extracellular release of putrescine
physiological function
-
ornithine decarboxylase and antizyme protein form a complex with 1:1 stoichiometry. Antizyme inhibits ornithine decarboxylase and faclilitates its degradation. The association constant is 6000000 per M. Circular dichroism spectra show a change in the secondary structure of the proteins in the complex
physiological function
Lactobacillus saerimneri 30a contains a three-component decarboxylation system consisting of ornithin decarboxylase, lysine decarboxylase and a transporter catalyzing both lysine/cadaverine and ornithine/putrescine exchange
physiological function
-
ornithine decarboxylase and sepiapterin reductase physically interact. The resulting heterocomplex is a compact structure, featuring two energetically and structurally equivalent binding modes both in monomer and in dimer conformations. siRNA-mediated knockdown of sepiapterin reductase expression significantly reduces endogenous ornithine decarboxylase enzyme activity in neuroblastoma cells
physiological function
enzyme can complement ornithine decarboxylase mutant in Saccharomyces cerevisiae
physiological function
-
ornithine decarboxylase system of Lacobacillus casei is composed of a decarboxylase active on ornithine and L-2,4-diaminobutyric acid and a transporter that mediates unidirectional transport of ornithine into the cytoplasm
-
physiological function
Lactobacillus gasseri DSM 20243
-
ornithine decarboxylase system of Lacobacillus gasseri is composed of a decarboxylase active on ornithine and L-2,4-diaminobutyric acid and a transporter that mediates unidirectional transport of ornithine into the cytoplasm
-
physiological function
Lactobacillus saerimneri 30a ATCC 33222
-
Lactobacillus saerimneri 30a contains a three-component decarboxylation system consisting of ornithin decarboxylase, lysine decarboxylase and a transporter catalyzing both lysine/cadaverine and ornithine/putrescine exchange
-
physiological function
Oenococcus oeni IOEB 89006
-
ornithine decarboxylase from Oenococcus oeni is coupled to an ornithine/putrescine transmembrane exchanger. Their combined activities results in the extracellular release of putrescine
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5alpha-dihydrotestosterone
?
show the reaction diagram
-
administration of 0.1 mM to the heart elicits a significant increase in ornithine decarboxylase activity in the left atrium of control male rats, that tends to decrease in gonadectomized rats, the effect is significant for female rats. Testosterone plasma levels positively correlate with the gradient of modifications of ornithine decarboxylase activity elicited by 5alpha-dihydrotestosterone exposure
-
-
?
alpha-methylornithine
2-methyl-1-pyrroline + NH3
show the reaction diagram
-
-
-
?
Arg
1-Amino-4-guanidinobutane
show the reaction diagram
-
0.1% of the activity with L-Orn
-
-
D-ornithine
putrescine + CO2
show the reaction diagram
-
very weak activity
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
show the reaction diagram
-
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
show the reaction diagram
-
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
show the reaction diagram
-
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
show the reaction diagram
Lactobacillus gasseri, Lactobacillus gasseri DSM 20243
Q040G7
-
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
show the reaction diagram
-
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
show the reaction diagram
Oenococcus oeni IOEB 89006
-
-
?
L-2,4-Diaminobutyrate
1,3-Diaminopropane + CO2
show the reaction diagram
-
2% of the activity with L-Orn
-
-
L-Lys
1,5-diaminopentane + CO2
show the reaction diagram
-
-
-
-
L-Lys
1,5-diaminopentane + CO2
show the reaction diagram
-
at 1.0% of the activity with Orn
-
-
L-Lys
1,5-diaminopentane + CO2
show the reaction diagram
-
2% of the activity with L-Orn
-
-
L-lysine
1,5-diaminopentane + CO2
show the reaction diagram
-
-
?
L-lysine
1,5-diaminopentane + CO2
show the reaction diagram
-
-
?
L-lysine
1,5-diaminopentane + CO2
show the reaction diagram
-
-
?
L-lysine
1,5-diaminopentane + CO2
show the reaction diagram
very low activity
-
?
L-lysine
1,5-diaminopentane + CO2
show the reaction diagram
Lactobacillus gasseri, Lactobacillus gasseri DSM 20243
Q040G7
very low activity
-
?
L-lysine
1,5-diaminopentane + CO2
show the reaction diagram
very low activity
-
?
L-lysine
1,5-diaminopentane + CO2
show the reaction diagram
Oenococcus oeni IOEB 89006
-
-
?
L-lysine
cadaverine + CO2
show the reaction diagram
-
-
?
L-lysine
cadaverine + CO2
show the reaction diagram
-
L-lysine is a poor substrate for ODC, with a Km approximately 100fold higher than that of L-ornithine
-
?
L-lysine
cadaverine + CO2
show the reaction diagram
Lactobacillus saerimneri 30a ATCC 33222
-
-
?
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
L-Orn
Putrescine + CO2
show the reaction diagram
Plasmodium falciparum FCR 3TC
-
-
-
-
L-Orn
?
show the reaction diagram
-
key enzyme in polyamine metabolism
-
-
-
L-Orn
?
show the reaction diagram
-
key enzyme in polyamine metabolism
-
-
-
L-Orn
?
show the reaction diagram
-
key enzyme in polyamine metabolism
-
-
-
L-Orn
?
show the reaction diagram
-
key enzyme in polyamine metabolism
-
-
-
L-Orn
?
show the reaction diagram
-
key enzyme in polyamine metabolism
-
-
-
L-Orn
?
show the reaction diagram
primary regulatory enzyme in polyamine biosynthesis
-
-
-
L-Orn
?
show the reaction diagram
-
alteration in the key enzyme in the growth-associated pathway of polyamine biosynthesis may play a role in colon tumor progression
-
-
-
L-Orn
?
show the reaction diagram
-
induced in mammary gland of fasted lactating rats by administration of 1,3-diaminopropan-2-ol
-
-
-
L-Orn
?
show the reaction diagram
-
first step in polyamine biosynthesis
-
-
-
L-Orn
?
show the reaction diagram
-
highly regulated enzyme of the polyamine pathway
-
-
-
L-Orn
?
show the reaction diagram
Plasmodium falciparum FCR 3TC
-
key enzyme in polyamine metabolism
-
-
-
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Pseudomonas syringae pv. phaseolicola
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
-
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Q040G7
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
very low activity
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
bifunctional enzyme with ODC and S-adenosylmethionine decarboxylase activity, AdoMetDC component is located at the N-terminus and linked to ODC by approx. 180 amino acid residues
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC activity increases abruptly in growing callus entire cells after 8 h, no change of activity in chloroplast
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
altered nitric oxide synthase, arginase and ornithine decarboxylase activities, and polyamine synthesis in response to ischemia of the detrusor in the bladder, ischemia increases ODC activity, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
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
show the reaction diagram
-
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 regulation occurs at the levels of transcription, translation and protein degradation, 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
show the reaction diagram
-
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 regulation occurs at the levels of transcription, translation and protein degradation, mechanisms, e.g. via the Ras effector pathways, and therapeutic potential, overview, ODC induction as a necessary step in MEK-induced tumorigenesis, enzyme inhibition reduces tumor growth, synergistic or additive effects, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
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
show the reaction diagram
-
L-arginine reduces cell proliferation and ornithine decarboxylase activity in patients with colorectal adenoma and adenocarcinoma, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC activity is higher in endosymbiont-bearing trypanosomatids than in aposymbiotic cells, but isolated endosymbionts do not display this enzyme activity, expressed levels of ODC are similar in both strains, suggesting that ODC is positively modulated in endosymbiont-bearing cells, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is a key enzyme in the polyamine biosynthetic pathway, polyamines are substrates for the synthesis of trypanothione, which is essential for the protection of the parasite against reactive oxygen species produced by the host
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the first committed enzyme in the polyamine biosynthesis pathway
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the first-rate limiting enzyme in the polyamine biosynthesis pathway, ODC plays a critical role in cell proliferation, and it is implicated as an essential promoter in normal cell cycles, activation of ODC is related to tumor promotion and progression, overview, expression of ODC is increased in gastric atrophy
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the initial and rate-limiting enzyme in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
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
show the reaction diagram
-
the enzyme is involved in polyamine biosynthesis, polyamines participate in the cellular response to different structural classes of histone deacetylase inhibitors, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
the enzyme is involved in polyamine biosynthesis, the enzyme is increased in cancer cells
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
the enzyme is involved in putrescine biosynthesis, diurnal changes in enzyme activity and polyamine contents in leaves, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
the enzyme is involved in the polyamine pathway
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
Cys360 plays an essential role in ensuring correct protonation of the decarboxylated reaction intermediate at Calpha
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
rate-limiting enzyme in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
a key enzymes in polyamine synthesis, putrescin formation leads subsequently to spermidine and spermine
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
key enzyme of polyamine biosynthesis, essential role of the polyamines in cancer cell adaptation to hypoxic stress, effects of hypoxia on the polyamine system in cancer cells, overview. Compensatory up-regulation of polyamine transport on inhibition of ODC
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
key rate-limiting enzyme in polyamine biosynthesis, elevated levels of ODC and polyamines stimulate proliferation of keratinocytes
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is a key enzyme in mammalian polyamine biosynthesis that is up-regulated in various types of cancer
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
Odc is the first and rate-limiting enzyme of polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the first rate-limiting enzyme in the polyamine biosynthesis pathway
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the rate-limiting enzyme in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the rate-limiting enzyme in polyamine biosynthesis that decarboxylates ornithine to putrescine
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the rate-limiting enzyme in the cellular biosynthetic pathway to polyamines putrescine, spermidine and spermine. During mitotic cell cycle, ODC exhibits two activity peaks, one at G1/S transition and the second during G2/M transition, anti-apoptotic role for ornithine decarboxylase during oocyte maturation, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the rate-limiting enzyme of the polyamine biosynthetic pathway, and plays an important role in cell cycle, tumor promotion and anti-apoptosis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
ornithine decarboxylase, the first and rate-limiting enzyme in the polyamine biosynthetic pathway, is a highly regulated enzyme
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
rate-limiting enzyme in polyamine biosynthesis. ODC is an essential cellular determinant necessary for the viability and growth of both Leishmania donovani promastigotes and amastigotes
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
the organism responds to alleviate the detrimental effects of polyamine depletion via regulation of its transcriptome and subsequently the proteome and metabolome, AdoMetDC/ODC transcriptome, proteome and metabolome analysis, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
the wild-type enzyme's substrate binding site is mutated at three amino acids D332, D361, and Y323 leading to reduced substrate binding activity, computational modelling, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
the enzyme is speciic for L-ornithine
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Serratia liquefaciens IFI65
the enzyme is involved in the polyamine pathway
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Lactobacillus gasseri DSM 20243
Q040G7
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Saccharomyces cerevisiae WDHT668
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Phytomonas sp. Jma
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Lactobacillus saerimneri 30a ATCC 33222
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Mus musculus K6/ODC
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
very low activity
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Phytomonas sp. T274
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Leishmania donovani LdBob
-
rate-limiting enzyme in polyamine biosynthesis. ODC is an essential cellular determinant necessary for the viability and growth of both Leishmania donovani promastigotes and amastigotes
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Entamoeba histolytica HM 1:IMSS
-
-
-
?
ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Oenococcus oeni IOEB 89006
-
-
?
additional information
?
-
-
bifunctional enzyme having both ODC and AdoMetDC, i.e. EC4.1.1.50, activity
-
-
?
additional information
?
-
circadian variations in ODC activity in female and male mice, influence of sex hormones, overview
-
-
-
additional information
?
-
-
increasing ODC activity is another way of prolactin preventing methotrexate-induced apoptosis, this induction of ODC activity enhances the expression of Bcl-2 strongly enough to bring about the anti-apoptotic function, prolactin-induced ODC activity is not required to upregulate Bcl-2 early, but indispensable in enhancing it later, overview
-
-
-
additional information
?
-
-
ODC activity in tumor cell lines correlates with sensitivity to cell death induced by histone deacetylase inhibitors, polyamine depletion increases resistance to trichostatin A-induced cell death, but the G1 arrest in cell cycle is not sufficient, overview
-
-
-
additional information
?
-
-
ODC degradation is not triggered by ubiquitination, the polyamines induce the degradation of ODC by affecting the synthesis of antizyme
-
-
-
additional information
?
-
-
ODC degradation is not triggered by ubiquitination, the polyamines induce the degradation of ODC by affecting the synthesis of antizyme, Trypanosoma brucei replicates extracellularly in the bloodstream of the host and is thus dependent on endogenous polyamines
-
-
-
additional information
?
-
-
ODC is rapidly degraded in mammalian cells as well as in a rabbit reticulocyte lysate system, ODC contains degradation signals that are also functionally active in mammalian cells involving the 26 S proteasome, degradation involves the PEST sequence in the N-terminal extension, overview
-
-
-
additional information
?
-
-
the Raf/MEK/ERK pathway is involved in the regulation of ODC during skin tumorigenesis, overview
-
-
-
additional information
?
-
-
the Raf/MEK/ERK pathway is involved in the regulation of ODC during skin tumorigenesis, the Raf/MEK/ERK cascade mediates ODC transcription and the PI 3-kinase cascade mediates ODC translation, overview, a single nucleotide polymorphism occurs in intron 1 of the ODC gene, which results in increased ODC expression in response to Myc
-
-
-
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
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-
-
additional information
?
-
Crithidia fasciculata ODC, in contrast to other phylogentically related enzymes, is rapidly degraded also in mammalian systems, and it contains several sequence elements essential for the rapid turnover of the protein, these regions are mainly located in the central part of the enzyme, overview
-
-
-
additional information
?
-
-
curcumin-induced apoptosis occurs through a mechanism of down-regulating ODC and along a ROS-dependent mitochondria-mediated pathway
-
-
-
additional information
?
-
-
degradation of lysine/ornithine decarboxylase by ATP-requiring protease(s) is accelerated by the binding of P22, which is a ribosomal protein of this strain, binding and activity analysis of wild-type and mutant P22s, segments A and B in P22 are crucial for P22 binding to LDC/ODC, overview
-
-
-
additional information
?
-
-
during liver regeneration from 70% partial hepatectomy, ODC produces newly synthesized spermidine, the inhibition of Gln-Lys bond production by the preferential formation of protein-spermidine bonds leads to an increase in DNA synthesis. Gln-Lys bond formation is catalyzed by transglutaminase 2 as a post-translational modification of proteins
-
-
-
additional information
?
-
-
in Plasmodium falciparum the two rate-limiting enzymes of polyamine biosynthesis, ornithine decarboxylase, ODC, and S-adenosylmethionine decarboxylase, ADoMetDC EC 4.1.1.50, form a single bifunctional protein, AdoMetDC/ODC
-
-
-
additional information
?
-
Leishmania donovani ODC has a very fast turnover in mammalian cells, but is a stable enzyme
-
-
-
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
?
-
-
ODC degradation is catalyzed by the 26S proteasome without prior polyubiquitination
-
-
-
additional information
?
-
-
ODC inhibition by alpha-difluoromethylornithine, and following polyamine depletion, activates opposing signaling pathways via phosphorylation of both Akt/protein kinase B and p27Kip1 in neuroblastoma
-
-
-
additional information
?
-
-
ODC is degraded by the 26S proteasome after being ubiquinated, ODC degradation is greatly stimulated by its interaction with a polyamine-induced protein termed antizyme, interaction with antizyme stimulates ODC degradation due to a conformational change resulting in the exposure of it C-terminal proteasome recognition signal, overview
-
-
-
additional information
?
-
-
ODC is the first and rate limiting enzyme in the synthesis of polyamines, which are essential for normal cell growth, the induction of the enzyme by interleukines 4 and 13 is involved in upregulation of kinases ERK, PI3K, and PKA, and in cell proliferation, overview. Dexamethasone, ERK, MEK, and PI3K pathways are involved in the regulation of ODC, overview
-
-
-
additional information
?
-
-
ornithine decarboxylase attenuates leukemic chemotherapy drugs-induced cell apoptosis and arrest in human promyelocytic HL-60 cells. With higher ODC activity, cells are resistant to the cancer chemotherapeutic drugs-induced apoptosis and keep on the cell cycle rolling with the significant interference in G1/S arrest caused by VP-16 and G2/M arrest by TAX, overview
-
-
-
additional information
?
-
-
ornithine decarboxylase is a cancer related protein. ODC is the key enzyme in polyamine synthesis and a regulator of cell proliferation. In gastric mucosal inflammation, induced by NaHCO3 feeding, ODC expression and activity is increased correlated to enhanced cell proliferation, overview
-
-
-
additional information
?
-
-
ornithine decarboxylase, the rate-limiting enzyme of polyamine biosynthesis, is a tumor promoter, provokes cell proliferation, and inhibits cell death, it interferes with macrophage-like differentiation and matrix metalloproteinase-9 expression by tumor necrosis factor alpha via NF-kappaB, ODC can directly inhibit and attenuate NF-kappaB DNA binding and transcriptional activation, mechanism, 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
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-
-
additional information
?
-
-
the genes encoding the isozymes are involved in putrescine formation, which is an indicator of food process deterioration
-
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-
additional information
?
-
-
yeast antizyme mediates degradation of yeast ornithine decarboxylase by yeast but not by mammalian proteasome, overview
-
-
-
additional information
?
-
no activity using arginine and lysine as substrates
-
-
-
additional information
?
-
-
the enzyme shows ODC activity
-
-
-
additional information
?
-
no activity with D-ornithine
-
-
-
additional information
?
-
-
the Arabidopsis rpS15 polypeptide interacts specifically with plant ODC
-
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-
additional information
?
-
-
the enzyme cannot decarboxylate L-lysine
-
-
-
additional information
?
-
no substrate: L-arginine
-
-
-
additional information
?
-
no substrate: L-arginine
-
-
-
additional information
?
-
no substrate: L-arginine
-
-
-
additional information
?
-
Q040G7
no substrate: L-arginine
-
-
-
additional information
?
-
no substrates: 2,4-diaminobutanoate, arginine
-
-
-
additional information
?
-
no substrates: lysine, arginine
-
-
-
additional information
?
-
Lactobacillus gasseri DSM 20243
Q040G7
no substrate: L-arginine
-
-
-
additional information
?
-
Lactobacillus saerimneri 30a ATCC 33222
no substrates: 2,4-diaminobutanoate, arginine
-
-
-
additional information
?
-
no substrate: L-arginine
-
-
-
additional information
?
-
Staphylococcus pseudolugdunensis B006
-
the enzyme shows ODC activity
-
-
-
additional information
?
-
Oenococcus oeni IOEB 89006
no substrate: L-arginine
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5alpha-dihydrotestosterone
?
show the reaction diagram
-
administration of 0.1 mM to the heart elicits a significant increase in ornithine decarboxylase activity in the left atrium of control male rats, that tends to decrease in gonadectomized rats, the effect is significant for female rats. Testosterone plasma levels positively correlate with the gradient of modifications of ornithine decarboxylase activity elicited by 5alpha-dihydrotestosterone exposure
-
-
?
L-lysine
1,5-diaminopentane + CO2
show the reaction diagram
Q9FPK5
-
-
?
L-Orn
?
show the reaction diagram
-
key enzyme in polyamine metabolism
-
-
-
L-Orn
?
show the reaction diagram
-
key enzyme in polyamine metabolism
-
-
-
L-Orn
?
show the reaction diagram
-
key enzyme in polyamine metabolism
-
-
-
L-Orn
?
show the reaction diagram
-
key enzyme in polyamine metabolism
-
-
-
L-Orn
?
show the reaction diagram
-
key enzyme in polyamine metabolism
-
-
-
L-Orn
?
show the reaction diagram
O76203
primary regulatory enzyme in polyamine biosynthesis
-
-
-
L-Orn
?
show the reaction diagram
-
alteration in the key enzyme in the growth-associated pathway of polyamine biosynthesis may play a role in colon tumor progression
-
-
-
L-Orn
?
show the reaction diagram
-
induced in mammary gland of fasted lactating rats by administration of 1,3-diaminopropan-2-ol
-
-
-
L-Orn
?
show the reaction diagram
-
first step in polyamine biosynthesis
-
-
-
L-Orn
?
show the reaction diagram
-
highly regulated enzyme of the polyamine pathway
-
-
-
L-Orn
?
show the reaction diagram
Plasmodium falciparum FCR 3TC
-
key enzyme in polyamine metabolism
-
-
-
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
P07805
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Q9FPK5
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
P09057
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
C9W982
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
C7BBC1
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
P11926
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC activity increases abruptly in growing callus entire cells after 8 h, no change of activity in chloroplast
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
altered nitric oxide synthase, arginase and ornithine decarboxylase activities, and polyamine synthesis in response to ischemia of the detrusor in the bladder, ischemia increases ODC activity, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
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
show the reaction diagram
-
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 regulation occurs at the levels of transcription, translation and protein degradation, 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
show the reaction diagram
-
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 regulation occurs at the levels of transcription, translation and protein degradation, mechanisms, e.g. via the Ras effector pathways, and therapeutic potential, overview, ODC induction as a necessary step in MEK-induced tumorigenesis, enzyme inhibition reduces tumor growth, synergistic or additive effects, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
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
show the reaction diagram
-
L-arginine reduces cell proliferation and ornithine decarboxylase activity in patients with colorectal adenoma and adenocarcinoma, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC activity is higher in endosymbiont-bearing trypanosomatids than in aposymbiotic cells, but isolated endosymbionts do not display this enzyme activity, expressed levels of ODC are similar in both strains, suggesting that ODC is positively modulated in endosymbiont-bearing cells, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is a key enzyme in the polyamine biosynthetic pathway, polyamines are substrates for the synthesis of trypanothione, which is essential for the protection of the parasite against reactive oxygen species produced by the host
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the first committed enzyme in the polyamine biosynthesis pathway
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the first-rate limiting enzyme in the polyamine biosynthesis pathway, ODC plays a critical role in cell proliferation, and it is implicated as an essential promoter in normal cell cycles, activation of ODC is related to tumor promotion and progression, overview, expression of ODC is increased in gastric atrophy
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the initial and rate-limiting enzyme in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
P00860
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
show the reaction diagram
-
the enzyme is involved in polyamine biosynthesis, polyamines participate in the cellular response to different structural classes of histone deacetylase inhibitors, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
the enzyme is involved in polyamine biosynthesis, the enzyme is increased in cancer cells
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
the enzyme is involved in putrescine biosynthesis, diurnal changes in enzyme activity and polyamine contents in leaves, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
A4Q8H0
the enzyme is involved in the polyamine pathway
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
rate-limiting enzyme in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
a key enzymes in polyamine synthesis, putrescin formation leads subsequently to spermidine and spermine
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
key enzyme of polyamine biosynthesis, essential role of the polyamines in cancer cell adaptation to hypoxic stress, effects of hypoxia on the polyamine system in cancer cells, overview. Compensatory up-regulation of polyamine transport on inhibition of ODC
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
key rate-limiting enzyme in polyamine biosynthesis, elevated levels of ODC and polyamines stimulate proliferation of keratinocytes
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is a key enzyme in mammalian polyamine biosynthesis that is up-regulated in various types of cancer
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
Odc is the first and rate-limiting enzyme of polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the first rate-limiting enzyme in the polyamine biosynthesis pathway
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the rate-limiting enzyme in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the rate-limiting enzyme in polyamine biosynthesis that decarboxylates ornithine to putrescine
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the rate-limiting enzyme in the cellular biosynthetic pathway to polyamines putrescine, spermidine and spermine. During mitotic cell cycle, ODC exhibits two activity peaks, one at G1/S transition and the second during G2/M transition, anti-apoptotic role for ornithine decarboxylase during oocyte maturation, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
ODC is the rate-limiting enzyme of the polyamine biosynthetic pathway, and plays an important role in cell cycle, tumor promotion and anti-apoptosis
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Q58P26
ornithine decarboxylase, the first and rate-limiting enzyme in the polyamine biosynthetic pathway, is a highly regulated enzyme
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
rate-limiting enzyme in polyamine biosynthesis. ODC is an essential cellular determinant necessary for the viability and growth of both Leishmania donovani promastigotes and amastigotes
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
-
the organism responds to alleviate the detrimental effects of polyamine depletion via regulation of its transcriptome and subsequently the proteome and metabolome, AdoMetDC/ODC transcriptome, proteome and metabolome analysis, overview
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Serratia liquefaciens IFI65
A4Q8H0
the enzyme is involved in the polyamine pathway
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Mus musculus K6/ODC
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Phytomonas sp. T274
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Leishmania donovani LdBob
-
rate-limiting enzyme in polyamine biosynthesis. ODC is an essential cellular determinant necessary for the viability and growth of both Leishmania donovani promastigotes and amastigotes
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Entamoeba histolytica HM 1:IMSS
-
-
-
?
additional information
?
-
P00860
circadian variations in ODC activity in female and male mice, influence of sex hormones, overview
-
-
-
additional information
?
-
-
increasing ODC activity is another way of prolactin preventing methotrexate-induced apoptosis, this induction of ODC activity enhances the expression of Bcl-2 strongly enough to bring about the anti-apoptotic function, prolactin-induced ODC activity is not required to upregulate Bcl-2 early, but indispensable in enhancing it later, overview
-
-
-
additional information
?
-
-
ODC activity in tumor cell lines correlates with sensitivity to cell death induced by histone deacetylase inhibitors, polyamine depletion increases resistance to trichostatin A-induced cell death, but the G1 arrest in cell cycle is not sufficient, overview
-
-
-
additional information
?
-
-
ODC degradation is not triggered by ubiquitination, the polyamines induce the degradation of ODC by affecting the synthesis of antizyme
-
-
-
additional information
?
-
-
ODC degradation is not triggered by ubiquitination, the polyamines induce the degradation of ODC by affecting the synthesis of antizyme, Trypanosoma brucei replicates extracellularly in the bloodstream of the host and is thus dependent on endogenous polyamines
-
-
-
additional information
?
-
-
ODC is rapidly degraded in mammalian cells as well as in a rabbit reticulocyte lysate system, ODC contains degradation signals that are also functionally active in mammalian cells involving the 26 S proteasome, degradation involves the PEST sequence in the N-terminal extension, overview
-
-
-
additional information
?
-
-
the Raf/MEK/ERK pathway is involved in the regulation of ODC during skin tumorigenesis, overview
-
-
-
additional information
?
-
-
the Raf/MEK/ERK pathway is involved in the regulation of ODC during skin tumorigenesis, the Raf/MEK/ERK cascade mediates ODC transcription and the PI 3-kinase cascade mediates ODC translation, overview, a single nucleotide polymorphism occurs in intron 1 of the ODC gene, which results in increased ODC expression in response to Myc
-
-
-
additional information
?
-
P90517
Crithidia fasciculata ODC, in contrast to other phylogentically related enzymes, is rapidly degraded also in mammalian systems, and it contains several sequence elements essential for the rapid turnover of the protein, these regions are mainly located in the central part of the enzyme, overview
-
-
-
additional information
?
-
-
curcumin-induced apoptosis occurs through a mechanism of down-regulating ODC and along a ROS-dependent mitochondria-mediated pathway
-
-
-
additional information
?
-
-
degradation of lysine/ornithine decarboxylase by ATP-requiring protease(s) is accelerated by the binding of P22, which is a ribosomal protein of this strain, binding and activity analysis of wild-type and mutant P22s, segments A and B in P22 are crucial for P22 binding to LDC/ODC, overview
-
-
-
additional information
?
-
-
during liver regeneration from 70% partial hepatectomy, ODC produces newly synthesized spermidine, the inhibition of Gln-Lys bond production by the preferential formation of protein-spermidine bonds leads to an increase in DNA synthesis. Gln-Lys bond formation is catalyzed by transglutaminase 2 as a post-translational modification of proteins
-
-
-
additional information
?
-
-
in Plasmodium falciparum the two rate-limiting enzymes of polyamine biosynthesis, ornithine decarboxylase, ODC, and S-adenosylmethionine decarboxylase, ADoMetDC EC 4.1.1.50, form a single bifunctional protein, AdoMetDC/ODC
-
-
-
additional information
?
-
P27116
Leishmania donovani ODC has a very fast turnover in mammalian cells, but is a stable enzyme
-
-
-
additional information
?
-
P00860
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
?
-
-
ODC degradation is catalyzed by the 26S proteasome without prior polyubiquitination
-
-
-
additional information
?
-
-
ODC inhibition by alpha-difluoromethylornithine, and following polyamine depletion, activates opposing signaling pathways via phosphorylation of both Akt/protein kinase B and p27Kip1 in neuroblastoma
-
-
-
additional information
?
-
-
ODC is degraded by the 26S proteasome after being ubiquinated, ODC degradation is greatly stimulated by its interaction with a polyamine-induced protein termed antizyme, interaction with antizyme stimulates ODC degradation due to a conformational change resulting in the exposure of it C-terminal proteasome recognition signal, overview
-
-
-
additional information
?
-
-
ODC is the first and rate limiting enzyme in the synthesis of polyamines, which are essential for normal cell growth, the induction of the enzyme by interleukines 4 and 13 is involved in upregulation of kinases ERK, PI3K, and PKA, and in cell proliferation, overview. Dexamethasone, ERK, MEK, and PI3K pathways are involved in the regulation of ODC, overview
-
-
-
additional information
?
-
-
ornithine decarboxylase attenuates leukemic chemotherapy drugs-induced cell apoptosis and arrest in human promyelocytic HL-60 cells. With higher ODC activity, cells are resistant to the cancer chemotherapeutic drugs-induced apoptosis and keep on the cell cycle rolling with the significant interference in G1/S arrest caused by VP-16 and G2/M arrest by TAX, overview
-
-
-
additional information
?
-
-
ornithine decarboxylase is a cancer related protein. ODC is the key enzyme in polyamine synthesis and a regulator of cell proliferation. In gastric mucosal inflammation, induced by NaHCO3 feeding, ODC expression and activity is increased correlated to enhanced cell proliferation, overview
-
-
-
additional information
?
-
-
ornithine decarboxylase, the rate-limiting enzyme of polyamine biosynthesis, is a tumor promoter, provokes cell proliferation, and inhibits cell death, it interferes with macrophage-like differentiation and matrix metalloproteinase-9 expression by tumor necrosis factor alpha via NF-kappaB, ODC can directly inhibit and attenuate NF-kappaB DNA binding and transcriptional activation, mechanism, 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
-
-
-
additional information
?
-
-
the genes encoding the isozymes are involved in putrescine formation, which is an indicator of food process deterioration
-
-
-
additional information
?
-
-
yeast antizyme mediates degradation of yeast ornithine decarboxylase by yeast but not by mammalian proteasome, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
0.02 mM, stimulates by 20-25%, cofactor
pyridoxal 5'-phosphate
-
Km: 0.00016 mM
pyridoxal 5'-phosphate
-
Km: 0.0002 mM, enzyme from epidermis
pyridoxal 5'-phosphate
-
firmly bound to the native enzyme; Km: 0.00009 mM
pyridoxal 5'-phosphate
-
Km: 0.01 mM
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
0.0128 mM, enzyme form B; Km: 0.00005 mM, enzyme form A
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
cofactor; one molecule of pyridoxal 5'-phosphate binds to each protomeric subunit
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
bound to Lys69
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
Km: 0.00023 mM
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
absolutely required for activity
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
apparent Km-value in wild-type 150 nM, in mutant K294A 36 microM
pyridoxal 5'-phosphate
Pseudomonas syringae pv. phaseolicola
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
the PLP cofactor is bound in a Schiff base linkage to Lys69
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
bindig site structure, modelling
pyridoxal 5'-phosphate
-
required for maximum activity
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate
-
protein has conserved pyridoxal 5'-phosphate binding residues
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(-)-epigallocatechin-3-gallate
-
polyphenolic compound of green tea with putative anti-cancer activity
(2R)-2-amino-4-[(2-oxopropyl)amino]butanoic acid
-
-
(2R)-2-amino-5-[(2-oxopropyl)amino]pentanoic acid
-
-
(2S)-5-amino-2-hydrazinylpentanoic acid
-
-
(DL)-difluoromethylornithine
-
irreversible inactivation, 50% inhibition at 0.0075 mM D-difluoromethylornithine
1,3-Diaminopropane
-
-
1,3-Diaminopropane
-
10 mM, approx. 60% inhibition
1,4-Diamino-2-butanone
-
-
1,4-Diamino-2-butanone
-
5 mM, complete inhibition
1,4-Dimethylputrescine
-
none of the three isomers, meso, +, and - inhibits in vitro, but strongly inhibits in vivo in rats or in H-35 hepatoma cells
1-amino-oxy-3-aminopropane
-
i.e. APA, analysis of the mode of the inhibitor binding to the enzyme, no oxime formation between APA and pyridoxal 5'-phosphate, homology modelling, overview
1-amino-oxy-3-aminopropane
-
i.e. APA, analysis of the mode of the inhibitor binding to the enzyme, no oxime formation between APA and pyridoxal 5'-phosphate, determined from the human enzyme-inhibitor cyrstal structure analysis and homology modelling, overview
1-diethyl-2-hydroxy-2-nitroso-hydrazine
-
nitric oxide donor, inhibition via S-nitrosylation of Cys360 in the active site of ODC
1H-indol-3-yl(morpholin-4-yl)acetonitrile
-
-
2-(difluoromethyl)-L-ornithine
-
ODC suicide inhibitor, 5 mM alpha-difluromethylornithine reduces ODC activity by 45fold
2-(difluoromethyl)ornithine
complete inhibition
-
2-phenylethyl carbamimidothioate
-
-
3-(morpholin-4-ylmethyl)-1H-indole
-
-
4,4'-[pentane-1,5-diylbis(oxy)]dibenzenecarboximidamide
-
-
4-aminobutyrate
-
-
4-chloromercuribenzoate
-
0.01 mM, complete inhibition
4-chloromercuribenzoate
0.01 mM, 99% inhibition
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.001 mM, approx. 80% inhibition of ODC activity after 8 min
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.01 mM, 99% inhibition
5,5'-dithiobis(2-nitrobenzoic acid)
0.01 mM, 98% inhibition
5-Aminopentanoate
-
-
5-Hydrazino-ornithine
-
competitive
6-Aminohexanoate
-
-
agmatine
-
non-competitive
agmatine
-
1 mM, 77% inhibition
alexidine
-
-
alpha-difluoromethylornithine
-
-
alpha-difluoromethylornithine
-
2 mM, 98% inhibition of ODC activity
alpha-difluoromethylornithine
-
5-10 mM, 25% inhibition in pellet, approx. 15% inhibition in supernatant, 20 mM, 40% inhibition in both pellet ans supernatant
alpha-difluoromethylornithine
Pseudomonas syringae pv. phaseolicola
-
-
alpha-difluoromethylornithine
a suicide inhibitor of ODC
alpha-difluoromethylornithine
-
i.e. DFMO, irreversible inactivator, physiologic effects, e.g. causes arrest in G1 phase in neuroblastoma cells, the cytostatic effect is reversible by putrescine, overview, acts synergistically with SAM486A, MDL-73811, cisplatin, and 5-fluorouracil
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
-
i.e. DFMO, irreversible inactivator, antitumor action of ODC inhibition using DFMO, chemopreventive effects, DFMO provides significant protection against 7,12-dimethylbenz[a]-anthracene-induced mammary carcinogenesis, overview
alpha-difluoromethylornithine
-
irreversible inhibitor, a curative agent of West African sleeping sickness
alpha-difluoromethylornithine
-
irreversible inhibitor
alpha-difluoromethylornithine
-
an enzyme-activated irreversible inhibitor, effective sue to the slow turnover of the trypanosomatid enzyme
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-difluoromethylornithine
-
inhibition of ODC by alpha-difluoromethylornithine increases resistance to trichostatin A-induced cell death in HCT116 cells
alpha-difluoromethylornithine
-
irreversible inhibitor of ODC
alpha-difluoromethylornithine
-
specific ODC inhibitor
alpha-difluoromethylornithine
-
i.e. DFMO or eflornithine
alpha-difluoromethylornithine
-
i.e. DFMO, ODC inhibition by alpha-difluoromethylornithine activates opposing signaling pathways via phosphorylation of both Akt/protein kinase B and p27Kip1 in neuroblastoma, inhibition of ODC by DFMO promotes cell survival by inducing the phosphorylation of Akt/PKB at residue Ser473 and glycogen synthase kinase-3B at Ser9, DFMO also induces the phosphorylation of p27Kip1 at residues Ser10, involved in nuclear export, and Thr198, involved in protein stabilization, but not Thr187, involved in proteasomal degradation,inhibition mechanism, overview
alpha-difluoromethylornithine
-
DFMO, a Odc suicide inhibitor, selective anticancer effects of DFMO on mouse and human MYCN-amplified neuroblastoma, overview
alpha-difluoromethylornithine
-
a suicide inhibitor of ODC, inhibits growth of wild-type Leishmania donovani amastigotes and effectively cures macrophages of parasites, thereby preventing host cell destruction
alpha-difluoromethylornithine
-
-
alpha-difluoromethylornithine
-
an irreversible inhibitor of ODC, cannot recover MMP-9 activation following NF-kappaB inhibitor treatment in parental cells
alpha-difluoromethylornithine
-
a highly specific suicide inhibitor of ODC causing complete, irreversible inhibition
alpha-difluoromethylornithine
-
specific and irreversible ODC inhibitor, complete inhibition at 0.1 mM
alpha-difluoromethylornithine
-
specific inhibitor
alpha-difluoromethylornithine
-
irreversible and specific inhibitor of ODC
alpha-difluoromethylornithine
-
suicide inactivator of ODC
alpha-difluoromethylornithine
-
-
alpha-difluoromethylornithine
-
-
alpha-difluoroornithine
-
-
alpha-DL-difluoromethylornithine
-
the nuclear enzyme is slightly more sensitive than the cytosolic
alpha-DL-difluoromethylornithine
-
irreversibel
alpha-DL-difluoromethylornithine
-
irreversibel
alpha-DL-difluoromethylornithine
-
irreversibel
alpha-DL-difluoromethylornithine
-
irreversibel
alpha-DL-difluoromethylornithine
-
irreversibel
alpha-DL-difluoromethylornithine
-
irreversibel
alpha-DL-difluoromethylornithine
-
irreversibel; mechanism of irreversible inactivation
alpha-DL-difluoromethylornithine
-
-
alpha-DL-difluoromethylornithine
-
-
alpha-DL-difluoromethylornithine
-
-
alpha-DL-difluoromethylornithine
-
-
alpha-DL-difluoromethylornithine
-
experimental interruption of pregnancy in the mouse
alpha-DL-difluoromethylornithine
-
irreversibel
alpha-DL-difluoromethylornithine
-
a medically used, irreversible inhibitor of ODC
alpha-Methylornithine
-
reversible
alpha-Methylornithine
-
competitive
antizyme
-
non-competitive inhibitor protein isolated from Thermus thermophilus or Escherichia coli, almost complete inhibition at higer concentrations
-
antizyme
-
non-competitive inhibitor protein isolated from Thermus thermophilus
-
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
-
the ornithine decarboxylase paralogue antizyme inhibitor ODCp acts as a regulator of ODC activity and inhibits its proteasomal degradation. ODCp binds antizymes, AZs, with higher affinity than does ODC and releases active ODC from catalytically inactive ODC-AZ complexes, overview
-
antizyme
-
antizymes are small polyamine-induced proteins that function as feedback regulators of cellular polyamine homeostasis. They bind to transient ODC monomeric subunits, resulting in inhibition of ODC activity and targeting ODC to ubiquitin-independent proteasomal degradation, unlike antizyme 1 and antizyme 2, which efficiently inhibit ODC activity and stimulate its proteasomal degradation, antizyme 3 poorly inhibits ODC activity and fails to promote ODC degradation. Furthermore, Az3 actually stabilizes ODC, probably by protecting it from the effect of Az1, overview. Interaction with antizyme stimulates ODC degradation due to a conformational change resulting in the exposure of it C-terminal proteasome recognition signal, overview. Az2 and Az3 are cloned by RT-PCR using RNA isolated from mouse liver and testis respectively, and expressed in HEK-293 cells
-
antizyme
-
role of ornithine decarboxylase antizyme inhibitor in vivo, ODC antizyme inhibitor, AZI, regulates ODC activity in cell cultures
-
antizyme
-
yeast, determination of sequences that are important for inhibiting ODC activity and promoting ODC degradation, the yeast ODC is not affected by mammalian antizyme
-
antizyme
-
ODC antizyme, a polyamine-induced protein, binds ODC, serving to inhibit ODC activity and to promote proteasome-mediated ODC degradation
-
antizyme
-
-
-
antizyme
-
non-competitive protein inhibitor of ODC. Binding of antizyme to an ODC monomer subunit results in enzymatic inhibition, rapid ubiquitin-independent degradation of ODC by the 26S proteasome and recycling of antizyme
-
antizyme 1
-
ODC is regulated by specific inhibitors, antizymes which in turn are inhibited by antizyme inhibitors. ODC alone is not degraded in reticulocyte lysate, whereas in the presence of antizyme 1, the degradation occurs rapidly. When antizyme inhibitor or ODC paralogue is added to the mixture, the antizyme 1-induced degradation of ODC is prevented.
-
Ba2+
-
0.8 mM, 50% inhibition
benzene-1,3-diyldiethane-2,1-diyl dicarbamimidothioate
-
-
benzene-1,4-diyldimethanediyl dicarbamimidothioate
-
-
but-2-yne-1,4-diyl dicarbamimidothioate
-
-
butane-1,4-diyl dicarbamimidothioate
-
-
Butylamine
-
-
Ca2+
-
0.9 mM, 50% inhibition
cadaverine
-
-
cadaverine
-
1 mM, 46% inhibition
Carbamoyl phosphate
-
-
CGP52622A
-
3-amino-oxy-1-propanamine analog, 0.00006 mM, 50% inhibition of recombinant Pf-Hinge-ODC
CGP52622A
-
0.000064 mM, 50% inhibition
CGP54619A
-
3-amino-oxy-1-propanamine analog, 0.000025 mM, 50% inhibition of recombinant Pf-Hinge-ODC
-
Co2+
-
0.5 mM, 50% inhibition
CPG541169A
-
0.000025 mM, 50% inhibition
-
D-Orn
-
weak
D-ornithine
-
1.5 mM, 50% inhibition
difluoro-methyl-ornithine
-
-
DL-alpha-Difluoromethylarginine
-
reduces ODC activity by 24%
DL-alpha-difluoromethylornithine
-
1.5 mM DL-alpha-difluoromethylornithine is an effective inhibitor of ODC. In the absence of phenanthrene, treatment reduces ODC activity by 52%.
DL-alpha-Monofluoromethylornithine
-
-
DL-alpha-Monofluoromethylornithine
-
-
ethyl[dimethylaminopropyl]carbodiimide
-
1.0 mM, 54% inhibition
ethyl[dimethylaminopropyl]carbodiimide
1.0 mM, 52% inhibition
geneticin
-
G418, weak non-competitive inhibition cs. L-ornithine
Hexylamine
-
-
histamine
-
-
Isonicotinic acid hydrazide
-
-
K+
-
220 mM, 50% inhibition
L-2,4-diaminobutyrate
-
-
L-arginine
-
competitive inhibition
L-arginine
-
L-arginine reduces cell proliferation and ornithine decarboxylase activity in patients with colorectal adenoma and adenocarcinoma, overview
L-canaline
-
-
L-lysine
-
competitive inhibition
Ly-294002
-
a PI3K inhibitor
Lys
-
competitive
Lys
-
L-Lys
Lys
-
relatively ineffective
methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]-1-methylhistidinate
-
-
methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]histidinate
-
-
methyl N5-(tert-butoxycarbonyl)-N2-{[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl}-L-ornithinate
-
-
metronidazole
-
-
Mg2+
-
15 mM, 50% inhibition
Mn2+
-
1.0 mM, 50% inhibition
MTA
1 mM, 70% inhibition
N-(4-ethoxy-1,3-benzothiazol-2-yl)-4-methoxybenzamide
-
-
N-(4-ethoxy-1,3-benzothiazol-2-yl)-4-propoxybenzamide
-
-
N-(4-ethoxy-1,3-benzothiazol-2-yl)benzamide
-
-
N-(6-ethoxy-1,3-benzothiazol-2-yl)-4-propoxybenzamide
-
-
N-acetylcysteine
-
decreases enzyme activity in lung carcinoma NCI-H82 cells and reduces the cell viability, overview
N-delta-chloroacetyl-L-ornithine
-
-
N-ethylmaleimide
-
0.01 mM, complete inhibition
N-ethylmaleimide
0.01 mM, 99% inhibition
Na+
-
300 mM, 50% inhibition
Na+
-
NaCl
Orn
-
inhibition of Lys decarboxylation
Ornithine decarboxylase antizyme
-
purification of the protein inhibitor
-
Ornithine decarboxylase antizyme
-
noncompetitive with respect to Orn, plays a role in the regulation of ornithine decarboxylase in mammary gland under physiological conditions
-
Ornithine decarboxylase antizyme
-
ornithine decarboxylase antizymes are proteins which negatively regulate cellular polyamine levels via their affects on polyamine synthesis and cellular uptake, development of a computer tool, OAF or ODC antizyme finder, for identifying antizyme encoding sequences in spliced or intronless nucleic acid sequenes, overview
-
ornithine decarboxylase antizyme-1
-
-
-
ornithine decarboxylase antizyme-2
-
-
-
ornithine decarboxylase antizyme-3
-
-
-
ornithine decarboxylase antizyme-t
-
-
-
PD-98059
-
a MEK inhibitor
pentane-1,5-diyl dicarbamimidothioate
-
-
peroxynitrite
-
0.1 mM, 50% inhibition, almost complete inhibition above 1 mM, nitration of tyrosine residues
Phaseolotoxin
Pseudomonas syringae pv. phaseolicola
-
-
Phenylglyoxal
-
1.0 mM, 36% inhibition
Phenylglyoxal
1.0 mM, 71% inhibition
phosphopyridoxyl-histidine
-
-
phosphopyridoxyl-L-tryptophan methyl ester
-
-
phosphopyridoxyl-phenylalanine
-
-
propane-1,3-diyl dicarbamimidothioate
-
-
putrescine
-
-
putrescine
-
-
putrescine
-
-
putrescine
-
competitive
putrescine
-
reversible
putrescine
-
no inhibition
putrescine
-
-
putrescine
-
-
putrescine
-
-
putrescine
-
-
putrescine
-
-
putrescine
-
slight
putrescine
-
1 mM, 70% inhibition
putrescine
1 mM, 63% inhibition
putrescine
-
slight inhibition
putrescine
-
product inhibition
pyridoxyl-L-phenylalanine methyl ester
-
-
pyridoxyl-L-tryptophan methyl ester
-
-
S-nitrosoglutathione
-
inhibition likely via S-transnitrosation
Salicylaldehyde
-
1.0 mM, 98% inhibition
Salicylaldehyde
1.0 mM, 82% inhibition
spermidine
-
-
spermidine
-
-
spermidine
-
no inhibition
spermidine
-
-
spermidine
-
weak
spermidine
-
-
spermidine
-
noncompetitive
spermidine
-
no inhibition
spermidine
-
1 mM, 61% inhibition of recombinant-Hinge-ODC and 63% inhibition of recombinant PfODC
spermidine
50% inhibition at 0.15 mM per l
spermine
-
-
spermine
-
-
spermine
-
-
spermine
-
-
spermine
-
noncompetitive
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
vitamin C
-
decreases enzyme activity in lung carcinoma NCI-H82 cells and reduces the cell viability, overview
Zn2+
-
0.8 mM, 50% inhibition
monofluoro-methyl-ornithine
-
-
additional information
-
the enzyme is an important target for antitrypanosomal chemotherapy
-
additional information
-
treatment of protozoan diseases by inhibitors of ornithine decarboxylase
-
additional information
-
protein kinase phosphorylates ornithine decarboxylase, the reaction is dependent on spermine and spermidine, phosphorylation of ornithine decarboxylase inhibits its capacity to catalyze decarboxylation of L-Orn
-
additional information
stilbamine isethionate, up to 0.1 mM, shows no inhibition
-
additional information
-
RR-methyl acetylenic putrescine has no significant effect
-
additional information
-
-
-
additional information
-
not inhibited by alpha-difluoromethylornithine
-
additional information
-
subcutaneous injection of 10 mg of dexamethasone/kg body weight decreases significantly the basal levels of lung ODC activity
-
additional information
-
ODC activity decreases by 30-50% after incubation of cells with 1 mM putrescine, 0.1 mM spermidine or 0.1 mM spermine
-
additional information
-
enzyme activity decreases upon addition of L-arginine or L-methionine to growth medium, but L-arginine or L-methionine are not inhibitory to enzyme
-
additional information
not inhibitory: alpha-difluoromethylornithine
-
additional information
-
some chemotherapeutic agents aim at reducing ODC expression and show inhibitory effects on cancer cell growth, overview
-
additional information
-
the enzyme is induced by phorbol esters, rapamycin, which blocks phosphorylation of 4E-BP1, inhibits the induction of ODC in response to serum
-
additional information
-
inhibition of ODC activity reverts the transformation of cells in vitro and reduces tumor growth
-
additional information
-
Bcl-2 has no effect on the activity and expression of ODC
-
additional information
-
serum deprivation reduces enzyme activity by 87.6% in SH-SY5Y cells, overview, enzyme activity is not affected in secondary cell lines exposed to 872 MHz RF radiation, overview
-
additional information
-
enzyme activity is not affected in secondary cell lines exposed to 872 MHz RF radiation, overview
-
additional information
-
serum deprivation reduces enzyme activity by 97.2% and by 87.0% in C6 cells, overview, enzyme activity is affected in primary astrocytes but not in secondary cell lines exposed to 872 MHz RF radiation, overview
-
additional information
-
retinoic acid suppresses the enzyme expression
-
additional information
-
ODC is degraded in an ubiquitin-independent manner mediated by antizyme 1
-
additional information
-
treatment of plants exposed to phenanthrene with DL-alpha-difluoromethylarginine does not result in any major changes to the trends in ODC activity observed in plants exposed to phenanthrene; treatment with methylglyoxal-bis(guanylhydrazone) does not significantly influence ODC activity
-
additional information
-
ODC is inhibited by MAPK kinase, PKA, and PI3K inhibitors
-
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
-
hypoxia deminishes ODC expression, ODC inhibition enhances the anti-tumor effect of antiangiogenesis therapy
-
additional information
-
hypoxia deminishes ODC expression
-
additional information
-
12-15% inhibition at 4-8 mg/ml by an ethanolic extract from the stem bark of Bursera fagaroides, collected during January 2004 in the region of Capula, Michoacan, Mexico, on ODC activity in vitro and on the growth of Entamoeba histolytica, overview
-
additional information
-
no inhibition by phosphopyridoxyl-pyridine-D-Ala and BOC-protected phosphopyridoxyl-alpha,gamma-diaminobutyric acid, coenzyme derivative inhibitor development, molecular modeling and inhibition mechanism, binding model of the phosphopyridoxyl conjugates in the active site of hODC, overview
-
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
-
ODC inhibition decreases putrescine levels, AdoMetDC inhibition decreases the levels of both spermidine and spermine
-
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
no inhibition of the Entamoeba histolytica enzyme by specific irreversible ODC inhibitor alpha-difluoromethylornithine, DFMO, the recombinant enzyme shows altered amino acid sequence and three-dimensional structure, Entamoeba histolytica putative ODC has a putative binding site for DFMO with substituted disrupted amino acids D332, D361, and Y323 by H296, F305, and N334, through which this inhibitor interacts with the protein
-
additional information
-
Arabidopsis S15 ribosomal protein does not inhibit the enzymatic activity of the plant ODC
-
additional information
-
ornithine decarboxylase and antizyme protein form a complex with 1:1 stoichiometry. Antizyme inhibits ornithine decarboxylase and faclilitates its degradation. The association constant is 6000000 per M. Circular dichroism spectra show a change in the secondary structure of the proteins in the complex
-
additional information
-
enzyme from Entamoeba histolytica is resistant to the irreversible inhibitor of ornithine decarboxylases, a-difluoromethylornithine. crystallographic data
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
-
3'-O-Methyl-GTP
-
stimulates
adenosine
-
approx. 10fold activation of dephosporylated ODC at 1 mM, approx. 2fold activation of native ODC
alpha,beta-methylene-GTP
-
stimulates
antizyme inhibitor 2
-
-
-
ATP
-
approx. 10fold activation of dephosporylated ODC at 1 mM, approx. 1.5fold activation of native ODC
beta,gamma-methylene-GTP
-
stimulates
dGTP
-
reactivation of ODC at pH values above 7.0
dithiothreitol
-
maximal activity in presence of 5 mM dithiothreitol
dithiothreitol
-
increases activity
dithiothreitol
-
required
dithiothreitol
-
increases activity
DNA
-
stimulates
GDP
-
reactivation of ODC at pH values above 7.0
GMP
-
approx. 10fold activation of dephosporylated ODC at 1 mM, approx. 1.2fold activation of native ODC
GTP
-
reactivation of ODC at pH values above 7.0, dodecameric ODC binds 2 GTPs per dimer at pH 5.8
GTP
-
approx. 10fold activation of dephosporylated ODC at 1 mM, approx. 2.5fold activation of native ODC
GTP
-
200% increase in enzyme activity in homogenates of whole pupae
Guanosine 5'-pentaphosphate
-
stimulates
guanosine 5'-tetraphosphate
-
stimulates
heparin
-
stimulates
ornithine decarboxylase paralogue
-
ODCp, degraded by the ubiquitin-dependent pathway. The ornithine decarboxylase paralogue antizyme inhibitor ODCp acts as a regulator of ODC activity and inhibits its proteasomal degradation. ODCp binds antizymes, AZs, with higher affinity than does ODC and releases active ODC from catalytically inactive ODC-AZ complexes, overview; ornithine decarboxylase paralogue acts as a regulator of ODC activity and inhibits its proteasomal degradation
-
phosphoserine
-
2 mM, 1.5fold activation
progesterone
-
ODC activity gradually increases in the presence of progesterone
RNA
-
stimulates
spermidine
-
1 mM, 211% activation
spermidine
-
2 mM, 40% activation
spermine
-
1 mM, 309% activation
spermine
-
2 mM, 140% activation
thiols
-
activate
UTP
-
approx. 10fold activation of dephosporylated ODC at 1 mM, approx. 2fold activation of native ODC
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, overview, ODC is induced during carcinogenesis by a variety of oncogenic stimuli, ODC activity is induced in cells that overexpress the translation initiation factor eIF4E, overview
-
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
-
ODC expression is induced by prolactin through the protein kinase C delta pathway leading to upregulation of Bcl-2 expression and thereby prevention of tumor necrosis factor alpha- and methotrexate-induced apoptosis, rottlerin, a protein kinase C delta inhibitor, completely blocks the induction of ODC activity by prolactin, while alpha-difluoromethylornithine does not, Bcl-2 has no effect on the activity and expression of ODC
-
additional information
-
the juvenile hormone at above 500 ng and cold stress at 6C induce the enzyme, synergistic effects, the ejaculatory apodeme of males is altered in length and width after incubation at 6C, overview
-
additional information
-
ODC activity is higher in endosymbiont-bearing trypanosomatids than in aposymbiotic cells, but isolated endosymbionts do not display this enzyme activity, expressed levels of ODC are similar in both strains, suggesting that ODC is positively modulated in endosymbiont-bearing cells, overview
-
additional information
-
light dramatically stimulates the activity of ornithine decarboxylase
-
additional information
-
ischemia increases ODC activity, overview
-
additional information
-
trichostatin A induces ODC activity and cell death in cancer cells
-
additional information
-
activation of ODC is related to tumor promotion and progression
-
additional information
-
the enzyme is induced by interleukines 4 and 13, the induction is decreased by MAPK kinase PKA and P3IK inhibitors
-
additional information
-
2,4-dichlorophenoxyacetic acid induces the enzyme, best at 0.025 mM
-
additional information
-
carbonate ions increase the ODC enzyme expression
-
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
-
expression of gene speF is ornithine-inducible
-
additional information
-
12-O-tetradecanoylphorobl-13-acetate induces expression of ODC
-
additional information
-
increased enzyme activity after wounding of the potatoe
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.092
alpha-Methylornithine
-
25C, pH 5.8
1 - 1.2
L-2,4-diaminobutanoate
30C, pH 5.5
1 - 2.1
L-2,4-diaminobutanoate
Q040G7
30C, pH 7.5
3.9
L-2,4-diaminobutanoate
30C, pH 7.5
4.9
L-2,4-diaminobutanoate
30C, pH 5.5
1.59
L-lysine
-
-
5
L-lysine
30C, pH 5.5
7.2
L-lysine
30C, pH 5.5
10.3
L-lysine
pH 5.5, 37C
0.0027
L-Orn
-
-
0.0047
L-Orn
-
-
0.03
L-Orn
-
mutant enzyme C360A
0.044
L-Orn
-
-
0.052
L-Orn
-
-
0.06
L-Orn
-
in 10 mM sodium phosphate buffer, pH 7.0
0.07
L-Orn
-
enzyme from epidermis
0.081
L-Orn
-
mutant enzyme K69A
0.086
L-Orn
-
wild type enzyme
0.09
L-Orn
-
in presence of 2.9 mM dithiothreitol
0.1
L-Orn
-
-
0.1
L-Orn
-
in absence of NaCl
0.1
L-Orn
-
-
0.109
L-Orn
-
-
0.11
L-Orn
-
-
0.13
L-Orn
-
-
0.15
L-Orn
-
mutant enzyme C70S
0.17
L-Orn
-
-
0.2
L-Orn
-
-
0.28
L-Orn
-
native enzyme
0.33
L-Orn
-
recombinant enzyme
0.35
L-Orn
-
-
0.36
L-Orn
-
-
0.6
L-Orn
-
in presence of 0.25 M NaCl
0.6
L-Orn
-
-
0.7
L-Orn
-
in presence of 0.25 M NaCl
1
L-Orn
-
enzyme from chromatin
1.7
L-Orn
-
-
2.2
L-Orn
-
cytosolic enzyme
3.6
L-Orn
-
degradative ornithine decarboxylase
5.6
L-Orn
-
biosynthetic ornithine decarboxylase
0.041
L-ornithine
-
recombinant PfODC
0.047
L-ornithine
-
recombinant Pf-Hinge-ODC
0.054
L-ornithine
-
C360S mutant
0.1
L-ornithine
-
C360A mutant
0.122
L-ornithine
-
CO2 assay, pH 7.8, 25C
0.16
L-ornithine
-
recombinant PfODC domain
0.18
L-ornithine
-
K69R mutant
0.19
L-ornithine
Pseudomonas syringae pv. phaseolicola
-
pH 7.3, 37C
0.214
L-ornithine
-
circular dichroism assay, pH 7.8, 25C
0.25
L-ornithine
-
-
0.27
L-ornithine
-
mutant enzyme S396A, at pH 7.5 and 37C
0.37
L-ornithine
-
wild-type, pH 8.0, 37C
0.37
L-ornithine
-
wild type enzyme, at pH 7.5 and 37C
0.395
L-ornithine
pH 8.0, 22C
0.4
L-ornithine
-
-
0.4
L-ornithine
-
apparent value, at 37C
0.49
L-ornithine
-
-
0.5
L-ornithine
-
-
0.5
L-ornithine
-
-
0.56
L-ornithine
-
-
0.6
L-ornithine
mutant I163T/E165T, pH 7.0, temperature not specified in the publication; mutant I163T, pH 7.0, temperature not specified in the publication
0.7
L-ornithine
30C, pH 5.5
0.7
L-ornithine
mutant E165T, pH 7.0, temperature not specified in the publication
1
L-ornithine
-
at pH 5.5, 35C
1
L-ornithine
30C, pH 5.5
1.1
L-ornithine
mutant I163V/E165V, pH 7.0, temperature not specified in the publication
1.3
L-ornithine
mutant I163V, pH 7.0, temperature not specified in the publication
1.4
L-ornithine
mutant E165V, pH 7.0, temperature not specified in the publication
1.5
L-ornithine
mutant I163A, pH 7.0, temperature not specified in the publication; mutant I163S, pH 7.0, temperature not specified in the publication
1.6
L-ornithine
pH 5.5, 37C
1.7
L-ornithine
mutant I163G, pH 7.0, temperature not specified in the publication
1.79
L-ornithine
-
C115A mutant
1.9
L-ornithine
mutant E165S, pH 7.0, temperature not specified in the publication
2.4
L-ornithine
mutant E165A, pH 7.0, temperature not specified in the publication
3
L-ornithine
mutant E165G, pH 7.0, temperature not specified in the publication
3.3
L-ornithine
wild-type, pH 7.0, temperature not specified in the publication
7.2
L-ornithine
Q040G7
30C, pH 7.5
43
L-ornithine
-
mutant K294A, pH 8.0, 37C
55.2
L-ornithine
-
mutant enzyme D364E, at pH 7.5 and 37C
207
L-ornithine
-
pupa, 37C, pH 7.1
438
L-ornithine
-
larva, 37C, pH 7.1
1660
L-ornithine
-
ovaries of young females, 37C, pH 7.1
0.091
Lys
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
alpha-Methylornithine
Lactobacillus sp. 30a
-
25C, pH 5.8
0.05
L-2,4-diaminobutanoate
Oenococcus oeni
Q5ZH57
30C, pH 5.5
0.35
L-2,4-diaminobutanoate
Lactobacillus gasseri
Q040G7
30C, pH 7.5
0.45
L-2,4-diaminobutanoate
Lactobacillus brevis
H8ZI01
30C, pH 5.5
0.5
L-2,4-diaminobutanoate
Lactobacillus casei
Q038E5
30C, pH 7.5
0.09
L-lysine
Oenococcus oeni
Q5ZH57
30C, pH 5.5
0.24
L-lysine
Nicotiana glutinosa
-
-
0.25
L-lysine
Lactobacillus saerimneri 30a
P43099
pH 5.5, 37C
0.57
L-lysine
Lactobacillus brevis
H8ZI01
30C, pH 5.5
0.003
L-ornithine
Plasmodium falciparum
-
recombinant PfODC domain
0.006
L-ornithine
Plasmodium falciparum
-
recombinant Pf-Hinge-ODC
0.015
L-ornithine
Trypanosoma brucei
-
mutant enzyme D364E, at pH 7.5 and 37C
0.14
L-ornithine
Lactobacillus gasseri
Q040G7
30C, pH 7.5
0.18
L-ornithine
Erythroxylum coca
G4XUJ8
pH 8.0, 22C
3
L-ornithine
Nicotiana glutinosa
-
-
3.3
L-ornithine
Saccharomyces cerevisiae
-
CO2 assay, pH 7.8, 25C
3.4
L-ornithine
Escherichia coli
P21169
wild-type, pH 7.0, temperature not specified in the publication
3.5
L-ornithine
Trypanosoma brucei
-
mutant K294A, pH 8.0, 37C
3.6
L-ornithine
Escherichia coli
P21169
mutant I163A, pH 7.0, temperature not specified in the publication
4.2
L-ornithine
Saccharomyces cerevisiae
-
circular dichroism assay, pH 7.8, 25C
4.2
L-ornithine
Escherichia coli
P21169
mutant I163G, pH 7.0, temperature not specified in the publication
4.4
L-ornithine
Escherichia coli
P21169
mutant I163V, pH 7.0, temperature not specified in the publication
4.8
L-ornithine
Lactobacillus brevis
H8ZI01
30C, pH 5.5
4.8
L-ornithine
Escherichia coli
P21169
mutant E165A, pH 7.0, temperature not specified in the publication
5.6
L-ornithine
Escherichia coli
P21169
mutant E165G, pH 7.0, temperature not specified in the publication
6.9
L-ornithine
Oenococcus oeni
Q5ZH57
30C, pH 5.5
7
L-ornithine
Trypanosoma brucei
-
wild type enzyme, at pH 7.5 and 37C
7.4
L-ornithine
Escherichia coli
P21169
mutant I163S, pH 7.0, temperature not specified in the publication
9.4
L-ornithine
Trypanosoma brucei
-
-
9.77
L-ornithine
Lactobacillus saerimneri 30a
P43099
pH 5.5, 37C
10
L-ornithine
Trypanosoma brucei
-
mutant enzyme S396A, at pH 7.5 and 37C
10.1
L-ornithine
Escherichia coli
P21169
mutant E165S, pH 7.0, temperature not specified in the publication; mutant I163T, pH 7.0, temperature not specified in the publication
10.9
L-ornithine
Escherichia coli
P21169
mutant E165V, pH 7.0, temperature not specified in the publication
15
L-ornithine
Trypanosoma brucei
-
-
15.4
L-ornithine
Trypanosoma brucei
-
wild-type, pH 8.0, 37C
24.8
L-ornithine
Escherichia coli
P21169
mutant E165T, pH 7.0, temperature not specified in the publication
25.7
L-ornithine
Escherichia coli
P21169
mutant I163V/E165V, pH 7.0, temperature not specified in the publication
38.5
L-ornithine
Escherichia coli
P21169
mutant I163T/E165T, pH 7.0, temperature not specified in the publication
77.8
L-ornithine
Nicotiana glutinosa
-
-
additional information
additional information
Escherichia coli
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
L-2,4-diaminobutanoate
Lactobacillus casei
Q038E5
30C, pH 7.5
2561
0.01
L-2,4-diaminobutanoate
Oenococcus oeni
Q5ZH57
30C, pH 5.5
2561
0.03
L-2,4-diaminobutanoate
Lactobacillus gasseri
Q040G7
30C, pH 7.5
2561
0.04
L-2,4-diaminobutanoate
Lactobacillus brevis
H8ZI01
30C, pH 5.5
2561
0.02
L-lysine
Oenococcus oeni
Q5ZH57
30C, pH 5.5
134
0.03
L-lysine
Lactobacillus saerimneri 30a
P43099
pH 5.5, 37C
134
0.08
L-lysine
Lactobacillus brevis
H8ZI01
30C, pH 5.5
134
0.00027
L-ornithine
Trypanosoma brucei
-
mutant enzyme D364E, at pH 7.5 and 37C
192
0.02
L-ornithine
Lactobacillus gasseri
Q040G7
30C, pH 7.5
192
0.465
L-ornithine
Erythroxylum coca
G4XUJ8
pH 8.0, 22C
192
1
L-ornithine
Escherichia coli
P21169
wild-type, pH 7.0, temperature not specified in the publication
192
1.8
L-ornithine
Escherichia coli
P21169
mutant I163T, pH 7.0, temperature not specified in the publication
192
1.9
L-ornithine
Escherichia coli
P21169
mutant E165G, pH 7.0, temperature not specified in the publication
192
2
L-ornithine
Escherichia coli
P21169
mutant E165A, pH 7.0, temperature not specified in the publication
192
2.3
L-ornithine
Escherichia coli
P21169
mutant I163V/E165V, pH 7.0, temperature not specified in the publication
192
2.4
L-ornithine
Escherichia coli
P21169
mutant I163A, pH 7.0, temperature not specified in the publication
192
2.5
L-ornithine
Escherichia coli
P21169
mutant I163G, pH 7.0, temperature not specified in the publication
192
3.5
L-ornithine
Escherichia coli
P21169
mutant I163V, pH 7.0, temperature not specified in the publication
192
3.7
L-ornithine
Escherichia coli
P21169
mutant E165T, pH 7.0, temperature not specified in the publication
192
4.7
L-ornithine
Lactobacillus brevis
H8ZI01
30C, pH 5.5
192
4.8
L-ornithine
Escherichia coli
P21169
mutant I163S, pH 7.0, temperature not specified in the publication
192
5.2
L-ornithine
Escherichia coli
P21169
mutant E165S, pH 7.0, temperature not specified in the publication
192
6
L-ornithine
Lactobacillus saerimneri 30a
P43099
pH 5.5, 37C
192
6.4
L-ornithine
Escherichia coli
P21169
mutant I163T/E165T, pH 7.0, temperature not specified in the publication
192
7.6
L-ornithine
Escherichia coli
P21169
mutant E165V, pH 7.0, temperature not specified in the publication
192
9.2
L-ornithine
Oenococcus oeni
Q5ZH57
30C, pH 5.5
192
18.9
L-ornithine
Trypanosoma brucei
-
wild type enzyme, at pH 7.5 and 37C
192
20
L-ornithine
Saccharomyces cerevisiae
-
circular dichroism assay, pH 7.8, 25C
192
27
L-ornithine
Saccharomyces cerevisiae
-
CO2 assay, pH 7.8, 25C
192
37
L-ornithine
Trypanosoma brucei
-
mutant enzyme S396A, at pH 7.5 and 37C
192
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00046
(2S)-5-amino-2-hydrazinylpentanoic acid
-
-
0.000001
1-amino-oxy-3-aminopropane
-
pH 7.5, 37C, recombinant enzyme
0.0271
1H-indol-3-yl(morpholin-4-yl)acetonitrile
-
at pH 7.5 and 37C
0.1
2-phenylethyl carbamimidothioate
-
Ki above 0.1 mM, at pH 7.5 and 37C
0.1
3-(morpholin-4-ylmethyl)-1H-indole
-
Ki above 0.1 mM, at pH 7.5 and 37C
0.0289
4,4'-[pentane-1,5-diylbis(oxy)]dibenzenecarboximidamide
-
at pH 7.5 and 37C
0.0027
alexidine
-
at pH 7.5 and 37C
0.026
alpha-difluoromethylornithine
Pseudomonas syringae pv. phaseolicola
-
pH 7.3, 37C
0.088
alpha-difluoromethylornithine
-
-
0.09
alpha-difluoroornithine
-
recombinant Pf-Hinge-ODC
0.8
Ba2+
-
-
0.0036
benzene-1,3-diyldiethane-2,1-diyl dicarbamimidothioate
-
at pH 7.5 and 37C
0.1
benzene-1,4-diyldimethanediyl dicarbamimidothioate
-
Ki above 0.1 mM, at pH 7.5 and 37C
0.1
but-2-yne-1,4-diyl dicarbamimidothioate
-
Ki above 0.1 mM, at pH 7.5 and 37C
0.0288
butane-1,4-diyl dicarbamimidothioate
-
at pH 7.5 and 37C
0.9
Ca2+
-
-
0.00002
CGP52622A
-
-
0.000008
CGP54619A
-
-
-
0.5
Co2+
-
-
0.38
D-ornithine
-
pH 7.8, 25C
4.5
geneticin
-
pH 8.0
8
geneticin
-
pH 7.0
220
K+
-
-
15
Mg2+
-
-
1
Mn2+
-
-
0.1
N-(4-ethoxy-1,3-benzothiazol-2-yl)-4-methoxybenzamide
-
Ki above 0.1 mM, at pH 7.5 and 37C
0.014
N-(4-ethoxy-1,3-benzothiazol-2-yl)-4-propoxybenzamide
-
at pH 7.5 and 37C
0.1
N-(4-ethoxy-1,3-benzothiazol-2-yl)benzamide
-
Ki above 0.1 mM, at pH 7.5 and 37C
0.1
N-(6-ethoxy-1,3-benzothiazol-2-yl)-4-propoxybenzamide
-
Ki above 0.1 mM, at pH 7.5 and 37C
300
Na+
-
-
0.0102
pentane-1,5-diyl dicarbamimidothioate
-
at pH 7.5 and 37C
0.016
Phaseolotoxin
Pseudomonas syringae pv. phaseolicola
-
pH 7.3, 37C
0.1
propane-1,3-diyl dicarbamimidothioate
-
Ki above 0.1 mM, at pH 7.5 and 37C
0.05
putrescine
-
recombinant Pf-Hinge-ODC
0.068
putrescine
-
-
0.16
putrescine
-
recombinant PfODC domain
0.25
putrescine
-
pH 7.8, 25C
0.8
Zn2+
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
1H-indol-3-yl(morpholin-4-yl)acetonitrile
Trypanosoma brucei
-
at pH 7.5 and 37C
0.1
2-phenylethyl carbamimidothioate
Trypanosoma brucei
-
IC50 above 0.1 mM, at pH 7.5 and 37C
0.1
3-(morpholin-4-ylmethyl)-1H-indole
Trypanosoma brucei
-
IC50 above 0.1 mM, at pH 7.5 and 37C
0.0342
4,4'-[pentane-1,5-diylbis(oxy)]dibenzenecarboximidamide
Trypanosoma brucei
-
at pH 7.5 and 37C
0.024
alexidine
Trypanosoma brucei
-
at pH 7.5 and 37C
0.2
alpha-difluoromethylornithine
Phytomonas sp.
-
at 37C
1
alpha-difluoromethylornithine
Plasmodium falciparum
-
-
0.014
benzene-1,3-diyldiethane-2,1-diyl dicarbamimidothioate
Trypanosoma brucei
-
at pH 7.5 and 37C
0.075
benzene-1,4-diyldimethanediyl dicarbamimidothioate
Trypanosoma brucei
-
at pH 7.5 and 37C
0.1
but-2-yne-1,4-diyl dicarbamimidothioate
Trypanosoma brucei
-
IC50 above 0.1 mM, at pH 7.5 and 37C
0.0303
butane-1,4-diyl dicarbamimidothioate
Trypanosoma brucei
-
at pH 7.5 and 37C
0.1
N-(4-ethoxy-1,3-benzothiazol-2-yl)-4-methoxybenzamide
Trypanosoma brucei
-
IC50 above 0.1 mM, at pH 7.5 and 37C
0.0594
N-(4-ethoxy-1,3-benzothiazol-2-yl)-4-propoxybenzamide
Trypanosoma brucei
-
at pH 7.5 and 37C
0.1
N-(4-ethoxy-1,3-benzothiazol-2-yl)benzamide
Trypanosoma brucei
-
IC50 above 0.1 mM, at pH 7.5 and 37C
0.1
N-(6-ethoxy-1,3-benzothiazol-2-yl)-4-propoxybenzamide
Trypanosoma brucei
-
IC50 above 0.1 mM, at pH 7.5 and 37C
0.0153
pentane-1,5-diyl dicarbamimidothioate
Trypanosoma brucei
-
at pH 7.5 and 37C
0.075
propane-1,3-diyl dicarbamimidothioate
Trypanosoma brucei
-
at pH 7.5 and 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000011
-
healthy bladder, mucosa
0.0000039
-
healthy bladder, muscularis
0.0000132
-
ischemic bladder, mucosa
0.0000311
-
ischemic bladder, muscularis
0.0043
-
recombinant pF-Hinge-ODC
0.0219
purified recombinant enzyme
0.0388
-
recombinant PfODC
0.049
-
-
0.11
-
about, ODC activity in anaplastic gliomas
0.33
-
chromatin-bound enzyme
1.36
-
-
3.3
Pseudomonas syringae pv. phaseolicola
-
pH 7.3, 37C
17 - 32
-
-
99
-
biosynthetic ornithine decarboxylase
130
-
degradative ornithine decarboxylase
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
less than 0.0000001 mM of D-ornithine decarboxylate/min/mg
additional information
-
putative ODC activity in leaf extract
additional information
-
assay for enzyme activity based on atmospheric pressure chemical ionization-mass spectrometry of dansylated putrescine
additional information
-
assay to quantify enzyme levels in formalin-fixed tumor tissues based on antibody coupled to Alexa 647 dye
additional information
circadian variations in ODC activity in female and male mice, overview
additional information
-
activity in patients with colorectal adenoma and adenocarcinoma, overview
additional information
-
regional enzyme activity in the heart, overview, tumor enzyme activity in relation to progression-free survival, overview
additional information
-
quantitative determination of polyamine contents in leaves, diurnal changes in polyamine content, arginine and ornithine decarboxylase, and diamine oxidase in tobacco leaves, overview
additional information
-
altered nitric oxide synthase, arginase and ornithine decarboxylase activities, and polyamine synthesis in response to ischemia of the rabbit detrusor, polyamine levels in ischemic detrusor tissue, overview
additional information
-
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide cell viability assay
additional information
-
immunohistochemical assay of ODC protein in gastric precancerous and cancerous lesions, overview
additional information
-
The ODC activity is determined by measuring the release of CO2 from L-ornithine, in vitro-translated proteins are combined in the proportion 2.5:1:7 (ODC:antizyme 1:ODC paralogue/AZIN2), ODC activity increases in the reaction mixtures containing ODC with either ODC paralogue or antizyme inhibitor together with antizyme 1 compared with the control reaction containing ODC with antizyme 1
additional information
-
activities in cell suspension cultures, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
-
L-lysine decarboxylation
6.8
-
assay at
6.9
-
degradative ornithine decarboxylase
7 - 8
-
recombinant PfODC domain
7.1
-
assay at
7.2
assay at
7.2
-
assay at
7.2
-
assay at
7.3
Pseudomonas syringae pv. phaseolicola
-
-
7.4
-
assay at
7.4
-
assay at
7.5
-
assay at
7.5 - 8.5
-
recombinant Pf-Hinge-ODC
7.8
-
assay at
8
-
enzyme form A
8
-
L-ornithine decarboxylation
8.3
-
biosynthetic ornithine decarboxylase
8.5
-
in supernatant fraction
8.5
-
assay at
9
-
in pellet fraction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
at least 40% of maximum activity
5.5
Pseudomonas syringae pv. phaseolicola
-
10% of the activity at pH 7.3
6.4 - 8.7
-
approx. 20% of maximal activity at pH 6.4, approx. 50% of maximal activity at pH 8.6
6.5 - 7.5
-
L-lysine decarboxylation, approx. 40% of maximal activity at pH 7.5
6.5 - 9
-
pH 6.5: about 60% of maximal activity, pH 9.0: about 45% of maximal activity
7 - 9
-
linear increase
7.2 - 8.7
-
L-ornithine decarboxylation, approx. 35% of maximal activity at pH 7.2
7.4 - 7.8
-
pH 7.4: about 50% of maximal activity, pH 7.8: maximal activity
8 - 9.5
-
pH 8.0: about 50% of maximal activity, pH 9.5: about 73% of maximal activity
8.8
Pseudomonas syringae pv. phaseolicola
-
38% of the activity at pH 7.3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
assay at
37
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37 - 50
initial reaction rate remains unchanged within this range
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22 - 45
-
no activity below 22C, activity is sharply diminished above 45C
35 - 65
-
35C: about 60% of maximal activity, 65C: about 45% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.61
sequence calculation
6.2
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
epithelial carcinoma cells
Manually annotated by BRENDA team
-
lung cancer cell line
Manually annotated by BRENDA team
-
lung carcinoma cells
Manually annotated by BRENDA team
-
a Balb/c mice-derived mouse cell line
Manually annotated by BRENDA team
sexual dimorphism of the enzyme in the adrenal
Manually annotated by BRENDA team
-
from livers and spleens of BALB/c mice
Manually annotated by BRENDA team
Leishmania donovani LdBob
-
from livers and spleens of BALB/c mice
-
Manually annotated by BRENDA team
-
AR4-2J pancreatic tumor cells, which show increased phosphorylation of the eIF4E regulatory protein 4E-BP1 and high levels of eIF4E compared to normal cells, also exhibit increased translational initiation of ODC mRNA
Manually annotated by BRENDA team
-
melanoma cell line
Manually annotated by BRENDA team
-
muscularis and mucosa, healthy and ischemic, ischemia increases ODC activity
Manually annotated by BRENDA team
-
post-mortem healthy and Alzheimers disease brains, altered subcellular localization of ornithine decarboxylase in Alzheimers disease brain, overview
Manually annotated by BRENDA team
-
epithelial cells
Manually annotated by BRENDA team
-
breast cancer cell line
Manually annotated by BRENDA team
transcript levels are highest in buds and rolled leaves and lower in other organs
Manually annotated by BRENDA team
-
colon adenocarcinoma cell, enzyme activity decreases upon addition of L-arginine or L-methionine to growth medium
Manually annotated by BRENDA team
-
maximal activity in the middle and late log phases of growth
Manually annotated by BRENDA team
-
embroynic and non-embryonic
Manually annotated by BRENDA team
-
multiple enzyme forms in tumor cells
Manually annotated by BRENDA team
-
of healthy and ischemic bladder
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
of young females, high activity
Manually annotated by BRENDA team
-
neonatal foreskin fibroblasts
Manually annotated by BRENDA team
-
ODC expression level is positively correlated with the degree of malignity of gastric mucosa and development of gastric lesions in precancerous and cancerous gastric lesions, overview
Manually annotated by BRENDA team
-
positive nuclei in the junction
Manually annotated by BRENDA team
-
colon carcinoma cells
Manually annotated by BRENDA team
-
basal ornithine decarboxylase activity in isolated left atria shows differences in the four groups of animals studied, being higher in males than estrogenized females, and increased in both sexes by castration, though not significantly changed in females
Manually annotated by BRENDA team
-
cervical carcinoma cells
Manually annotated by BRENDA team
-
a cervix cancer cell line
Manually annotated by BRENDA team
-
human acute myeloid leukemia cell, enzyme activity correlates with myeloid cell differentiation induced by retinoic acid treatment
Manually annotated by BRENDA team
-
intestinal epithelial cells
Manually annotated by BRENDA team
-
2 enzyme forms
Manually annotated by BRENDA team
-
of testosterone treated mouse. 13fold higher activity in male mice than that in females
Manually annotated by BRENDA team
-
hyperplastic and hypertrophic kidney, 80- to 1000fold increase in enzyme activity
Manually annotated by BRENDA team
-
leukemia cell line
Manually annotated by BRENDA team
-
a fibroblast cell line
Manually annotated by BRENDA team
-
neuroblastoma cell line
Manually annotated by BRENDA team
-
a human NB cell line
Manually annotated by BRENDA team
-
diurnal changes in enzyme activity and polyamine contents, overview
Manually annotated by BRENDA team
transcript levels are highest in buds and rolled leaves and lower in other organs
Manually annotated by BRENDA team
-
one enzyme form in liver and Morris hepatoma 7777 cells
Manually annotated by BRENDA team
-
pretreated with thioacetamide
Manually annotated by BRENDA team
-
a colon carcinoma cell line
Manually annotated by BRENDA team
-
breast epithelial cell line
Manually annotated by BRENDA team
-
breast cancer cell line
Manually annotated by BRENDA team
-
a breast cancer cell line
Manually annotated by BRENDA team
-
breast cancer cell line
Manually annotated by BRENDA team
-
breast cancer cell line
Manually annotated by BRENDA team
-
Helicobacter pylori-infected gastric mucosa, oral administation of Lactobacillus brevis induces a decrease in gastric enzyme activity and polyamine levels
Manually annotated by BRENDA team
-
Odc1 is expressed predominantly in proliferating myoblasts
Manually annotated by BRENDA team
-
lung carcinoma cells
Manually annotated by BRENDA team
-
lung carcinoma cell line
Manually annotated by BRENDA team
-
overexpression of constitutively active Ras12V results in up to 20fold increase of enzyme activity due to increase in enzyme transcription and translation
Manually annotated by BRENDA team
-
neuroblastoma cell line
Manually annotated by BRENDA team
-
of young and adult females, highest activity found
Manually annotated by BRENDA team
-
prostate cancer cell line
Manually annotated by BRENDA team
-
prostatic carcinoma cell line
Manually annotated by BRENDA team
-
from livers and spleens of BALB/c mice
Manually annotated by BRENDA team
Leishmania donovani LdBob
-
from livers and spleens of BALB/c mice
-
Manually annotated by BRENDA team
-
fluorescent location of ornithine decarboxylase employing derivatives of the specific inhibitor alpha-difluoromethylornithine, location of squamous cell carcinoma cells
Manually annotated by BRENDA team
Mus musculus K6/ODC
-
-
-
Manually annotated by BRENDA team
Entamoeba histolytica HM 1:IMSS
-
-
-
Manually annotated by BRENDA team
-
osteosarcoma cells
Manually annotated by BRENDA team
additional information
-
immunocytochemical localization of ornithine decarboxylase
Manually annotated by BRENDA team
additional information
-
autoradiographic localization
Manually annotated by BRENDA team
additional information
-
cervix carcinoma cell line
Manually annotated by BRENDA team
additional information
-
the enzyme is increased in cancer cells
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
-
ODC activity is higher in endosymbiont-bearing trypanosomatids than in aposymbiotic cells, but isolated endosymbionts do not display this enzyme activity
Manually annotated by BRENDA team
additional information
-
ODC activity is elevated in tumor cells
Manually annotated by BRENDA team
additional information
-
ODC is overexpressed in a variety of cancer cells
Manually annotated by BRENDA team
additional information
-
ODC is expressed in all types of cells
Manually annotated by BRENDA team
additional information
-
during mitotic cell cycle, ODC exhibits two activity peaks, one at G1/S transition and the second during G2/M transition
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
variation from mainly cytoplasmic to both cytoplasm and nucleus, regulatory protein antizyme-1 is mainly localized to nuceus
Manually annotated by BRENDA team
-
prostate of cancer patients
Manually annotated by BRENDA team
-
altered subcellular localization of ornithine decarboxylase from nucleus to cytosol in Alzheimers disease brain, overview
Manually annotated by BRENDA team
-
one peak, just after light induction, occurrs in the cytosolic fraction with 35% of the total ornithine decarboxylase activity
Manually annotated by BRENDA team
Entamoeba histolytica HM 1:IMSS, Plasmodium falciparum FCR 3TC
-
-
-
Manually annotated by BRENDA team
-
both cytoplasm and nucleus, regulatory protein antizyme-1 is mainly localized to nuceus
Manually annotated by BRENDA team
-
mainly, one peak, just after light induction, occurrs in the cytosolic fraction with 35% of the total ornithine decarboxylase activity
-
Manually annotated by BRENDA team
-
prostate of patients suffering from benign prostatic hyperplasia
-
Manually annotated by BRENDA team
additional information
-
regulatory protein antizyme-1 is involved in nucleocytoplasmic shuttling of enzyme
-
Manually annotated by BRENDA team
additional information
-
immunohictochemic subcellular analysis of cells, overview
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39000
-
gel filtration
4000
45970
calculated from amino acid sequence
709697
46000
-
SDS-PAGE
708441
55000
-
gel filtration in presence of 0.25 NaCl
4001
55000
-
gel filtration in presence of 0.25 M NaCl, 10 mM sodium phosphate buffer, pH 7.0, monomeric form
4010
55000
-
gel filtration in presence of 0.1 M NaCl
4043
57000
-
gel filtration
4002
64000
-
gel filtration
4007
68000
-
gel filtration
4044
80000
-
HPLC in 0.15 M NaCl
4011
90000
-
native enzyme, gel filtration
3999
90000
-
gel filtration
4030
90000
-
gel filtration and SDS-PAGE, protein cross-linked by glutaraldehyde
728543
90670
-
dimeric enzyme, MALDI-TOF
728543
92000
-
recombinant enzyme, gel filtration
3999
92000
-
native PAGE
649722, 651824
100000
-
gel filtration
4003
100000
-
-
4015
100000
-
gel filtration
4024
100000 - 110000
-
gel filtration
4009
105000
-
non-denaturing native PAGE
4016
106000
native PAGE
651824
110000
-
gel filtration in presence of 0.25 M NaCl
4002
110000
-
-
4002
110000
-
gel filtration
4004
110000
-
gel filtration
4035
110000
-
gel filtration
4042
135000
-
gel filtration
653200
150000
-
gel filtration in presence of 10 mM sodium phosphate buffer, trimeric enzyme form
4010
160000
Pseudomonas syringae pv. phaseolicola
-
gel filtration
666559
170000
-
gel filtration in absence of NaCl
4043
190000
-
gel filtration in absence of NaCl
4043
210000
-
gel filtration
4038
211000
-
gel filtration
4029
216000
-
gel filtration
651210
250000
-
gel filtration in presence of 1 mM sodium phosphate buffer, polymeric enzyme form
4010
330000
gel filtration
649770
990600
-
-
649110
1040000
-
equilibrium sedimentation
4023
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
2 protein bands detected in SDS-PAGE, MW 52000 and MW 54000
?
-
x * 53000, SDS-PAGE
?
-
x * 47100, SDS-PAGE
?
-
x * 51000, immunoblot
?
x * 46000, about, sequence calculation, x * 48000, recombinant His- and S-tagged enzyme, SDS-PAGE
?
-
x * 85000, SDS-PAGE
?
x * 44522, calculated
?
Lactobacillus saerimneri 30a ATCC 33222
-
x * 84000, SDS-PAGE
-
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 43000, SDS-PAGE
dimer
-
2 * 53000
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 80000, degradative ornithine decarboxylase; 2 * 81000, biosynthetic ornithine decarboxylase
dimer
-
2 * 47000, SDS-PAGE
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 46500, SDS-PAGE
dimer
-
ODC is an obligate homodimer
dimer
-
2 * 46000, SDS-PAGE
dimer
-
2 * 53000, SDS-PAGE
dimer
-
crystal structure
dimer
-
2 * 68000, SDS-PAGE
dimer
-
antizyme binds to the monomeric form of ODC, preventing formation of the enzymatically active homodimer, and then targets ODC for degradation
dimer
-
2 * 44558, MALDI-TOF; 2 * 46000, SDS-PAGE
dodecamer
-
12 * 85000, SDS-PAGE
dodecamer
-
the dodecamer dissociates into dimers at high pH in the presence or absence of GTP
dodecamer
-
12 * 83000, SDS-PAGE, dodecamer composed of six homodimers
monomer
-
1 * 55000, SDS-PAGE
monomer
-
1 * 64000, SDS-PAGE
monomer
-
1 * 55000, gel filtration in presence of 0.25 M NaCl
pentamer
-
5 * 45000, SDS-PAGE
tetramer
-
4 * 55000, SDS-PAGE
tetramer
Pseudomonas syringae pv. phaseolicola
-
4 * 41000, SDS-PAGE, or 3 * 41000 + 1 * 56000, SDS-PAGE
monomer
-
1 * 50000, SDS-PAGE, the enzyme exists as monomer at high salt concentrations and in polymeric form at low salt concentrations
additional information
structural analysis and modelling
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
inactive after incubation with alkaline phosphatase
additional information
-
supplemental L-methionine or L-arginine induce a marked decrease in enzyme half-life concomitantly with an increase in the activity of enzyme inhibitory protein antizyme
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
C-terminally truncated enzyme, to 2.8 a resolution. Comparison with other ornithine decarboxylase homologs. Resistance to the irreversible inhibitor of ornithine decarboxylases, a-difluoromethylornithine, is due to substitution of key substrate binding residues in active site pocket. Additionally, a few more substitutions similar to antizyme inhibitor, a non-functional homologue of ornithine decarboxylases, are present
-
circular dichroism analysis reveals 39% alpha-helix, 25% beta-sheets and 36% random coils. Modeling of the enzyme dimer shows two separate active sites at the dimer interface with Lys57 and Cys334 residues of opposite monomers contributing to each active site
-
homology modeling based on the crystal structure of ODC from Lactobacillus 30a, PDB entry 1ORD. The model reveals an unusually deep and narrow shape of the substrate tunnel. Amino acids at the substrate entry site are V156, D160, I163, E165, E689, and Q691
crystal structure at 2.1 A
-
purified recombinant His6-tagged enzyme in complex with inhibitor 1-amino-oxy-3-aminopropane or with both inhibitor and cofactor, sitting drop vapour diffusion method, 15C, 6 mg/ml protein in 25 mM HEPES, pH 7.2, 2 mM DTT, 0.5 mM EDTA, 0.02% Brij 35, 1 mM PMSF and 2 mM 1-amino-oxy-3-aminopropane, with or without 0.02 mM pyridoxal 5'-phosphate, mixed with well solution containing 25% v/v PEG 3350, 0.2 M ammonium acetate and 0.1 M Bis-Tris, pH 6.5, 2 days, needle-cluster crystals, single crystals are obtained by using a well solution containing 18% v/v PEG 3350, 0.2 M ammonium acetate, 0.1 M Bis-Tris, pH 6.5, and 3 mg/ml protein concentration, X-ray diffraction structure determination and analysis at 1.9-3.0 A resolution, molecular replacement
-
G121Y mutant dimer at pH 7.0 in the presence of GTP, purified ODC is dialyzed against 100 mM sodium-HCl, pH 6.5, 1 mM dithiothreitol, 0.2 mM pyridoxal 5'-phosphate, 0.02% sodium azide and 0.5 mM EDTA and concentrated to 20 mg/ml, crystals are grown at room temperature by the sitting-drop method from reservoirs containing 30% polyethylene glycol 3350, 200 mM ammonium acetate and 100 mM Na-HEPES, pH 7.0, crystals diffract to 2.7 A resolution
-
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
-
co-crystallization with D-ornithine and geneticin sulfate, 23 mg/ml ODC in 10 mM HEPES, pH 7.2, 50 mM NaCl, 10 mM dithiothreitol, 0.5 mM EDTA, 0.01% Brij-20, is preincubated with 25 mM D-ornithine and 100 mM geneticin sulfate for 10 min at room temperature, equal volumes of preincubated enzyme and well solution consisting of 20% polyethylene glycol 3350, 100 mM HEPES, pH 8.0, 10 mM dithiothreitol, 25 mM D-ornithine, pH 7.5, and 100 mM geneticine are used to form crystal drops, crystals diffract to 2.5 A
-
mutant K294A in complex with substrate analogue D-ornithine
-
ODC complexed with putrescine, 25 mg/ml ODC in 10 mM HEPES, pH 7.2, 450 mM NaCl, 10 mM dithiothreitol, 0.5 mM EDTA, 0.01% Brij-20, are preincubated with 15 mM D-ornithine for 10 min at room temperatur before crystallization, crystals are obtained at 16C by vapor diffusion mixing equal volumes of ODC-D-ornithine mixture and well solution containing 20% polyethylene glycol 3350, 200 mM NaOAc, 100 mM HEPES, pH 7.5 and 10 mM dithiothreitol
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
1 h, 14% loss of activity
4044
40
-
half-life 70 min
649722
50
-
half-life 20 min
649722
60
-
half-life 5 min
649722
70 - 85
-
85% loss of activity after 15 min at 75C, more than 95% loss of activity after 15 min at 85C and above
653200
100
-
complete loss of activity after 10 min
4000
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Crithidia fasciculata ODC, in contrast to other phylogentically related enzymes, is rapidly degraded also in mammalian systems, and it contains several sequence elements essential for the rapid turnover of the protein, these regions are mainly located in the central part of the enzyme, overview, half-life of the wild-type enzyme is 3.2 h
ODC is rapidly degraded in mammalian cells as well as in a rabbit reticulocyte lysate system, ODC contains degradation signals that are also functionally active in mammalian cells involving the 26 S proteasome
-
dithiothreitol stabilizes the enzyme
lability increases during purification
-
antizyme 3 stabilize the enzyme
-
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
-
50% loss of activity after freezing and thawing of the purified enzyme
-
repeated freezing and thawing in the presence of 10% v/v glycerol causes 15-20% loss of activity
-
Leishmania donovani ODC has a very fast turnover in mammalian cells, but is a stable enzyme, half-life of the wild-type enzyme is 5.5 h
the enzyme is stable compared to mammalia or Crithida fasciculata and Phytomonas sp. enzymes, which are rapidly degraded, overview
-
formation of inactive forms in the absence of thiol-reducing agents
-
mouse ODC is quickly degraded by the 26S proteasome in mammalian and fungal cells
NAD(P)H quinone oxidoreductase binds to the enzyme and stabilizes it
-
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
-
dithiothreitol stabilizes
-
Phytomonas ODC can be markedly stabilized by 0.05 mM MG-132
-
enzyme is sensitive to freeze-thawing
Pseudomonas syringae pv. phaseolicola
-
formation of inactive forms in the absence of thiol-reducing agents
-
repeated freezing and thawing results in progressive inactivation
-
stabilized by 50% ethylene glycol or 0.1% Tween 80
-
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
-
the enzyme is stable compared to mammalia or Crithida fasciculata and Phytomonas sp. enzymes, which are rapidly degraded, overview
-
ODC has a very short half-life
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DMSO
-
about 40% specific activity after 0.5 h of DMSO treatment
DMSO
Phytomonas sp. Jma
-
about 40% specific activity after 0.5 h of DMSO treatment
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, stable for 15 days
-
-70C, 2 years, no loss of activity
-
4C, 1 month, no loss of activity
-
0-4C, 24 h, stable in presence of 0.05 mM pyridoxal 5'-phosphate, 2.5 mM dithiothreitol or 5 mM 2-mercaptoethanol, 10% w/v glycerol at pH 8.5
-
0C, stable
-
-40C, 25 mM Tris-HCl, pH 7.5, 0.1 mM EDTA, 2.5 mM dithiothreitol, 0.02% Brij 35
-
4C, 40 mM Tris/HCl, pH 7.5, 1 mM dithiothreitol, 1 mM EDTA, stable for several weeks
-
-20C, presence of 0.04 mM pyridoxal 5'-phosphate , 1.0 mM dithiothreitol, 10% glycerol, stable for at least 5 months
Pseudomonas syringae pv. phaseolicola
-
4C, presence of 0.04 mM pyridoxal 5'-phosphate , 1.0 mM dithiothreitol, stable for 2 weeks
Pseudomonas syringae pv. phaseolicola
-
-20C, 5 mM dithiothreitol, stable for at least 1 week
-
-20C, in presence of 0.03% Brij 35, stable for several weeks
-
-80C, in presence of dithiothreitol, pyridoxal phosphate, and Tween 80 unless very dilute, stable for 2 weeks
-
-80C, stable for at least 10 weeks
-
-20C, unstable in absence of pyridoxal 5'-phosphate
-
stable at 0C
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE Bio-Gel, Bio-Gel, Affi-Gel 501
-
Ni-affinity column chromatography
-
recombinant His- and S-tagged enzyme from Escherichia coli by nickel affinity chromatography
a biosynthetic ornithine decarboxylase and a degradative ornithine decarboxylase