Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5alpha-dihydrotestosterone
?
-
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
-
-
-
?
Arg
1-Amino-4-guanidinobutane
-
0.1% of the activity with L-Orn
-
-
?
D-ornithine
putrescine + CO2
-
very weak activity
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
L-2,4-Diaminobutyrate
1,3-Diaminopropane + CO2
-
2% of the activity with L-Orn
-
-
?
L-Lys
1,5-diaminopentane + CO2
L-lysine
1,5-diaminopentane + CO2
L-lysine
cadaverine + CO2
L-ornithine
putrescine + CO2
ornithine
putrescine + CO2
-
-
-
-
?
additional information
?
-
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
-
-
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
-
-
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
-
-
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
-
-
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
-
-
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
-
-
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
-
-
-
?
L-Lys
1,5-diaminopentane + CO2
-
2% of the activity with L-Orn
-
-
?
L-Lys
1,5-diaminopentane + CO2
-
-
-
-
?
L-Lys
1,5-diaminopentane + CO2
-
at 1.0% of the activity with Orn
-
-
?
L-lysine
1,5-diaminopentane + CO2
very low activity
-
-
?
L-lysine
1,5-diaminopentane + CO2
very low activity
-
-
?
L-lysine
1,5-diaminopentane + CO2
very low activity
-
-
?
L-lysine
1,5-diaminopentane + CO2
very low activity
-
-
?
L-lysine
1,5-diaminopentane + CO2
-
-
-
?
L-lysine
1,5-diaminopentane + CO2
-
-
?
L-lysine
1,5-diaminopentane + CO2
-
-
-
?
L-lysine
1,5-diaminopentane + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
L-lysine is a poor substrate for ODC, with a Km approximately 100fold higher than that of L-ornithine
-
-
?
L-Orn
?
-
first step in polyamine biosynthesis
-
-
?
L-Orn
?
-
key enzyme in polyamine metabolism
-
-
?
L-Orn
?
primary regulatory enzyme in polyamine biosynthesis
-
-
?
L-Orn
?
-
alteration in the key enzyme in the growth-associated pathway of polyamine biosynthesis may play a role in colon tumor progression
-
-
?
L-Orn
?
-
highly regulated enzyme of the polyamine pathway
-
-
?
L-Orn
?
-
key enzyme in polyamine metabolism
-
-
?
L-Orn
?
-
key enzyme in polyamine metabolism
-
-
?
L-Orn
?
-
key enzyme in polyamine metabolism
-
-
?
L-Orn
?
-
induced in mammary gland of fasted lactating rats by administration of 1,3-diaminopropan-2-ol
-
-
?
L-Orn
?
-
key enzyme in polyamine metabolism
-
-
?
L-Orn
?
-
key enzyme in polyamine metabolism
-
-
?
L-Orn
?
-
first step in polyamine biosynthesis
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
4002, 4008, 4009, 4010, 4013, 4016, 4022, 4024, 4025, 4027, 4035, 4045, 4051 -
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
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
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
a key enzymes in polyamine synthesis, putrescin formation leads subsequently to spermidine and spermine
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
ornithine decarboxylase, the first and rate-limiting enzyme in the polyamine biosynthetic pathway, is a highly regulated enzyme
-
-
?
L-ornithine
putrescine + CO2
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
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
677292, 677508, 677616, 677922, 679273, 680217, 680257, 681723, 681869, 682982, 690809, 695299, 696119, 696956, 697101, 697104, 697111, 699928, 699929, 699934, 707923, 708645, 708798, 709568, 714920 -
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
first enzyme in polyamine biosynthesis, the unique and tight regulation of the enzyme occurs at the levels of transcription, translation and protein degradation, dysregulation of ornithine decarboxylase during oncogenic transformation 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
-
L-arginine reduces cell proliferation and ornithine decarboxylase activity in patients with colorectal adenoma and adenocarcinoma, overview
-
-
?
L-ornithine
putrescine + CO2
ODC is the first committed enzyme in the polyamine biosynthesis pathway
-
-
?
L-ornithine
putrescine + CO2
-
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
-
ODC is the initial and rate-limiting enzyme in polyamine biosynthesis
-
-
?
L-ornithine
putrescine + CO2
-
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
-
the enzyme is involved in polyamine biosynthesis, the enzyme is increased in cancer cells
-
-
?
L-ornithine
putrescine + CO2
-
rate-limiting enzyme in polyamine biosynthesis
-
-
?
L-ornithine
putrescine + CO2
-
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
-
ODC is a key enzyme in mammalian polyamine biosynthesis that is up-regulated in various types of cancer
-
-
?
L-ornithine
putrescine + CO2
-
Odc is the first and rate-limiting enzyme of polyamine biosynthesis
-
-
?
L-ornithine
putrescine + CO2
-
ODC is the first rate-limiting enzyme in the polyamine biosynthesis pathway
-
-
?
L-ornithine
putrescine + CO2
-
ODC is the rate-limiting enzyme in polyamine biosynthesis
-
-
?
L-ornithine
putrescine + CO2
-
ODC is the rate-limiting enzyme in polyamine biosynthesis that decarboxylates ornithine to putrescine
-
-
?
L-ornithine
putrescine + CO2
-
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
-
-
-
-
?
L-ornithine
putrescine + CO2
very low activity
-
-
?
L-ornithine
putrescine + CO2
very low activity
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
-
?
L-ornithine
putrescine + CO2
-
ODC is the first committed enzyme in the polyamine biosynthesis pathway
-
-
?
L-ornithine
putrescine + CO2
-
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
-
-
-
-
?
L-ornithine
putrescine + CO2
-
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
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
677508, 680214, 680257, 697094, 708244, 708546, 708797, 709519, 709568, 710340, 713681, 713718, 713733, 714920, 749065 -
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
enzyme regulation, overview, ODC initiates the polyamine biosynthetic pathway, rapid turnover of ODC is brought about by the 26S proteasome, the structure of the COOH-terminal region needed for rapid degradation, ubiquitination is not required for this degradation, antizyme increases the degradation of ODC by enhancing its interaction with the proteasome but does not increase the rate of proteasomal processing, role of ODC and antizyme in carcinogenesis, overview
-
-
?
L-ornithine
putrescine + CO2
-
first enzyme in polyamine biosynthesis, the unique and tight regulation of the enzyme occurs at the levels of transcription, translation and protein degradation, dysregulation of ornithine decarboxylase during oncogenic transformation, mechanisms and therapeutic potential, overview, ODC induction as a necessary step in MEK-induced tumorigenesis, enzyme inhibition reduces tumor growth, synergistic or additive effects with vindesine or doxorubicin, overview
-
-
?
L-ornithine
putrescine + CO2
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
-
Cys360 plays an essential role in ensuring correct protonation of the decarboxylated reaction intermediate at Calpha
-
-
?
L-ornithine
putrescine + CO2
-
key rate-limiting enzyme in polyamine biosynthesis, elevated levels of ODC and polyamines stimulate proliferation of keratinocytes
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
the enzyme is involved in putrescine biosynthesis, diurnal changes in enzyme activity and polyamine contents in leaves, overview
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
the enzyme is speciic for L-ornithine
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
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
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
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
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
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
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
677508, 680257, 685991, 697101, 697772, 707088, 708412, 709568, 709804, 709921, 710168 -
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
first enzyme in polyamine biosynthesis, the unique and tight regulation of the enzyme occurs at the levels of transcription, translation and protein degradation, dysregulation of ornithine decarboxylase during oncogenic transformation 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
-
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
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
the enzyme is involved in the polyamine pathway
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
the enzyme is involved in the polyamine pathway
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
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
-
-
-
-
?
L-ornithine
putrescine + CO2
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
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
-
-
-
?
L-ornithine
putrescine + CO2
-
ODC activity increases abruptly in growing callus entire cells after 8 h, no change of activity in chloroplast
-
?
additional information
?
-
-
the Arabidopsis rpS15 polypeptide interacts specifically with plant ODC
-
-
?
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
?
-
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
?
-
-
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
?
-
-
enzyme activity detection using radioactive-labeled substrate
-
-
?
additional information
?
-
no activity using arginine and lysine as substrates
-
-
?
additional information
?
-
-
no activity using arginine and lysine as substrates
-
-
?
additional information
?
-
no activity with D-ornithine
-
-
?
additional information
?
-
-
no activity with D-ornithine
-
-
?
additional information
?
-
no substrates: lysine, arginine
-
-
?
additional information
?
-
-
no substrates: lysine, arginine
-
-
?
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
?
-
-
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
?
-
-
curcumin-induced apoptosis occurs through a mechanism of down-regulating ODC and along a ROS-dependent mitochondria-mediated pathway
-
-
?
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
?
-
-
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, 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
?
-
no substrate: L-arginine
-
-
?
additional information
?
-
no substrate: L-arginine
-
-
?
additional information
?
-
no substrate: L-arginine
-
-
?
additional information
?
-
no substrate: L-arginine
-
-
?
additional information
?
-
-
ODC degradation is not triggered by ubiquitination, the polyamines induce the degradation of ODC by affecting the synthesis of antizyme
-
-
?
additional information
?
-
Leishmania donovani ODC has a very fast turnover in mammalian cells, but is a stable enzyme
-
-
?
additional information
?
-
-
Leishmania donovani ODC has a very fast turnover in mammalian cells, but is a stable enzyme
-
-
?
additional information
?
-
-
ODC degradation is not triggered by ubiquitination, the polyamines induce the degradation of ODC by affecting the synthesis of antizyme
-
-
?
additional information
?
-
no substrate: L-arginine
-
-
?
additional information
?
-
no substrates: 2,4-diaminobutanoate, arginine
-
-
?
additional information
?
-
-
no substrates: 2,4-diaminobutanoate, arginine
-
-
?
additional information
?
-
-
the genes encoding the isozymes are involved in putrescine formation, which is an indicator of food process deterioration
-
-
?
additional information
?
-
circadian variations in ODC activity in female and male mice, influence of sex hormones, overview
-
-
?
additional information
?
-
-
circadian variations in ODC activity in female and male mice, influence of sex hormones, overview
-
-
?
additional information
?
-
-
the Raf/MEK/ERK pathway is involved in the regulation of ODC during skin tumorigenesis, overview
-
-
?
additional information
?
-
-
NAD(P)H quinone oxidoreductase binds to the enzyme and stabilizes it, this interaction is disrupted with dicoumarol, it sensitizes ODC monomers to degradation by the 20S proteasome in a manner independent of both antizyme and ubiquitin, overview
-
-
?
additional information
?
-
mouse ODC is quickly degraded by the 26S proteasome in an ubiquitin-dependent manner in mammalian and fungal cells. Within cODC, Cys441 functions as a proteasome association element, while the C-terminal end of cODC initiates entry into the proteasome
-
-
?
additional information
?
-
-
mouse ODC is quickly degraded by the 26S proteasome in an ubiquitin-dependent manner in mammalian and fungal cells. Within cODC, Cys441 functions as a proteasome association element, while the C-terminal end of cODC initiates entry into the proteasome
-
-
?
additional information
?
-
-
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 enzyme cannot decarboxylate L-lysine
-
-
?
additional information
?
-
no substrate: L-arginine
-
-
?
additional information
?
-
no substrate: L-arginine
-
-
?
additional information
?
-
-
bifunctional enzyme having both ODC and AdoMetDC, i.e. EC4.1.1.50, activity
-
?
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
?
-
-
the Raf/MEK/ERK pathway is involved in the regulation of ODC during skin tumorigenesis, 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
?
-
-
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 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
?
-
-
yeast antizyme mediates degradation of yeast ornithine decarboxylase by yeast but not by mammalian proteasome, overview
-
-
?
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
?
-
-
the enzyme shows ODC activity
-
-
?
additional information
?
-
-
the enzyme shows ODC activity
-
-
?
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 degradation is not triggered by ubiquitination, the polyamines induce the degradation of ODC by affecting the synthesis of antizyme
-
-
?
additional information
?
-
-
ODC degradation is catalyzed by the 26S proteasome without prior polyubiquitination
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5alpha-dihydrotestosterone
?
-
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
-
-
?
L-ornithine
putrescine + CO2
additional information
?
-
L-Orn
?
-
first step in polyamine biosynthesis
-
-
?
L-Orn
?
-
key enzyme in polyamine metabolism
-
-
?
L-Orn
?
primary regulatory enzyme in polyamine biosynthesis
-
-
?
L-Orn
?
-
alteration in the key enzyme in the growth-associated pathway of polyamine biosynthesis may play a role in colon tumor progression
-
-
?
L-Orn
?
-
highly regulated enzyme of the polyamine pathway
-
-
?
L-Orn
?
-
key enzyme in polyamine metabolism
-
-
?
L-Orn
?
-
key enzyme in polyamine metabolism
-
-
?
L-Orn
?
-
key enzyme in polyamine metabolism
-
-
?
L-Orn
?
-
induced in mammary gland of fasted lactating rats by administration of 1,3-diaminopropan-2-ol
-
-
?
L-Orn
?
-
key enzyme in polyamine metabolism
-
-
?
L-Orn
?
-
key enzyme in polyamine metabolism
-
-
?
L-Orn
?
-
first step in polyamine biosynthesis
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
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
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
a key enzymes in polyamine synthesis, putrescin formation leads subsequently to spermidine and spermine
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
ornithine decarboxylase, the first and rate-limiting enzyme in the polyamine biosynthetic pathway, is a highly regulated enzyme
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
677616, 680217, 680257, 681723, 690809, 696956, 699928, 707923, 708645, 708798, 709568 -
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
first enzyme in polyamine biosynthesis, the unique and tight regulation of the enzyme occurs at the levels of transcription, translation and protein degradation, dysregulation of ornithine decarboxylase during oncogenic transformation 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
-
L-arginine reduces cell proliferation and ornithine decarboxylase activity in patients with colorectal adenoma and adenocarcinoma, overview
-
-
?
L-ornithine
putrescine + CO2
ODC is the first committed enzyme in the polyamine biosynthesis pathway
-
-
?
L-ornithine
putrescine + CO2
-
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
-
ODC is the initial and rate-limiting enzyme in polyamine biosynthesis
-
-
?
L-ornithine
putrescine + CO2
-
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
-
the enzyme is involved in polyamine biosynthesis, the enzyme is increased in cancer cells
-
-
?
L-ornithine
putrescine + CO2
-
rate-limiting enzyme in polyamine biosynthesis
-
-
?
L-ornithine
putrescine + CO2
-
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
-
ODC is a key enzyme in mammalian polyamine biosynthesis that is up-regulated in various types of cancer
-
-
?
L-ornithine
putrescine + CO2
-
Odc is the first and rate-limiting enzyme of polyamine biosynthesis
-
-
?
L-ornithine
putrescine + CO2
-
ODC is the first rate-limiting enzyme in the polyamine biosynthesis pathway
-
-
?
L-ornithine
putrescine + CO2
-
ODC is the rate-limiting enzyme in polyamine biosynthesis
-
-
?
L-ornithine
putrescine + CO2
-
ODC is the rate-limiting enzyme in polyamine biosynthesis that decarboxylates ornithine to putrescine
-
-
?
L-ornithine
putrescine + CO2
-
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
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
-
?
L-ornithine
putrescine + CO2
-
ODC is the first committed enzyme in the polyamine biosynthesis pathway
-
-
?
L-ornithine
putrescine + CO2
-
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
-
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
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
enzyme regulation, overview, ODC initiates the polyamine biosynthetic pathway, rapid turnover of ODC is brought about by the 26S proteasome, the structure of the COOH-terminal region needed for rapid degradation, ubiquitination is not required for this degradation, antizyme increases the degradation of ODC by enhancing its interaction with the proteasome but does not increase the rate of proteasomal processing, role of ODC and antizyme in carcinogenesis, overview
-
-
?
L-ornithine
putrescine + CO2
-
first enzyme in polyamine biosynthesis, the unique and tight regulation of the enzyme occurs at the levels of transcription, translation and protein degradation, dysregulation of ornithine decarboxylase during oncogenic transformation, mechanisms and therapeutic potential, overview, ODC induction as a necessary step in MEK-induced tumorigenesis, enzyme inhibition reduces tumor growth, synergistic or additive effects with vindesine or doxorubicin, overview
-
-
?
L-ornithine
putrescine + CO2
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
-
key rate-limiting enzyme in polyamine biosynthesis, elevated levels of ODC and polyamines stimulate proliferation of keratinocytes
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
the enzyme is involved in putrescine biosynthesis, diurnal changes in enzyme activity and polyamine contents in leaves, overview
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
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
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
-
?
L-ornithine
putrescine + CO2
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
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
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
first enzyme in polyamine biosynthesis, the unique and tight regulation of the enzyme occurs at the levels of transcription, translation and protein degradation, dysregulation of ornithine decarboxylase during oncogenic transformation 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
-
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
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
the enzyme is involved in the polyamine pathway
-
-
?
L-ornithine
putrescine + CO2
the enzyme is involved in the polyamine pathway
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
involved in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
-
?
L-ornithine
putrescine + CO2
-
first step in polyamine biosynthesis
-
?
L-ornithine
putrescine + CO2
-
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
-
ODC is a key enzyme in the polyamine biosynthetic pathway
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
-
-
-
?
L-ornithine
putrescine + CO2
-
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
-
ODC activity increases abruptly in growing callus entire cells after 8 h, no change of activity in chloroplast
-
?
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
?
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
curcumin-induced apoptosis occurs through a mechanism of down-regulating ODC and along a ROS-dependent mitochondria-mediated pathway
-
-
?
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
?
-
-
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, 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
?
-
-
ODC degradation is not triggered by ubiquitination, the polyamines induce the degradation of ODC by affecting the synthesis of antizyme
-
-
?
additional information
?
-
Leishmania donovani ODC has a very fast turnover in mammalian cells, but is a stable enzyme
-
-
?
additional information
?
-
-
Leishmania donovani ODC has a very fast turnover in mammalian cells, but is a stable enzyme
-
-
?
additional information
?
-
-
ODC degradation is not triggered by ubiquitination, the polyamines induce the degradation of ODC by affecting the synthesis of antizyme
-
-
?
additional information
?
-
-
the genes encoding the isozymes are involved in putrescine formation, which is an indicator of food process deterioration
-
-
?
additional information
?
-
circadian variations in ODC activity in female and male mice, influence of sex hormones, overview
-
-
?
additional information
?
-
-
circadian variations in ODC activity in female and male mice, influence of sex hormones, overview
-
-
?
additional information
?
-
-
the Raf/MEK/ERK pathway is involved in the regulation of ODC during skin tumorigenesis, overview
-
-
?
additional information
?
-
mouse ODC is quickly degraded by the 26S proteasome in an ubiquitin-dependent manner in mammalian and fungal cells. Within cODC, Cys441 functions as a proteasome association element, while the C-terminal end of cODC initiates entry into the proteasome
-
-
?
additional information
?
-
-
mouse ODC is quickly degraded by the 26S proteasome in an ubiquitin-dependent manner in mammalian and fungal cells. Within cODC, Cys441 functions as a proteasome association element, while the C-terminal end of cODC initiates entry into the proteasome
-
-
?
additional information
?
-
-
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
?
-
-
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
?
-
-
the Raf/MEK/ERK pathway is involved in the regulation of ODC during skin tumorigenesis, 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
?
-
-
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 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
?
-
-
yeast antizyme mediates degradation of yeast ornithine decarboxylase by yeast but not by mammalian proteasome, overview
-
-
?
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
?
-
-
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 degradation is not triggered by ubiquitination, the polyamines induce the degradation of ODC by affecting the synthesis of antizyme
-
-
?
additional information
?
-
-
ODC degradation is catalyzed by the 26S proteasome without prior polyubiquitination
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(-)-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
1,4-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
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-difluoromethylornithine
DFMO, is used in therapy combined with MQT 1426, a polyamine transport inhibitor, for treatment of squamous cell carcinoma in a mouse model, K6/ODC
2-phenylethyl carbamimidothioate
-
3-(morpholin-4-ylmethyl)-1H-indole
-
4,4'-[pentane-1,5-diylbis(oxy)]dibenzenecarboximidamide
-
5,5'-dithiobis(2-nitrobenzoic acid)
5-Hydrazino-ornithine
-
competitive
alpha-difluoromethylornithine
alpha-difluoroornithine
-
-
alpha-DL-difluoromethylornithine
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.
-
Antizyme1
AZ1, molecular basis for the inactivation of ODC by AZ1, analysis of the interactions between ODC and AZ1, overview. The ODC-cAZ1 complex forms a heterodimer, which consists of one ODC monomer and one AZ1 molecule, AZ1 is embedded into a concave surface formed between the N- and C-domains of ODC. Binding of the truncated cAZ1 to ODC occludes the binding of a second molecule of ODC to form the active homodimer, thus the substrate binding site is disrupted and ODC is inactivated. The binding of cAZ1 to ODC causes a global conformational change of ODC and renders its C-terminal region flexible, therefore exposing this region for degradation by the 26S proteasome. AZ1 inhibits ODC activity, exhibits anti-tumor activities, and may be considered a tumor suppressor
-
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
-
Ca2+
-
0.9 mM, 50% inhibition
CGP54169A
-
0.000025 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
difluoro-methyl-ornithine
-
-
DL-alpha-difluoromethylarginine
-
reduces ODC activity by 24%
DL-alpha-difluoromethylornithine
DL-alpha-Monofluoromethylornithine
ethyl[dimethylaminopropyl]carbodiimide
geneticin
-
G418, weak non-competitive inhibition cs. L-ornithine
Isonicotinic acid hydrazide
-
-
K+
-
220 mM, 50% inhibition
L-2,4-diaminobutyrate
-
-
L-alpha-difluoromethylornithine
-
L-lysine
-
competitive inhibition
Ly-294002
-
a PI3K inhibitor
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
-
Mg2+
-
15 mM, 50% inhibition
Mn2+
-
1.0 mM, 50% inhibition
monofluoro-methyl-ornithine
-
-
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
-
-
Orn
-
inhibition of Lys decarboxylation
Ornithine decarboxylase antizyme
-
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
phosphopyridoxyl-histidine
-
phosphopyridoxyl-L-tryptophan methyl ester
-
phosphopyridoxyl-phenylalanine
-
propane-1,3-diyl dicarbamimidothioate
-
pyridoxyl-L-phenylalanine methyl ester
-
pyridoxyl-L-tryptophan methyl ester
-
S-nitrosoglutathione
-
inhibition likely via S-transnitrosation
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
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-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
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
agmatine
-
non-competitive
agmatine
1 mM, 77% inhibition
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
-
2 mM, 98% inhibition of ODC activity
alpha-difluoromethylornithine
DFMO, a suicide inhibitor, at 5 mM for 72 h, it inhibits membrane-associated ODC activity. Following exposure to alpha-DFMO, the putrescine content in the cells declineds, while the norspermidine content increases over 2fold. Partial inhibition of putrescine synthesis by alpha-DFMO results in increased norspermidine production in the cells suggesting that the suicide inhibitor may also act as an abiotic stress agent
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
irreversible inhibitor, a curative agent of West African sleeping sickness
alpha-difluoromethylornithine
-
-
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
-
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
-
an irreversible inhibitor of ODC, cannot recover MMP-9 activation following NF-kappaB inhibitor treatment in parental cells
alpha-difluoromethylornithine
-
-
alpha-difluoromethylornithine
-
irreversible inhibitor
alpha-difluoromethylornithine
-
an enzyme-activated irreversible inhibitor, effective sue to the slow turnover of the trypanosomatid enzyme
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
DFMO, specific inhibitor
alpha-difluoromethylornithine
-
an enzyme-activated irreversible inhibitor, effective sue to the slow turnover of the trypanosomatid enzyme
alpha-difluoromethylornithine
a suicide inhibitor of ODC
alpha-difluoromethylornithine
-
i.e. DFMO, irreversible inactivator, antitumor action of ODC inhibition using DFMO, chemopreventive effects, DFMO provides significant protection against N-butyl-N(4-hydroxybutyl)-nitrosamine-induced bladder cancer, overview
alpha-difluoromethylornithine
-
the enzyme is inhibited in the combination therapy with 2-difluoromethylornithine and a polyamine transport inhibitor MQT 1426, i.e. D-Lys-spermine, against squamous cell carcinoma, the apoptotic index of the cells is transiently increased by combination therapy but not by DFMO alone, a K6/ODC mouse model, overview
alpha-difluoromethylornithine
-
specific ODC inhibitor
alpha-difluoromethylornithine
-
irreversible and specific inhibitor of ODC
alpha-difluoromethylornithine
-
suicide inactivator of ODC
alpha-difluoromethylornithine
-
-
alpha-difluoromethylornithine
-
specific inhibitor
alpha-difluoromethylornithine
-
-
alpha-difluoromethylornithine
-
-
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
-
i.e. DFMO or eflornithine
alpha-difluoromethylornithine
-
specific and irreversible ODC inhibitor, complete inhibition at 0.1 mM
alpha-difluoromethylornithine
-
alpha-difluoromethylornithine
-
an enzyme-activated irreversible inhibitor, effective sue to the slow turnover of the trypanosomatid enzyme
alpha-difluoromethylornithine
-
an enzyme-activated irreversible inhibitor, effective sue to the slow turnover of the trypanosomatid enzyme
alpha-difluoromethylornithine
-
a highly specific suicide inhibitor of ODC causing complete, irreversible inhibition
alpha-DL-difluoromethylornithine
-
-
alpha-DL-difluoromethylornithine
-
irreversibel
alpha-DL-difluoromethylornithine
a medically used, irreversible inhibitor of ODC
alpha-DL-difluoromethylornithine
-
irreversibel; mechanism of irreversible inactivation
alpha-DL-difluoromethylornithine
-
experimental interruption of pregnancy in the mouse
alpha-DL-difluoromethylornithine
-
irreversibel
alpha-DL-difluoromethylornithine
-
irreversibel
alpha-DL-difluoromethylornithine
-
irreversibel
alpha-DL-difluoromethylornithine
-
-
alpha-DL-difluoromethylornithine
-
-
alpha-DL-difluoromethylornithine
-
irreversibel
alpha-DL-difluoromethylornithine
-
the nuclear enzyme is slightly more sensitive than the cytosolic
alpha-DL-difluoromethylornithine
-
-
alpha-DL-difluoromethylornithine
-
irreversibel
alpha-DL-difluoromethylornithine
-
-
alpha-DL-difluoromethylornithine
-
irreversibel
alpha-DL-difluoromethylornithine
-
-
alpha-Methylornithine
-
competitive
alpha-Methylornithine
-
reversible
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
-
non-competitive inhibitor protein isolated from Thermus thermophilus or Escherichia coli, almost complete inhibition at higer concentrations
-
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
-
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
-
an important endogenous regulator of ODC and polyamine homeostasis, overview, the wild type form of ODC has an extremely short half life of 20-30 min, and its degradation is mediated by antizyme, which binds to the monomeric form of ODC, preventing formation of the enzymatically active homodimer, and then targets ODC for degradation
-
antizyme
-
there are multiple antizyme genes with at least four members, all members, which are localized in different compartments or tissue, inhibit ODC activity, overview, the antizyme inhibitor blocks the effects of antizyme on the enzyme, overview
-
antizyme
-
role of ornithine decarboxylase antizyme inhibitor in vivo, ODC antizyme inhibitor, AZI, regulates ODC activity in cell cultures
-
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
-
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
-
non-competitive inhibitor protein isolated from Thermus thermophilus
-
antizyme
-
ODC antizyme, a polyamine-induced protein, binds ODC, serving to inhibit ODC activity and to promote proteasome-mediated ODC degradation
-
cadaverine
-
-
cadaverine
1 mM, 46% inhibition
CGP52622A
-
3-amino-oxy-1-propanamine analog, 0.00006 mM, 50% inhibition of recombinant Pf-Hinge-ODC
CGP52622A
-
0.000064 mM, 50% inhibition
D-Orn
-
-
D-ornithine
-
1.5 mM, 50% inhibition
DL-alpha-difluoromethylornithine
DFMO, an irreversible suicide inhibitor. DFMO inhibits growth of endometrial cancer cells in vitro and DFMO treatment significantly reduces endometrial tumor growth in vivo
DL-alpha-difluoromethylornithine
-
DFMO, an irreversible suicide inhibitor
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
-
-
DL-alpha-Monofluoromethylornithine
-
-
DL-alpha-Monofluoromethylornithine
-
-
ethyl[dimethylaminopropyl]carbodiimide
1.0 mM, 54% inhibition
ethyl[dimethylaminopropyl]carbodiimide
1.0 mM, 52% inhibition
L-Arg
-
-
L-arginine
-
L-arginine reduces cell proliferation and ornithine decarboxylase activity in patients with colorectal adenoma and adenocarcinoma, overview
L-arginine
-
competitive inhibition
Lys
-
-
Lys
-
relatively ineffective
N-ethylmaleimide
0.01 mM, complete inhibition
N-ethylmaleimide
0.01 mM, 99% inhibition
Na+
-
300 mM, 50% inhibition
Ornithine decarboxylase antizyme
-
purification of the protein inhibitor
-
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
-
noncompetitive with respect to Orn, plays a role in the regulation of ornithine decarboxylase in mammary gland under physiological conditions
-
Phenylglyoxal
1.0 mM, 36% inhibition
Phenylglyoxal
1.0 mM, 71% inhibition
putrescine
-
-
putrescine
1 mM, 70% inhibition
putrescine
1 mM, 63% inhibition
putrescine
-
product inhibition
putrescine
-
no inhibition
putrescine
-
slight inhibition
Salicylaldehyde
1.0 mM, 98% inhibition
Salicylaldehyde
1.0 mM, 82% inhibition
spermidine
-
noncompetitive
spermidine
50% inhibition at 0.15 mM per l
spermidine
-
1 mM, 61% inhibition of recombinant-Hinge-ODC and 63% inhibition of recombinant PfODC
spermidine
-
no inhibition
spermidine
-
no inhibition
spermine
-
noncompetitive
additional information
-
Arabidopsis S15 ribosomal protein does not inhibit the enzymatic activity of the plant ODC
-
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
alpha-difluoromethylarginine, DFMA, a suicide inhibitor, does not inhibit the enzyme
-
additional information
-
alpha-difluoromethylarginine, DFMA, a suicide inhibitor, does not inhibit the enzyme
-
additional information
-
treatment of protozoan diseases by inhibitors of ornithine decarboxylase
-
additional information
-
not inhibited by alpha-difluoromethylornithine
-
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 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
-
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
enzyme from Entamoeba histolytica is resistant to the irreversible inhibitor of ornithine decarboxylases, a-difluoromethylornithine. crystallographic data
-
additional information
-
enzyme from Entamoeba histolytica is resistant to the irreversible inhibitor of ornithine decarboxylases, a-difluoromethylornithine. crystallographic data
-
additional information
stilbamine isethionate, up to 0.1 mM, shows no inhibition
-
additional information
-
stilbamine isethionate, up to 0.1 mM, shows no inhibition
-
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
-
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
-
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
-
ODC is degraded in an ubiquitin-independent manner mediated by antizyme 1
-
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
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
-
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
not inhibitory: alpha-difluoromethylornithine
-
additional information
-
not inhibitory: alpha-difluoromethylornithine
-
additional information
-
inhibition of ODC activity reverts the transformation of cells in vitro and reduces tumor growth
-
additional information
-
enzyme activity is not affected in secondary cell lines exposed to 872 MHz RF radiation, overview
-
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
-
radiation at 5 W/kg does not affect the enzyme activity or cell proliferation and caspase-3 activity in L-929 cells
-
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
MQT 1426 has no inhibitory effect on squamous cell carcinoma ODC activity nor does it enhance the inhibition by 2-difluoromethylornithine, but it reduces the polyamine levels in squamous cell carcinoma cells
-
additional information
-
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
-
ODC inhibition decreases putrescine levels, AdoMetDC inhibition decreases the levels of both spermidine and spermine
-
additional information
-
RR-methyl acetylenic putrescine has no significant effect
-
additional information
-
RR-methyl acetylenic putrescine has no significant effect
-
additional information
-
subcutaneous injection of 10 mg of dexamethasone/kg body weight decreases significantly the basal levels of lung ODC activity
-
additional information
-
inhibition of ODC activity reverts the transformation of cells in vitro and reduces tumor growth
-
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 inhibited by MAPK kinase, PKA, and PI3K inhibitors
-
additional information
-
hypoxia deminishes ODC expression
-
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
-
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
-
the enzyme is an important target for antitrypanosomal chemotherapy
-
additional information
-
treatment of protozoan diseases by inhibitors of ornithine decarboxylase
-
additional information
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3'-O-Methyl-GTP
-
stimulates
7-methyl-GTP
-
stimulates
adenosine
-
approx. 10fold activation of dephosphorylated ODC at 1 mM, approx. 2fold activation of native ODC
alpha,beta-methylene-GTP
-
stimulates
antizyme inhibitor 2
-
-
-
antizyme inhibitor AzI1
AzI1 stimulates ODC activity, polyamine uptake and growth rate of enzyme ODC. AzI saves ODC from Az-induced degradation and it increases polyamine uptake. Superiority of AzI1 to ODCp in inhibiting the Az-stimulated ODC degradation. AzI, likeODCp, is degraded in a ubiquitin-dependent manner, in a reaction that does not require either interaction with Az or the integrity of its C-terminus
-
ATP
-
approx. 10fold activation of dephosphorylated 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
GDP
-
reactivation of ODC at pH values above 7.0
GMP
-
approx. 10fold activation of dephosphorylated ODC at 1 mM, approx. 1.2fold activation of native ODC
Guanosine 5'-pentaphosphate
-
stimulates
guanosine 5'-tetraphosphate
-
stimulates
ODCp
ODC-related protein or ODC paralogue, another ODCp is suggested to function as antizyme, like AzI, showing ability to increase ODC activity and inhibit Az-stimulated ODC degradation in vitro. ODCp is indeed capable of negating Az functions, as reflected by its ability to increase ODC activity and polyamine uptake and by its ability to provide growth advantage in stably transfected cells. But ODCp is less potent than AzI1 in stimulating ODC activity, polyamine uptake, and growth rate. ODCp, like AzI, is degraded in a ubiquitin-dependent manner, in a reaction that does not require either interaction with Az or the integrity of its C-terminus. Its degradation is inhibited by inactivation of a thermosensitive ubiquitin-activating enzyme, E1. And Az inhibits ODCp degradation by interfering with its ubiquitination. Interaction with Az actually stabilizes ODCp by interfering with its ubiquitination. An ODCp chimaera containing the C-terminal degradation signal of ODC is still stabilized by Az. Superiority of AzI1 to ODCp in inhibiting the Az-stimulated ODC degradation because ODCp shows lower affinity towards Az (Az1 and Az3). Human ODCp is stably overexpressed in NIH 3T3-derived cells and in HEK-293 cells, either alone or together with Az1
-
ornithine decarboxylase paralogue
-
phosphoserine
-
2 mM, 1.5fold activation
progesterone
-
ODC activity gradually increases in the presence of progesterone
UTP
-
approx. 10fold activation of dephosphorylated ODC at 1 mM, approx. 2fold activation of native ODC
dithiothreitol
-
maximal activity in presence of 5 mM dithiothreitol
dithiothreitol
-
required
dithiothreitol
-
increases activity
dithiothreitol
-
increases activity
GTP
-
200% increase in enzyme activity in homogenates of whole pupae
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 dephosphorylated ODC at 1 mM, approx. 2.5fold activation of native ODC
ornithine decarboxylase paralogue
-
ornithine decarboxylase paralogue acts as a regulator of ODC activity and inhibits its proteasomal degradation
-
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
-
spermidine
1 mM, 211% activation
spermidine
-
2 mM, 40% activation
spermine
1 mM, 309% activation
spermine
-
2 mM, 140% activation
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
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
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
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
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
2,4-dichlorophenoxyacetic acid induces the enzyme, best at 0.025 mM
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
activation of ODC is related to tumor promotion and progression
-
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
-
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
-
trichostatin A induces ODC activity and cell death in cancer cells
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
expression of gene speF is ornithine-inducible
-
additional information
-
ODC induction, e.g. in response to the tumor promoter 12-O-tetradecanoylphorbol-13-acetate, is a necessary step in MEK-induced tumorigenesis, ODC is induced during carcinogenesis by a variety of oncogenic stimuli, overview
-
additional information
-
12-O-tetradecanoylphorobl-13-acetate induces expression of ODC
-
additional information
-
radiation at 5 W/kg does not affect the enzyme activity or cell proliferation and caspase-3 activity in L-929 cells
-
additional information
-
antizyme inhibitor has the ability to bind antizyme with higher affinity than ODC, in this manner, it prevents antizyme from binding and inhibiting ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
in the adult prostate, ornithine decarboxylase activity is androgen-dependent
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
light dramatically stimulates the activity of ornithine decarboxylase
-
additional information
-
ischemia increases ODC activity, overview
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
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
-
carbonate ions increase the ODC enzyme expression
-
additional information
-
the enzyme is induced by interleukines 4 and 13, the induction is decreased by MAPK kinase PKA and P3IK inhibitors
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
increased enzyme activity after wounding of the potatoe
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
additional information
-
antizyme inhibitors are homologs of ODC that have lost their decarboxylation activity but have retained their ability to bind the ODC inhibitor antizyme, in most cases even more tightly than ODC
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
epithelial carcinoma cells
brenda
-
a Balb/c mice-derived mouse cell line
brenda
-
brenda
-
-
brenda
sexual dimorphism of the enzyme in the adrenal
brenda
-
-
brenda
-
-
brenda
-
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
brenda
-
primary cells
brenda
-
melanoma cell line
brenda
-
muscularis and mucosa, healthy and ischemic, ischemia increases ODC activity
brenda
-
-
brenda
-
-
brenda
-
epithelial cells
brenda
-
-
brenda
-
breast cancer cell line
brenda
transcript levels are highest in buds and rolled leaves and lower in other organs
brenda
-
-
brenda
-
-
brenda
-
colon adenocarcinoma cell, enzyme activity decreases upon addition of L-arginine or L-methionine to growth medium
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
multiple enzyme forms in tumor cells
brenda
-
-
brenda
-
-
brenda
-
of healthy and ischemic bladder
brenda
endometrioid cell
brenda
-
-
brenda
-
-
brenda
normal immortalized endometrial epithelial cells
brenda
-
of young females, high activity
brenda
-
-
brenda
-
brenda
-
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
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
intestinal epithelial cells
brenda
-
-
brenda
-
primary
brenda
-
leukemia cell line
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
a colon carcinoma cell line
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
breast epithelial cell line
brenda
-
breast cancer cell line
brenda
-
breast cancer cell line
brenda
-
-
brenda
-
Helicobacter pylori-infected gastric mucosa, oral administation of Lactobacillus brevis induces a decrease in gastric enzyme activity and polyamine levels
brenda
-
-
brenda
-
-
brenda
CD11b+ myeloid cells and CD11b- nonmyeloid cells from the gastric lamina propria of mice infected with Helicobacter pylori premouse Sydney strain 1 (PMSS1) for 48 h
brenda
-
653-1
brenda
-
Odc1 is expressed predominantly in proliferating myoblasts
brenda
-
-
brenda
-
-
brenda
-
lung carcinoma cells
brenda
-
lung carcinoma cell line
brenda
-
-
brenda
-
-
brenda
-
MYCN-2 cell
brenda
-
neuroblastoma cell line
brenda
-
-
brenda
-
-
brenda
-
of young and adult females, highest activity found
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
prostate cancer cell line
brenda
-
prostatic carcinoma cell line
brenda
-
caused by the aphid Tetraneura ulmi L. in Siberian elm leaves
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
S180 cells
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
osteosarcoma cells
brenda
-
-
brenda
ODC1 is highly expressed in endometrial cancers, ncreased expression of ODC1 in late stage and in higher grade cancers
brenda
ODC1 is highly expressed in endometrial cancers
brenda
-
-
brenda
-
lung cancer cell line
brenda
-
lung carcinoma cells
brenda
-
brenda
-
from livers and spleens of BALB/c mice
brenda
-
from livers and spleens of BALB/c mice
-
brenda
-
-
brenda
-
post-mortem healthy and Alzheimers disease brains, altered subcellular localization of ornithine decarboxylase in Alzheimers disease brain, overview
brenda
-
-
brenda
-
-
brenda
-
embryogenic cultures
brenda
-
maximal activity in the middle and late log phases of growth
brenda
-
embroynic and non-embryonic
brenda
-
analysis of in vivo activity of ornithine decarboxylase in three different cell lines of Daucus carota, namely N1 (embryogenic), F1 (non-embryogenic), and O3 (habituated and non-embryogenic), during growth and somatic embryogenesis. The enzyme activity in the presence of various levels of auxin (2,4-dichlorophenoxy acetic acid) is highest during periods of active cell division. During somatic embryo development, the enzyme activity is highest during globular stage formation. Stage-specific activity of ODC, overview
brenda
colonic epithelial cells, the enzyme is expressed in ulcerative colitis and colitis-associated colon carcinogenesis
brenda
colonic epithelial cells
brenda
-
somatic
brenda
-
-
brenda
-
somatic
brenda
-
ornithine decarboxylase protein is expressed in the urogenital sinus (UGS) epithelium of the male and female embryo prior to prostate development, and expression continues in prostatic epithelial buds as they emerge from the UGS
brenda
-
ornithine decarboxylase protein is expressed in the urogenital sinus (UGS) epithelium of the male and female embryo prior to prostate development, and expression continues in prostatic epithelial buds as they emerge from the UGS
-
brenda
-
brenda
-
-
-
brenda
-
brenda
-
-
-
brenda
-
-
brenda
-
brenda
-
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
brenda
-
-
-
brenda
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
-
brenda
-
brenda
-
-
-
brenda
-
neonatal foreskin fibroblasts
brenda
-
-
brenda
-
-
brenda
relationship between expression level of the enzyme and mucosal proliferation, overview
brenda
-
relationship between expression level of the enzyme and mucosal proliferation, overview
-
brenda
-
positive nuclei in the junction
brenda
analysis of expression of the cancer-related protein ornithine decarboxylase (ODC) in nontransformed gastric mucosa, relationship between expression level of the enzyme and mucosal proliferation, overview
brenda
-
analysis of expression of the cancer-related protein ornithine decarboxylase (ODC) in nontransformed gastric mucosa, relationship between expression level of the enzyme and mucosal proliferation, overview
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
colon carcinoma cells
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
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
brenda
-
cervical carcinoma cells
brenda
-
a cervix cancer cell line
brenda
-
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
human acute myeloid leukemia cell, enzyme activity correlates with myeloid cell differentiation induced by retinoic acid treatment
brenda
-
-
brenda
-
of testosterone treated mouse. 13fold higher activity in male mice than that in females
brenda
-
2 enzyme forms
brenda
-
hyperplastic and hypertrophic kidney, 80- to 1000fold increase in enzyme activity
brenda
-
-
brenda
-
a fibroblast cell line
brenda
-
neuroblastoma cell line
brenda
-
a human NB cell line
brenda
transcript levels are highest in buds and rolled leaves and lower in other organs
brenda
-
diurnal changes in enzyme activity and polyamine contents, overview
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
one enzyme form in liver and Morris hepatoma 7777 cells
brenda
-
pretreated with thioacetamide
brenda
-
-
-
brenda
-
-
brenda
M1 and M2 macrophages, human colonic macrophages express increased ODC levels in active ulcerative colitis and Crohn's disease, colitis-associated dysplasia, and colitis-associated carcinogenesis
brenda
-
-
brenda
bone-marrow-derived macrophages
brenda
M1 and M2 macrophages
brenda
-
breast cancer cell line
brenda
-
a breast cancer cell line
brenda
-
-
brenda
-
overexpression of constitutively active Ras12V results in up to 20fold increase of enzyme activity due to increase in enzyme transcription and translation
brenda
-
brenda
-
-
-
brenda
-
-
brenda
-
brenda
-
from livers and spleens of BALB/c mice
brenda
-
from livers and spleens of BALB/c mice
-
brenda
-
-
brenda
-
ornithine decarboxylase protein is expressed in the epithelium of the ventral, dorsolateral and anterior lobes of the adult mouse prostate
brenda
-
ornithine decarboxylase protein is expressed in the epithelium of the ventral, dorsolateral and anterior lobes of the adult mouse prostate
-
brenda
-
developing
brenda
-
-
brenda
-
-
brenda
-
fluorescent location of ornithine decarboxylase employing derivatives of the specific inhibitor alpha-difluoromethylornithine, location of squamous cell carcinoma cells
brenda
-
-
brenda
-
brenda
-
-
-
brenda
-
-
brenda
-
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
-
-
brenda
-
-
brenda
-
-
-
brenda
additional information
-
ODC activity is higher in endosymbiont-bearing trypanosomatids than in aposymbiotic cells, but isolated endosymbionts do not display this enzyme activity
brenda
additional information
-
free and conjugated putrescine profiles in cell lines of Araucaria angustifolia with different embryogenic potential do not correlate with levels of ADC and ODC activity
brenda
additional information
both ODC transcript and protein are expressed at all stages of development and show high expression in prestalk/stalk cells
brenda
additional information
-
both ODC transcript and protein are expressed at all stages of development and show high expression in prestalk/stalk cells
brenda
additional information
-
cervix carcinoma cell line
brenda
additional information
-
ODC activity is elevated in tumor cells
brenda
additional information
-
ODC is overexpressed in a variety of cancer cells
brenda
additional information
-
the enzyme is increased in cancer cells
brenda
additional information
-
ODC is expressed in all types of cells
brenda
additional information
ornithine decarboxylase (ODC) is often overexpressed in cancers and contributes to polyamine-induced cell proliferation. Quantitative real-time PCR enzyme expression analysis in a validation cohort of 60 endometrial cancers, overview
brenda
additional information
-
ornithine decarboxylase (ODC) is often overexpressed in cancers and contributes to polyamine-induced cell proliferation. Quantitative real-time PCR enzyme expression analysis in a validation cohort of 60 endometrial cancers, overview
brenda
additional information
significantly higher growth of Leishmania donovani parasites in the presence of recombinant LdODC compared with the parasite culture in the absence of any stimulation of both promastigotes and amastigotes, although it is higher in amastigotes
brenda
additional information
-
significantly higher growth of Leishmania donovani parasites in the presence of recombinant LdODC compared with the parasite culture in the absence of any stimulation of both promastigotes and amastigotes, although it is higher in amastigotes
brenda
additional information
-
immunocytochemical localization of ornithine decarboxylase
brenda
additional information
-
autoradiographic localization
brenda
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
brenda
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
brenda
additional information
-
ornithine decarboxylase co-localizes with vimentin in the developing urogenital sinus. Immunohistochemic localization analysis, overview
brenda
additional information
-
ornithine decarboxylase co-localizes with vimentin in the developing urogenital sinus. Immunohistochemic localization analysis, overview
-
brenda
additional information
-
immunocytochemical localization of ornithine decarboxylase
brenda
additional information
immunohistochemic expression analysis of gene ODC, the ODC protein is detected mainly in the cytoplasm of the epithelial cells in all 3 groups of animals, i.e. unoperated rats, operated rats fed a normal diet, and operated rats given a carbonate-supplemented diet, also some stromal and inflammatory cells are positively stained, overview
brenda
additional information
-
immunohistochemic expression analysis of gene ODC, the ODC protein is detected mainly in the cytoplasm of the epithelial cells in all 3 groups of animals, i.e. unoperated rats, operated rats fed a normal diet, and operated rats given a carbonate-supplemented diet, also some stromal and inflammatory cells are positively stained, overview
brenda
additional information
-
immunohistochemic expression analysis of gene ODC, the ODC protein is detected mainly in the cytoplasm of the epithelial cells in all 3 groups of animals, i.e. unoperated rats, operated rats fed a normal diet, and operated rats given a carbonate-supplemented diet, also some stromal and inflammatory cells are positively stained, overview
-
brenda
additional information
-
ODC activity in healthy leaves is highest at the fully developed stage, while in aphid-damaged leaves, the enzyme activity is highest at the initial phase, especially in the helathy parts of the damaged leaves, and in the initial and fully developed stage in the damaged parts. In galls, the enzyme activity drops after the initial stage. Activity profile overview
brenda
additional information
-
during mitotic cell cycle, ODC exhibits two activity peaks, one at G1/S transition and the second during G2/M transition
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
ODC is the major route to polyamine formation in the Chlamydomonas CC-406 cell-wall mutant, in contrast to the preferential ADC route reported for Chlorella vulgaris, suggesting that significant species differences exist in biosynthetic pathways which modulate endogenous polyamine levels in green algae
evolution
-
ODC is the major route to polyamine formation in the Chlamydomonas CC-406 cell-wall mutant, in contrast to the preferential ADC route reported for Chlorella vulgaris, suggesting that significant species differences exist in biosynthetic pathways which modulate endogenous polyamine levels in green algae
-
malfunction
-
inhibition of ODC activity in C2C12 myoblasts by alpha-difluoromethylornithine decreases myoblast number by 40% and 66% following 48 and 72 h of treatment, respectively
malfunction
-
ODC inhibition is associated with an abnormal morphology of the actin cytoskeleton during cell spreading and migration
malfunction
-
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
both overexpression of DdODC and putrescine treatment result in inhibition of cell proliferation
malfunction
disruption of enzyme ODC function by inhibitors renders cells non-viable and causes embryonic lethality
malfunction
double knockdown of ODC1 and ADC, EC 4.1.1.19, (MAO-ODC1:ADC) results in two phenotypes of conceptuses (a or b): 33% of conceptuses appear to be morphologically and functionally normal (phenotype a) and 67% of the conceptuses present an abnormal morphology and functionality (phenotype b). Furthermore, MAO-ODC1:ADC (a) conceptuses have greater tissue concentrations of agmatine, putrescine, and spermidine than MAO control conceptuses, while AO-ODC1:ADC (b) conceptuses only have greater tissue concentrations of agmatine. Uterine flushes from ewes with MAO-ODC1:ADC (a) have greater amounts of arginine, aspartate, tyrosine, citrulline, lysine, phenylalanine, isoleucine, leucine, and glutamine, while uterine flushes of ewes with MAO-ODC1:ADC (b) conceptuses have lower amount of putrescine, spermidine, spermine, alanine, aspartate, glutamine, tyrosine, phenylalanine, isoleucine, leucine, and lysine. In vivo knockdown of translation of ODC1 and ADC mRNAs individually and in combination affects the abundance of polyamines in the uterine lumen
malfunction
-
inhibiting ornithine decarboxylase using DL-alpha-difluromethylornithine in urogenital sinus (UGS) organ culture blocks the induction of prostatic buds by androgens, and significantly decreases expression of key prostate transcription factor, Nkx3.1, by androgens. DL-alpha-Difluromethylornithine also significantly decreases the expression of developmental regulatory gene Notch1. Other genes implicated in prostatic development, including Sox9, Wif1 and Srd5a2, are unaffected by the inhibitor. Inhibiting ornithine decarboxylase using pharmacologic agents such as alpha-difluromethylornithine or ablating Odc1 using a genetic approach renders pregnant mice unable to carry pups to term
malfunction
myeloid-specific deletion of Odc (OdcDELTAmye) provokes a marked increase in the response of mouse bone marrow-derived macrophages to M1 stimuli including Helicobacter pylori, Citrobacter rodentium, or lipopolysaccharides plus IFN-gamma, and to increased expression of M1 genes
malfunction
myeloid-specific Odc deletion significantly increases gastric and colonic inflammation, respectively, and enhances M1 activation. Add-back of putrescine, the product of ODC, reverses the increased macrophage activation, indicating that ODC and putrescine are regulators of macrophage function. Odc-deficient macrophages have increased histone 3, lysine 4 (H3K4) monomethylation, and H3K9 acetylation, accompanied by decreased H3K9 di/trimethylation both in vivo and ex vivo in primary macrophages. These alterations in chromatin structure directly result in upregulated gene transcription, especially M1 gene expression. OdcDELTAmye mice have significantly increased histologic gastritis, but significantly decreased Helicobacter pylori burden after chronic infection. ODC deletion augments proinflammatory cytokine and chemokine production in vivo. ODC deletion in macrophages also enhances NLRP3-inflammasome activation. ODC deletion promotes histone modifications leading to euchromatin formation and transcription
malfunction
use of enzyme inhibitor alpha-difluoromethylornithine can reduce the activity of ornithine decarboxylase of Leishmannia donovani eliminating the parasite-induced immune suppression and inducing collateral host protective responses in visceral leishmaniasis. Inhibition of r-LdODC can direct the active IFN-c dominant immune responses necessary for parasite clearance in VL patients
malfunction
-
double knockdown of ODC1 and ADC, EC 4.1.1.19, (MAO-ODC1:ADC) results in two phenotypes of conceptuses (a or b): 33% of conceptuses appear to be morphologically and functionally normal (phenotype a) and 67% of the conceptuses present an abnormal morphology and functionality (phenotype b). Furthermore, MAO-ODC1:ADC (a) conceptuses have greater tissue concentrations of agmatine, putrescine, and spermidine than MAO control conceptuses, while AO-ODC1:ADC (b) conceptuses only have greater tissue concentrations of agmatine. Uterine flushes from ewes with MAO-ODC1:ADC (a) have greater amounts of arginine, aspartate, tyrosine, citrulline, lysine, phenylalanine, isoleucine, leucine, and glutamine, while uterine flushes of ewes with MAO-ODC1:ADC (b) conceptuses have lower amount of putrescine, spermidine, spermine, alanine, aspartate, glutamine, tyrosine, phenylalanine, isoleucine, leucine, and lysine. In vivo knockdown of translation of ODC1 and ADC mRNAs individually and in combination affects the abundance of polyamines in the uterine lumen
-
malfunction
-
inhibiting ornithine decarboxylase using DL-alpha-difluromethylornithine in urogenital sinus (UGS) organ culture blocks the induction of prostatic buds by androgens, and significantly decreases expression of key prostate transcription factor, Nkx3.1, by androgens. DL-alpha-Difluromethylornithine also significantly decreases the expression of developmental regulatory gene Notch1. Other genes implicated in prostatic development, including Sox9, Wif1 and Srd5a2, are unaffected by the inhibitor. Inhibiting ornithine decarboxylase using pharmacologic agents such as alpha-difluromethylornithine or ablating Odc1 using a genetic approach renders pregnant mice unable to carry pups to term
-
metabolism
-
ornithine decarboxylase is the rate-limiting enzyme of polyamine synthesis
metabolism
-
ODC is the rate-limiting enzyme in polyamine biosynthesis
metabolism
-
changes in the contents of plant biogenic amines (putrescine, cadaverine, spermidine, tryptamine, spermine and histamine) and key enzymes of their biosynthesis, i.e. lysine decarboxylase (LDC), tyrosine decarboxylase, and ornithine decarboxylase (ODC) in galls and other parts of Siberian elm (Ulmus pumila) leaves during the galling process caused by the aphid Tetraneura ulmi first instar larvae, overview
metabolism
murine ODC (ornithine decarboxylase) is quickly degraded by the 26S proteasome in mammalian and fungal cells. Its degradation is independent of ubiquitin but requires a degradation signal composed of residues 425-461 at the ODC C-terminus, cODC (the last 37 amino acids of the ODC C-terminus). The presence of two essential elements in the degradation signal: the first consists of cysteine and alanine at residues 441 and 442 respectively, the second element is the C-terminus distal to residue 442. It has little or no sequence specificity, but is intolerant of insertions or deletions that alter its span. Reducing conditions, which preclude all well-characterized chemical reactions of the Cys441 thiol, are essential for in vitro degradation. The degradative function of Cys441 does not involve its participation in chemical reaction, instead, it functions within a structural element for recognition by the 26S proteasome. Rattus norvegicus AZ1-stimulated ODC degradation is conducted in reticulocyte lysate. the thiol group of Cys441 must be maintained in a reduced state to act as a recognition signal for the 26S proteasome, and does not act as a bonding partner with other residues. Within cODC, Cys441 functions as a proteasome association element, while the C-terminal end of cODC initiates entry into the proteasome
metabolism
ornithine decarboxylase (ODC) catalyzes the first and rate-limiting step of polyamine biosynthesis in humans
metabolism
ornithine decarboxylase (ODC) degradation is stimulated by Az (antizyme), a polyamine-induced protein, which in turn is regulated by an ODC-related protein termed AzI (Az inhibitor)
metabolism
ornithine decarboxylase (ODC) is the first and rate-limiting enzyme in the biosynthesis pathway of polyamines. ODC decarboxylates ornithine to form putrescine, which is further converted to spermidine and spermine via the action of spermidine and spermine synthase, respectively. Mammalian antizyme (mAz) is a central element of a feedback circuit regulating cellular polyamines by accelerating ODC degradation and inhibiting polyamine uptake
metabolism
ornithine decarboxylase (ODC) is the rate-limiting enzyme for polyamine biosynthesis
metabolism
ornithine decarboxylase (ODC) is the rate-limiting enzyme for polyamine biosynthesis
metabolism
-
ornithine decarboxylase catalyzes the first and rate-limiting step in polyamine synthesis
metabolism
-
ornithine decarboxylase is a key enzyme in the biosynthesis of putrescine and thus polyamines
metabolism
putrescine is the major polyamine in both free (88%) and membrane-bound fractions (93%) in Chlamydomonas reinhardtii, while norspermidine is the next most abundant in these fractions accounting for 11% and 6%, respectively. Low levels of diaminopropane, spermidine and spermine are also observed although no cadaverine or norspermine are detected. Ornithine decarboxylase (ODC) activity is almost five times higher than arginine decarboxylase (ADC, EC 4.1.1.19) and is the major route of putrescine synthesis. Following exposure to ODC inhibitor alpha-DFMO, the putrescine content in the cells declines, while the norspermidine content increases over 2fold. Addition of norspermidine to cultures stimulates cell division mimicking the effects observed using alpha-DFMO and also reverses the inhibitory effects of cyclohexylamine on growth
metabolism
-
the enzyme ornithine decarboxylase (ODC) is involved in putrescine and polyamine biosynthesis
metabolism
-
ornithine decarboxylase (ODC) is the first and rate-limiting enzyme in the biosynthesis pathway of polyamines. ODC decarboxylates ornithine to form putrescine, which is further converted to spermidine and spermine via the action of spermidine and spermine synthase, respectively. Mammalian antizyme (mAz) is a central element of a feedback circuit regulating cellular polyamines by accelerating ODC degradation and inhibiting polyamine uptake
-
metabolism
-
ornithine decarboxylase catalyzes the first and rate-limiting step in polyamine synthesis
-
metabolism
-
putrescine is the major polyamine in both free (88%) and membrane-bound fractions (93%) in Chlamydomonas reinhardtii, while norspermidine is the next most abundant in these fractions accounting for 11% and 6%, respectively. Low levels of diaminopropane, spermidine and spermine are also observed although no cadaverine or norspermine are detected. Ornithine decarboxylase (ODC) activity is almost five times higher than arginine decarboxylase (ADC, EC 4.1.1.19) and is the major route of putrescine synthesis. Following exposure to ODC inhibitor alpha-DFMO, the putrescine content in the cells declines, while the norspermidine content increases over 2fold. Addition of norspermidine to cultures stimulates cell division mimicking the effects observed using alpha-DFMO and also reverses the inhibitory effects of cyclohexylamine on growth
-
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
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
enzyme can complement ornithine decarboxylase mutant in Saccharomyces cerevisiae
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 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
-
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
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 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 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
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
enzyme ODC is involved in polyamine biosynthesis and squamous cell carcinoma proliferation
physiological function
functional roles of ornithine decarboxylase and arginine decarboxylase (EC 4.1.1.19) during the peri-implantation period of pregnancy in sheep. Polyamines stimulate DNA transcription and mRNA translation for protein synthesis in trophectoderm cells, as well as proliferation and migration of cells. Therefore, they are essential for development and survival of conceptuses (embryo/fetus and placenta). The ovine conceptus produces polyamines via classical and non-classical pathways. In the classical pathway, arginine (Arg) is transformed into ornithine, which is then decarboxylated by ornithine decarboxylase (ODC1) to produce putrescine which is the substrate for the production of spermidine and spermine. In the non-classical pathway, Arg is converted to agmatine (Agm) by arginine decarboxylase (ADC), and Agm is converted to putrescine by agmatinase (AGMAT)
physiological function
-
human ornithine decarboxylase paralogue (ODC-like protein, ODCp or ODC paralogue), which has been suggested to function either as mammalian arginine decarboxylase, ADC, or ornithine decarboxylase, ODC, is actually an antizyme inhibitor but not an arginine or ornithine decarboxylase. Human ODCp is devoid of ODC catalytic activity. ODCp acts as a regulator of ODC activity and inhibits its proteasomal degradation. ODCp is degraded by ubiquitination like AZI (AZ inhibitor)
physiological function
-
in Araucaria angustifolia, polyamines can efficiently modulate early-somatic embryo formation
physiological function
ODC catalyzes the synthesis of putrescine from ornithine and is a rate-limiting enzyme in polyamine biosynthesis. The enzyme is involved in cell growth and its activity increases rapidly and markedly in regenerating liver after partial hepatectomy. Ornithine, which is a substrate of ODC, is a key metabolite in the urea cycle and the first precursor of the polyamine pathway, it increases progressively in the liver of partially hepatectomized rats, as a consequence of the increased flow of metabolites through the urea cycle. Polyamines, ODC-catalyzed products, play important roles in cell growth and differentiation due to the modification of proteins and are good substrates of transglutaminase 2 (TG2). TG2 and ornithine decarboxylase conversely regulate cell growth and differentiation, overview
physiological function
ODC is essential for trypanothione biosynthesis. Trypanothione is the major reduced thiol which is responsible for the modulation of the immune response and pathogenesis in visceral leishmaniasis (VL). Analysis of the host protective role of an anti-ODC CD4+ T cell response and anti-leishmanial MU function in VL patients, relationship between ornithine decarboxylase and the cellular immune response in VL patients, overview. Pivotal role for recombinant LdODC in causing strong immune suppression in a susceptible host. Recombinant LdODC-induced CD4+ and CD8+ T-cell responses, functional profiles and effects on IFN-gamma and interleukin-10 levels, overview
physiological function
Ornithine decarboxylase (ODC) and gamma-glutamylcysteine synthetase (GSH1) produce molecules that are direct precursors of trypanothione. Trypanosomatids present a unique mechanism for detoxification of peroxides that is dependent on trypanothione (bis-glutathionylspermidine)
physiological function
ornithine decarboxylase (ODC) catalyzes the first and rate-limiting step of polyamine biosynthesis in humans. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis. Excessive accumulation of polyamines has a cytotoxic effect on cells and elevated level of ODC activity is associated with cancer development. To maintain normal cellular proliferation, regulation of polyamine synthesis is imposed by Antizyme1 (AZ1). The expression of AZ1 is induced by a ribosomal frameshifting mechanism in response to increased intracellular polyamines. AZ1 regulates polyamine homeostasis by inactivating ODC activity and enhancing its degradation. ODC is indispensable because of its central role in polyamine biosynthesis, because the polyamine products play essential roles in normal cell growth and differentiation. The enzyme is degraded by the 26S proteasome. Ornithine decarboxylase inactivation by AZ1 leads to accelerated degradation
physiological function
ornithine decarboxylase (ODC) is a rate limiting enzyme in polyamine synthesis that decarboxylates ornithine to form the diamine putrescine. The enzyme is predominantly expressed in the prestalk/stalk cells of multicellular structures
physiological function
ornithine decarboxylase (ODC) is the first and rate-limiting enzyme in the biosynthesis pathway of polyamines. ODC decarboxylates ornithine to form putrescine
physiological function
ornithine decarboxylase (ODC) is the first enzyme in the polyamine biosynthesis pathway in mammalian cells
physiological function
Ornithine decarboxylase (ODC) is the key enzyme in polyamine synthesis and a regulator of cell proliferation. ODC enhances cell proliferation in the gastric mucosa
physiological function
ornithine decarboxylase (ODC) is the rate-limiting enzyme in polyamine biosynthesis and involved in the production of putrescine through the decarboxylation of ornithine. ODC is often overexpressed in cancerous tissues and contributes to cell proliferation and tumor growth through generation of increased polyamines including not only putrescine but also the higher-order polyamines spermidine and spermine. The ODC1 gene is a direct target of MYC and related MYCN and a bona fide oncogene that can transform cells. ODC1 expression in endometrial cancers is associated with shorter time to recurrence and decreased survival
physiological function
ornithine decarboxylase (ODC) is the rate-limiting enzyme in polyamine metabolism. Ornithine decarboxylase regulates M1 macrophage activation and mucosal inflammation via histone modifications. Macrophage-derived ODC is a critical regulator of M1 macrophage activation during both Helicobacter pylori and Citrobacter rodentium infection. ODC in macrophages tempers antimicrobial, M1 macrophage responses during bacterial infections through histone modifications and altered euchromatin formation, leading to the persistence and pathogenesis of these organisms. ODC-driven histone modifications are essential for alterations in M1 macrophage activation
physiological function
ornithine decarboxylase (ODC) is the regulatory enzyme in polyamine biosynthesis. Elevated ornithine decarboxylase activity promotes skin tumorigenesis by stimulating the recruitment of bulge stem cells but not via toxic polyamine catabolic metabolites (reactive oxygen species)
physiological function
polyamine biosynthesis begins with the production of the biogenic amine, putrescine, which is produced by the enzyme ornithine decarboxylase (ODC1). Ornithine decarboxylase (ODC) is the rate-limiting enzyme for polyamine biosynthesis and restricts M1 macrophage activation in gastrointestinal infections. Ornithine decarboxylase in macrophages exacerbates colitis and promotes colitis-associated colon carcinogenesis by impairing M1 immune responses, role of macrophage ODC in colonic epithelial-driven inflammation, overview. In both dextran sulfate sodium (DSS)-induced colitis and the azoxymethane (AOM)-DSS model of colitis-associated carcinogenesis, myeloid-selective loss of Odc reduces clinical disease and tumorigenesis, and this is linked to increases in the M1 response. Both an epithelial injury model and in associated carcinogenesis, M1 macrophage functions are beneficial, and ODC acts to impair this response
physiological function
polyamine biosynthesis begins with the production of the biogenic amine, putrescine, which is produced by the enzyme ornithine decarboxylase (ODC1). Ornithine decarboxylase (ODC) is the rate-limiting enzyme for polyamine biosynthesis and restricts M1 macrophage activation in gastrointestinal infections. Ornithine decarboxylase in macrophages exacerbates colitis and promotes colitis-associated colon carcinogenesis by impairing M1 immune responses, role of macrophage ODC in colonic epithelial-driven inflammation, overview. ODC regulates the mucosal pro-inflammatory response during acute colitis, contribution of epithelial-derived ODC to the development of dextran sulfate sodium-induced colitis
physiological function
-
the enzyme is active during growth and somatic embryogenesis and contributes to polyamine biosynthesis, its activity lead to putrescine and, subsequently, to spermidine and spermine formation
physiological function
-
the first and rate-limiting step in polyamine synthesis is catalyzed by the enzyme ornithine decarboxylase which is encoded by the gene Odc1. Ornithine decarboxylase catalyzes the conversion of L-ornithine to putrescine. Ornithine decarboxylase activity is required for prostatic budding in the developing mouse prostate. Odc1 and polyamines are required for androgens to exert their effect in mediating prostatic bud induction, and are required for the expression of a subset of prostatic developmental regulatory genes including Notch1 and Nkx3.1. Testosterone administered to castrated male mice restores prostate secretory activity, whereas administering testosterone and the ornithine decarboxylase inhibitor DL-alpha-difluromethylornithine (DFMO) to castrated males does not restore prostate secretory activity, suggesting that polyamines are required for androgens to exert their effects
physiological function
-
functional roles of ornithine decarboxylase and arginine decarboxylase (EC 4.1.1.19) during the peri-implantation period of pregnancy in sheep. Polyamines stimulate DNA transcription and mRNA translation for protein synthesis in trophectoderm cells, as well as proliferation and migration of cells. Therefore, they are essential for development and survival of conceptuses (embryo/fetus and placenta). The ovine conceptus produces polyamines via classical and non-classical pathways. In the classical pathway, arginine (Arg) is transformed into ornithine, which is then decarboxylated by ornithine decarboxylase (ODC1) to produce putrescine which is the substrate for the production of spermidine and spermine. In the non-classical pathway, Arg is converted to agmatine (Agm) by arginine decarboxylase (ADC), and Agm is converted to putrescine by agmatinase (AGMAT)
-
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
-
ornithine decarboxylase (ODC) is the first and rate-limiting enzyme in the biosynthesis pathway of polyamines. ODC decarboxylates ornithine to form putrescine
-
physiological function
-
the first and rate-limiting step in polyamine synthesis is catalyzed by the enzyme ornithine decarboxylase which is encoded by the gene Odc1. Ornithine decarboxylase catalyzes the conversion of L-ornithine to putrescine. Ornithine decarboxylase activity is required for prostatic budding in the developing mouse prostate. Odc1 and polyamines are required for androgens to exert their effect in mediating prostatic bud induction, and are required for the expression of a subset of prostatic developmental regulatory genes including Notch1 and Nkx3.1. Testosterone administered to castrated male mice restores prostate secretory activity, whereas administering testosterone and the ornithine decarboxylase inhibitor DL-alpha-difluromethylornithine (DFMO) to castrated males does not restore prostate secretory activity, suggesting that polyamines are required for androgens to exert their effects
-
physiological function
-
ornithine decarboxylase (ODC) is the regulatory enzyme in polyamine biosynthesis. Elevated ornithine decarboxylase activity promotes skin tumorigenesis by stimulating the recruitment of bulge stem cells but not via toxic polyamine catabolic metabolites (reactive oxygen species)
-
physiological function
-
ODC catalyzes the synthesis of putrescine from ornithine and is a rate-limiting enzyme in polyamine biosynthesis. The enzyme is involved in cell growth and its activity increases rapidly and markedly in regenerating liver after partial hepatectomy. Ornithine, which is a substrate of ODC, is a key metabolite in the urea cycle and the first precursor of the polyamine pathway, it increases progressively in the liver of partially hepatectomized rats, as a consequence of the increased flow of metabolites through the urea cycle. Polyamines, ODC-catalyzed products, play important roles in cell growth and differentiation due to the modification of proteins and are good substrates of transglutaminase 2 (TG2). TG2 and ornithine decarboxylase conversely regulate cell growth and differentiation, overview
-
physiological function
-
Ornithine decarboxylase (ODC) is the key enzyme in polyamine synthesis and a regulator of cell proliferation. ODC enhances cell proliferation in the gastric mucosa
-
physiological function
-
enzyme ODC is involved in polyamine biosynthesis and squamous cell carcinoma proliferation
-
physiological function
-
Ornithine decarboxylase (ODC) and gamma-glutamylcysteine synthetase (GSH1) produce molecules that are direct precursors of trypanothione. Trypanosomatids present a unique mechanism for detoxification of peroxides that is dependent on trypanothione (bis-glutathionylspermidine)
-
physiological function
-
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
-
additional information
enzyme residue Cys441 takes part in functionally significant side-chain interactions with an amino acid in this local neighbourhood. Cys441 is intolerant of positional change. Cys441 does not form an intramolecular disulfide bond
additional information
-
ODC in vivo activity varies with auxin concentration in the medium, overview
additional information
ODC secondary and tertiary structure homology modeling
additional information
-
ODC secondary and tertiary structure homology modeling
additional information
role of N-terminal extension in the enzyme protein, overview
additional information
-
role of N-terminal extension in the enzyme protein, overview
additional information
structural basis of ornithine decarboxylase inactivation and accelerated degradation by polyamine sensor Antizyme1
additional information
-
structural basis of ornithine decarboxylase inactivation and accelerated degradation by polyamine sensor Antizyme1
additional information
the stability of yODC in mammalian cells is not a result of the absence of a compatible Aantizyme Az or lack of a C-terminal-destabilizing signal found on the mammalian enzyme, but is rather a result of the inability of the mammalian proteasome to degrade yeast ODC. Overexpression of yAz in yeast cells results in polyamine depletion and growth inhibition mainly through inhibiting enzyme ODC
additional information
-
the stability of yODC in mammalian cells is not a result of the absence of a compatible Aantizyme Az or lack of a C-terminal-destabilizing signal found on the mammalian enzyme, but is rather a result of the inability of the mammalian proteasome to degrade yeast ODC. Overexpression of yAz in yeast cells results in polyamine depletion and growth inhibition mainly through inhibiting enzyme ODC
additional information
-
the stability of yODC in mammalian cells is not a result of the absence of a compatible Aantizyme Az or lack of a C-terminal-destabilizing signal found on the mammalian enzyme, but is rather a result of the inability of the mammalian proteasome to degrade yeast ODC. Overexpression of yAz in yeast cells results in polyamine depletion and growth inhibition mainly through inhibiting enzyme ODC
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C334A
mutation of a putative active site at the dimer interface, completely abolishes enzyme activity. Partial restoration of the enzyme activity is observed when inactive K57A and C334A mutants are mixed, confirming that the dimer is the active form
G361Y
mutation at dimer interface, abolishes enzyme activity and destabilizes the dimer
K157A
mutation at dimer interface, abolishes enzyme activity and destabilizes the dimer
K57A
mutation of a putative active site at the dimer interface, completely abolishes enzyme activity. Partial restoration of the enzyme activity is observed when inactive K57A and C334A mutants are mixed, confirming that the dimer is the active form
E165A
1.9fold increase in catalytic efficiency
E165G
1.8fold increase in catalytic efficiency
E165S
5.1fold increase in catalytic efficiency
E165T
36fold increase in catalytic efficiency
E165V
7.4fold increase in catalytic efficiency
I163A
2.4fold increase in catalytic efficiency
I163G
2.4fold increase in catalytic efficiency
I163S
4.7fold increase in catalytic efficiency
I163T
17.6fold increase in catalytic efficiency
I163T/E165T
62.5fold increase in catalytic efficiency
I163V
3.4fold increase in catalytic efficiency
I163V/E165V
22.7fold increase in catalytic efficiency
A124R/N125D/Q129D/E136V/V137D/M140E
-
mutant shows very little resistance to antizyme inhibition
G316A
-
the naturally occuring ODC G316A genotype is prognostic for colorectal adenoma recurrence and predicts efficacy of aspirin chemoprevention, genotyping, overview
K69A/C360A
-
site-directed mutagenesis, a dominant negative mutant
Q119H/A124R/N125D/E136V/V137D/M140E
-
mutant is moderately resistant to antizyme inhibition
Q119H/A124R/N125D/Q129D/E136V/M140E
-
mutant shows very little resistance to antizyme inhibition
Q119H/A124R/N125D/Q129D/E136V/V137D
-
mutant shows very little resistance to antizyme inhibition
Q119H/A124R/N125D/Q129D/E136V/V137D/M140E
-
mutations introduced to match the Trypanosoma brucei onithine decarboxylase protein sequence. Mutant is less sensitive to antizyme inhibition
Q119H/A124R/N125D/Q129D/V137D/M140E
-
mutant shows a pattern of inhibition similar to mutant Q119H/A124R/N125D/Q129D/E136V/V137D/M140E
Q119H/A124R/Q129D/E136V/V137D/M140E
-
mutant is moderately resistant to antizyme inhibition
Q119H/N125D/Q129D/E136V/V137D/M140E
-
mutant shows a pattern of inhibition similar to mutant Q119H/A124R/N125D/Q129D/E136V/V137D/M140E
Q119H/V137D
-
mutant is much less sensitive to antizyme inhibition than wild-type, pattern similar to mutant Q119H/A124R/N125D/Q129D/E136V/V137D/M140E
Q119H/V137D/M140E
-
mutant is much less sensitive to antizyme inhibition than wild-type, pattern similar to mutant Q119H/A124R/N125D/Q129D/E136V/V137D/M140E
G121Y
-
Gly121 is buried in the dimer-dimer interface, mutation of Gly121 into Tyr prevents association of dimers into dodecamers, G121Y shows similar activity as native ODC
A123S
-
mutation in a conserved residue of the antizyme-binding region, mutant is somehow more resistant to degradation than wild-type. About 130% of wild-type activity
C441A/A442C
site-directed mutagenesis, swapping the cysteine residue with either of the two adjacent residues stabilizes ODC, reducing degradation from 25% to less than 5% in each case
C441S
-
the isosteric alteration of the enzyme completely stabilizes ODC even in the presence of excess antizyme
C70S
-
mutant enzyme C70S has a 2fold increased Km-value
E138A
-
mutation in a conserved residue of the antizyme-binding region, mutant is degraded as efficientlyas wild-type. Almost complete loss of activity. Mutation diminishes the formation of enzyme dimers
E138A/L139S
-
mutation prevents the degradation by the proteasome, complete loss of activity. Mutation diminishes the formation of enzyme dimers
K115A
-
mutation in a conserved residue of the antizyme-binding region. About 30 of wild-type activity. Mutation diminishes the formation of enzyme dimers
K115A/K141A
-
degradation by the proteasome occurs with similar efficiency as for wild-type. About 10% of wild-type activity. Mutation diminishes the formation of enzyme dimers
K141A
-
mutation in a conserved residue of the antizyme-binding region. About 25% of wild-type activity
K69/C360A
-
expression in Mus musculus
K69A
-
mutant enzyme K69A shows a changed spectrum and a 550fold decrease in the turnover/Km value
L139A
-
mutation in a conserved residue of the antizyme-binding region, mutant is resistant to degradation. About 15% of wild-type activity. Mutation diminishes the formation of enzyme dimers
L139S
-
mutation in a conserved residue of the antizyme-binding region, mutant is resistant to degradation. Almost complete loss of activity
S440C/C441S
site-directed mutagenesis, swapping the cysteine residue with either of the two adjacent residues stabilizes ODC, reducing degradation from 25% to less than 5% in each case. The stabilization of ODC by the C441S mutation implies that the hydroxy group cannot replicate the functional properties of the thiol of Cys441
C115A
0.08% of wild-type activity
C338A
14% of wild-type L-ornithine decarboxylase activity
C377A
4% of wild-type L-ornithine decarboxylase activity
C96A
42% of wild-type L-ornithine decarboxylase activity
K95A
1% of wild-type L-ornithine decarboxylase activity
C1355A
-
8.7% of wild-type activity
D1356A
-
8% of wild-type activity
D1359A
-
3% of wild-type activity
S73A
-
no AdometDC, i.e. ec4.1.1.50, activity, 90% of wild-type ODC activity
C360A
-
2% of wild-type activity
C114A
59% of wild-type activity
C360S
0.1% of wild-type activity
D137A
103% of wild-type activity
D361A
33% of wild-type activity
D364E
the mutant shows almost no activity compared to the wild type enzyme
E36A
59% of wild-type activity
F170A
53% of wild-type activity
F400A
0.15% of wild-type activity
I291A
20% of wild-type activity
K141A
3% of wild-type activity
K169A
1% of wild-type activity
K69A
-
ODC copurifies with amines, e.g. putrescine, similar affinity for pyridoxal 5'-phosphate as wild-type
K69R
-
0.02% of wild-type activity, binds diamines and amino acids with higher affinity than wild-type ODC
L330A
29% of wild-type activity
L363A
36% of wild-type activity
N398A
3% of wild-type activity
Q116A
67% of wild-type activity
S395A
6% of wild-type activity
S396A
the mutant shows about 2fold increased activity compared to the wild type enzyme
T93A
61% of wild-type activity
V392A
10% of wild-type activity
W356A
17% of wild-type activity
Y317A
10% of wild-type activity
Y323A
0.4% of wild-type activity
Y331A
64% of wild-type activity
A457W
site-directed mutagenesis, the mutation does not stabilize ODC
A457W
site-directed mutagenesis, the mutation does not stabilize the enzyme
C360A
-
mutation C360A 26fold reduces the specificity constant and 2fold decreases the Km
C360A
-
mutant enzyme C360A is completely resistant to inactivation by (R,R)-delta-methyl-alpha-acetylenicputrescine and is much less sensitive than the wild type enzyme to alpha-monofluoromethyldehydromethylornithine
C441A
construction of a duplicated cODC, from fusing ODC to a tandem cODC-cODCC441A at its C-terminus, with the first ODC copy being wild-type including a wild-type Cys441, and the distal C-terminal copy of cODC carrying mutation C441A
C441A
site-directed mutagenesis, the mutation stabilizes the enzyme but also profoundly reduces its activity
S456A
site-directed mutagenesis, the mutation does not stabilize ODC
S456A
site-directed mutagenesis, the mutation does not stabilize the enzyme
C360A
2% of wild-type activity
C360A
3% of wild-type activity
F397A
0.6% of wild-type activity
F397A
0.3% of wild-type activity
K294A
8% of wild-type activity
K294A
mutation increases the disorder of residues Leu166 - Ala172 and increases the population of inactive conformations
additional information
construction of chimeric mutant enzymes consisting of sequence from the Crithidia fasciculata and the Leishmania donovani enzymes, e.g. exchanging the C-terminal PEST region, which show altered protein stability compared to the wild-type enzymes, overview
additional information
-
construction of chimeric mutant enzymes consisting of sequence from the Crithidia fasciculata and the Leishmania donovani enzymes, e.g. exchanging the C-terminal PEST region, which show altered protein stability compared to the wild-type enzymes, overview
additional information
enzyme overexpression in Dictyostelium discoideum cells inhibits cell proliferation and leads to mild developmental defect, because high putrescine levels are detrimental for cell proliferation, phenotype, overview
additional information
-
enzyme overexpression in Dictyostelium discoideum cells inhibits cell proliferation and leads to mild developmental defect, because high putrescine levels are detrimental for cell proliferation, phenotype, overview
additional information
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
additional information
-
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
additional information
-
adenovirus-mediated expression of both antisense ornithine decarboxylase and S-adenosylmethionine decarboxylase in A-549 cells injected into BALB/c nude male mice inhibits lung cancer cell growth in the mouse tumor, overview
additional information
-
ODC transgenic rodent models of skin carcinogenesis, phenotypes, overview
additional information
-
construction of transgenic mice expressing the human MYCN gene under the control of the rat tyrosine hydroxylase promoter, targeting ornithine decarboxylase impairs development of MYCN-amplified neuroblastoma
additional information
-
ornithine decarboxylase overexpression prevents TNF-alpha- and methotrexate-induced apoptosis via reduction of reactive oxygen species, e.g. in curcumin-induced apoptosis, ODC overexpression prevents cytochrome c release and the activation of caspase-9 and caspase-3 following curcumin treatment, overview
additional information
-
overexpression of ODC leads to restored MMP-9 secretion involving stimulation by TNF-alpha, and reduced MMP-9 activity and expression during macrophage-like differentiation
additional information
-
overexpression of ODC prevents apoptosis induced by tumor necrosis factor-alpha and methotrexate. ODC overexpressing cells seem to overcome the G1 arrest and G2/M arrest, caused by VP-16 and TAX, respectively, and keep on the cell cycle rolling. Overexpression of ODC increases the expression of Cyclin A, D, E and Cdk4 and the enzyme activity of Cdk1 and Cdk2 after the treatment of VP-16 and TAX, respectively
additional information
-
positive correlation between the level of ODC mRNA and the staging of tumors in MDA-MB-231 cells expressing an ODC antisense construct. Gene transfection of rAd-ODC/Ex3as markedly down-regulates expression of ODC and cyclin D1, resulting in suppression of proliferation and cell cycle arrest at G0-G1 phase, and the inhibition of colony formation, an anchorage-independent growth pattern, and the migratory ability of MDA-MB-231 cells. rAd-ODC/Ex3as also markedly reduces the concentration of putrescine, but not spermidine or spermine, in MDA-MB-231 cells
additional information
ODC paralogue ODCp-overexpressing cells display elevated ODC and polyamine uptake activity as compared with control cells
additional information
construction of chimeric mutant enzymes consisting of sequence from the Crithidia fasciculata and the Leishmania donovani enzymes, e.g. exchanging the C-terminal PEST region, which show altered protein stability compared to the wild-type enzymes, overview
additional information
-
construction of chimeric mutant enzymes consisting of sequence from the Crithidia fasciculata and the Leishmania donovani enzymes, e.g. exchanging the C-terminal PEST region, which show altered protein stability compared to the wild-type enzymes, overview
additional information
-
construction of conditionally lethal DELTAodc null mutants by double targeted gene replacement within a virulent strain. Parasitemias of DELTAodc null mutants are reduced by 6 and 3 orders of magnitude, respectively, in livers and spleens of BALB/c mice showing compromised infectivity phenotypes, overview. Nutritional phenotypes and Survival of DELTAodc parasites in peritoneal macrophages, overview
additional information
removal of the N-terminal extended region of LdODC results in improved stability of the protein, but the truncated enzyme LdODC does not show any activity
additional information
-
removal of the N-terminal extended region of LdODC results in improved stability of the protein, but the truncated enzyme LdODC does not show any activity
additional information
-
construction of conditionally lethal DELTAodc null mutants by double targeted gene replacement within a virulent strain. Parasitemias of DELTAodc null mutants are reduced by 6 and 3 orders of magnitude, respectively, in livers and spleens of BALB/c mice showing compromised infectivity phenotypes, overview. Nutritional phenotypes and Survival of DELTAodc parasites in peritoneal macrophages, overview
-
additional information
Leishmania guyanensis odc overexpressor cell lines are generated to investigate the contribution of the gene to the trivalent antimony (SbIII)-resistance phenotype. The ODC-overexpressors parasites present an increase of 2fold in SbIII-resistance index, when compared with the wild-type line. Pharmacological inhibition of ODC with the specific inhibitor alpha-difluoromethylornithine (DFMO) increases the antileishmanial effect of SbIII in all cell lines. Nevertheless the ODC-overexpressor is still more resistant to SbIII than the parental cell line
additional information
-
Leishmania guyanensis odc overexpressor cell lines are generated to investigate the contribution of the gene to the trivalent antimony (SbIII)-resistance phenotype. The ODC-overexpressors parasites present an increase of 2fold in SbIII-resistance index, when compared with the wild-type line. Pharmacological inhibition of ODC with the specific inhibitor alpha-difluoromethylornithine (DFMO) increases the antileishmanial effect of SbIII in all cell lines. Nevertheless the ODC-overexpressor is still more resistant to SbIII than the parental cell line
additional information
-
Leishmania guyanensis odc overexpressor cell lines are generated to investigate the contribution of the gene to the trivalent antimony (SbIII)-resistance phenotype. The ODC-overexpressors parasites present an increase of 2fold in SbIII-resistance index, when compared with the wild-type line. Pharmacological inhibition of ODC with the specific inhibitor alpha-difluoromethylornithine (DFMO) increases the antileishmanial effect of SbIII in all cell lines. Nevertheless the ODC-overexpressor is still more resistant to SbIII than the parental cell line
-
additional information
-
construction of enzyme overexpressing and enzyme-deficient transgenic mice, deletion of the 5 terminal residues 457-461 also stabilizes ODC but to a lesser extent than removing the terminal 37 residues or mutation of Cys441
additional information
-
transgenic mice overexpressing ODC in hair follicle keratinocytes using keratin promotors are much more sensitive than littermate controls to DMBA-induced carcinogenesis, and do not require treatment with a tumor promoter to develop tumors, overview
additional information
-
construction of ODC-overexpressing K6/ODC transgenic mice in which a keratin 6 promoter directs the expression of ODC to the outer root sheath cells of hair follicles in the skin. Although elevated levels of ODC and polyamines stimulate proliferation of keratinocytes, mutant Ker/ODC cells undergo apoptotic cell death within days of primary culture unlike wild-type Ker/Norm cells that continue to proliferate. Ker/ODC also displays increased generation of H2O2, acroleinlysine conjugates, and protein oxidation products as well as polyamine-dependent DNA damage, phenotype, overview
additional information
construction of several truncated enzyme mutants, mutant protein stabilities, overview
additional information
-
construction of several truncated enzyme mutants, mutant protein stabilities, overview
additional information
-
establishment of an embryonic stem cell clone with disrupted Azin1 gene by the gene trap technique, construction of a mutant mouse line using these trapped embryonic stem cells. Homozygous mutant mice die at P0 with abnormal liver morphology, deletion of Azin1 in homozygous mice results in the degradation of ODC, and reduced the biosynthesis of putrescine and spermidine, genotype and phenotype, overview
additional information
construction of myeloid-specific Odc deletion mutant mice (OdcDELTAmye). Increased mRNA expression of Nos2, Tnfa, Il1b, Il12a, Ccl5 and Cxcl10 is demonstrated in dextran sulfate sodium-treated OdcDELTAmye versus Odcfl/fl mice, while expression levels of the M2 markers, Arg1 and Chil3, are comparable in colonic tissues of dextran sulfate sodium-treated Odcfl/fl and OdcDELTAmye mice. OdcDELTAmye mice are protected from colitis-associated carcinogenesis
additional information
in ODC-ER transgenic mice, in which an involucrin promoter directs the expression of the inducible ODC cDNA fused in frame to a 4-hydroxytamoxifen (4OHT)-responsive mutant estrogen receptor ligand binding domain to the suprabasal epidermis, elevated expression of ornithine decarboxylase (ODC), the regulatory enzyme in polyamine biosynthesis, targeted to the epidermis is sufficient to promote skin tumor development following a single subthreshold dose of dimethylbenz(a)anthracene (DMBA). ODC-ER transgenic mice and their normal littermates have been backcrossed into either the FVB or C57Bl/6 background for at least 10 generations. An inducible Cre-activated bi-transgenic mouse system is used to track hair follicle bulge stem cells and their progeny. K15-CrePR1 transgenic mice, that express CrePR1 under the control of a keratin 15 (K15) promoter, are generated to target expression of genes to the adult epidermal stem cells located in the hair follicle bulge cells. K15-CrePR1 transgenic mice are crossed with Cre-responsive R26R transgenic mice, that express lacZ under the control of a ubiquitous promoter, after Cre-mediated removal of an inactivating sequence. The resulting K15-CrePR1-R26R bitransgenic mice are treated topically with RU486 to induce expression of lacZ in the bulge stem cells of the skin. Polyamine oxidase inhibitor MDL72527 is applied. MDL72527 treatment increases skin tumor growth and conversion to carcinomas in DMBA-initiated ODC-ER mice, overview
additional information
-
in ODC-ER transgenic mice, in which an involucrin promoter directs the expression of the inducible ODC cDNA fused in frame to a 4-hydroxytamoxifen (4OHT)-responsive mutant estrogen receptor ligand binding domain to the suprabasal epidermis, elevated expression of ornithine decarboxylase (ODC), the regulatory enzyme in polyamine biosynthesis, targeted to the epidermis is sufficient to promote skin tumor development following a single subthreshold dose of dimethylbenz(a)anthracene (DMBA). ODC-ER transgenic mice and their normal littermates have been backcrossed into either the FVB or C57Bl/6 background for at least 10 generations. An inducible Cre-activated bi-transgenic mouse system is used to track hair follicle bulge stem cells and their progeny. K15-CrePR1 transgenic mice, that express CrePR1 under the control of a keratin 15 (K15) promoter, are generated to target expression of genes to the adult epidermal stem cells located in the hair follicle bulge cells. K15-CrePR1 transgenic mice are crossed with Cre-responsive R26R transgenic mice, that express lacZ under the control of a ubiquitous promoter, after Cre-mediated removal of an inactivating sequence. The resulting K15-CrePR1-R26R bitransgenic mice are treated topically with RU486 to induce expression of lacZ in the bulge stem cells of the skin. Polyamine oxidase inhibitor MDL72527 is applied. MDL72527 treatment increases skin tumor growth and conversion to carcinomas in DMBA-initiated ODC-ER mice, overview
additional information
Odc knockdown in myeloid cells, generation of mutant mice with a myeloid-specific deletion of gene Odc, by crossing C57BL/6 Odcfl/fl mice with myeloid-specific LysMcre/cre driver mice, yielding the OdcDELTAmye mice
additional information
purified [35S]methionine-labeled recombinant His6-TEV (tobacco etch virus)-FLAG-ODC is generated and degraded in vitro
additional information
-
in ODC-ER transgenic mice, in which an involucrin promoter directs the expression of the inducible ODC cDNA fused in frame to a 4-hydroxytamoxifen (4OHT)-responsive mutant estrogen receptor ligand binding domain to the suprabasal epidermis, elevated expression of ornithine decarboxylase (ODC), the regulatory enzyme in polyamine biosynthesis, targeted to the epidermis is sufficient to promote skin tumor development following a single subthreshold dose of dimethylbenz(a)anthracene (DMBA). ODC-ER transgenic mice and their normal littermates have been backcrossed into either the FVB or C57Bl/6 background for at least 10 generations. An inducible Cre-activated bi-transgenic mouse system is used to track hair follicle bulge stem cells and their progeny. K15-CrePR1 transgenic mice, that express CrePR1 under the control of a keratin 15 (K15) promoter, are generated to target expression of genes to the adult epidermal stem cells located in the hair follicle bulge cells. K15-CrePR1 transgenic mice are crossed with Cre-responsive R26R transgenic mice, that express lacZ under the control of a ubiquitous promoter, after Cre-mediated removal of an inactivating sequence. The resulting K15-CrePR1-R26R bitransgenic mice are treated topically with RU486 to induce expression of lacZ in the bulge stem cells of the skin. Polyamine oxidase inhibitor MDL72527 is applied. MDL72527 treatment increases skin tumor growth and conversion to carcinomas in DMBA-initiated ODC-ER mice, overview
-
additional information
in vivo knockdown of translation of ODC1 and ADC (EC 4.1.1.19) mRNAs individually and in combination. Double knockdown of ODC1 and ADC (MAO-ODC1:ADC) results in two phenotypes (a or b) of conceptuses: 33% of conceptuses appear to be morphologically and functionally normal (phenotype a) and 67% of the conceptuses present an abnormal morphology and functionality (phenotype b). Furthermore, MAO-ODC1:ADC (a) conceptuses have greater tissue concentrations of agmatine, putrescine, and spermidine than MAO control conceptuses, while AO-ODC1:ADC (b) conceptuses only have greater tissue concentrations of agmatine. Uterine flushes from ewes with MAO-ODC1:ADC (a) have greater amounts of arginine, aspartate, tyrosine, citrulline, lysine, phenylalanine, isoleucine, leucine, and glutamine, while uterine flushes of ewes with MAO-ODC1:ADC (b) conceptuses have lower amount of putrescine, spermidine, spermine, alanine, aspartate, glutamine, tyrosine, phenylalanine, isoleucine, leucine, and lysine. Phenotypes, overview
additional information
-
in vivo knockdown of translation of ODC1 and ADC (EC 4.1.1.19) mRNAs individually and in combination. Double knockdown of ODC1 and ADC (MAO-ODC1:ADC) results in two phenotypes (a or b) of conceptuses: 33% of conceptuses appear to be morphologically and functionally normal (phenotype a) and 67% of the conceptuses present an abnormal morphology and functionality (phenotype b). Furthermore, MAO-ODC1:ADC (a) conceptuses have greater tissue concentrations of agmatine, putrescine, and spermidine than MAO control conceptuses, while AO-ODC1:ADC (b) conceptuses only have greater tissue concentrations of agmatine. Uterine flushes from ewes with MAO-ODC1:ADC (a) have greater amounts of arginine, aspartate, tyrosine, citrulline, lysine, phenylalanine, isoleucine, leucine, and glutamine, while uterine flushes of ewes with MAO-ODC1:ADC (b) conceptuses have lower amount of putrescine, spermidine, spermine, alanine, aspartate, glutamine, tyrosine, phenylalanine, isoleucine, leucine, and lysine. Phenotypes, overview
additional information
-
in vivo knockdown of translation of ODC1 and ADC (EC 4.1.1.19) mRNAs individually and in combination. Double knockdown of ODC1 and ADC (MAO-ODC1:ADC) results in two phenotypes (a or b) of conceptuses: 33% of conceptuses appear to be morphologically and functionally normal (phenotype a) and 67% of the conceptuses present an abnormal morphology and functionality (phenotype b). Furthermore, MAO-ODC1:ADC (a) conceptuses have greater tissue concentrations of agmatine, putrescine, and spermidine than MAO control conceptuses, while AO-ODC1:ADC (b) conceptuses only have greater tissue concentrations of agmatine. Uterine flushes from ewes with MAO-ODC1:ADC (a) have greater amounts of arginine, aspartate, tyrosine, citrulline, lysine, phenylalanine, isoleucine, leucine, and glutamine, while uterine flushes of ewes with MAO-ODC1:ADC (b) conceptuses have lower amount of putrescine, spermidine, spermine, alanine, aspartate, glutamine, tyrosine, phenylalanine, isoleucine, leucine, and lysine. Phenotypes, overview
-
additional information
enzyme activity is reduced up to 95% when the deletion of a parasite-specific insert occurs within the respective domain. Inserts mediate specific physical interactions between the two domains of the bifunctional enzyme that are essential for both S-adenosylmethionine decarboxylase and ornithine decarboxylase activities
additional information
-
enzyme activity is reduced up to 95% when the deletion of a parasite-specific insert occurs within the respective domain. Inserts mediate specific physical interactions between the two domains of the bifunctional enzyme that are essential for both S-adenosylmethionine decarboxylase and ornithine decarboxylase activities
additional information
-
development of the bla gene-based organism identification, confirmed by 16S rDNA and rpoB sequencing, ODC detection provides a reliable Raoultella identification method widely available as not requiring sequencing equipment, overview
additional information
-
overexpression of yeast antizyme in Saccharomyces cerevisiae results in polyamine depletion and growth inhibition of yeast cells mainly through inhibiting ODC. Overexpression of mammalian antizyme in mammalian cells leads to growth arrest due to polyamine depletion, being an outcome of reduced ODC activity and polyamine uptake. Construction of an ODC mutant lacking the first 47 amino acids and fusion to the C-terminus of mammalian ODC
additional information
the stability of yODC in mammalian cells is not a result of the absence of a compatible antizyme Az or lack of a C-terminal-destabilizing signal found on the mammalian enzyme, but is rather a result of the inability of the mammalian proteasome to degrade yeast ODC
additional information
-
the stability of yODC in mammalian cells is not a result of the absence of a compatible antizyme Az or lack of a C-terminal-destabilizing signal found on the mammalian enzyme, but is rather a result of the inability of the mammalian proteasome to degrade yeast ODC
additional information
-
the stability of yODC in mammalian cells is not a result of the absence of a compatible antizyme Az or lack of a C-terminal-destabilizing signal found on the mammalian enzyme, but is rather a result of the inability of the mammalian proteasome to degrade yeast ODC
-
additional information
-
inhibition of ODC translation by antisense morpholino oligos, xODC mo, abolishes ODC activity increase during oocyte maturation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
AdoMetDC/ODC transcriptome, proteome and metabolome analysis, overview
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
expressed in a polyamine-deficient strain of Saccharomyces cerevisiae (HNU121)
expressed in Datura innoxia
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Saccharomyces cerevisiae
-
expression in Escherichia coli
expression in Escherichia coli and Saccharomyces cerevisiae
expression in Escherichia coli strain BLR(DE3)
-
expression in HEK-293 cells, co-expression with wild-type mammalian ODC and the yeast/mammlian enzyme chimera
-
expression in transgenic mice expressing the human MYCN gene under the control of the rat tyrosine hydroxylase promoter
-
expression of cDNA in CHO cells
-
expression of His6-tagged enzyme in Escherichia coli strain BLR(DE3)
expression of ODC domain, i.e. rPfODC, and ODC domain in conjunction with the preceeding part of the hinge region of the bifunctional ODC/AdoMetDC, i.e.rPfHinge-ODC, in Escherichia coli
-
expression of ODC dominant-negative mutant K69/C360A in Mus musculus
-
expression of ODC in transgenic mice or rats leading to altered, tumoric skin phenotypes, overview, a single nucleotide polymorphism occurs in intron 1 of the ODC gene, which results in increased ODC expression in response to Myc, expression in NIH-3T3 cells overexpressing eIF4E, alpha-difluoromethylornithine not only inhibits proliferation, but also reverts the transformed phenotype of NIH-3T3 cells overexpressing eIF4E
-
expression of Strep-tactin-PfODC/AdoMetDC fusion in Escherichia coli
-
expression of wild-type and chimeric mutant enzymes in COS cells
for transient transfection experiments, ODC cDNAs are cloned into the p3xFLAG-CMV-10 vector, transient transfections of COS-7 cells, used in the ODC activity assay, are performed.
-
gene ODC, adenovirus-mediated expression, the virus containing the cytomegalovirus promoter and the green fluorescent protein gene, of both antisense ornithine decarboxylase and S-adenosylmethionine decarboxylase in A-549 cells, quantitative and tissue expression analysis, G1 arrest rate, overview
-
gene odc, expression as stable enzyme in Trypanosoma cruzi makes the parasite overcome the exogenous putrescine requirement for growth
-
gene ODC, HEK-293 cells are transiently transfected with yeast ODC, mammalian ODC or the chimerical proteins together with either yeast Az or mammalian Az. Overexpression of yAz in yeast cells results in polyamine depletion and growth inhibition
gene odc, located on chromosome 3 between coxadordinates 4069177 to 4070741, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, domain organization, recombinant expression of a fluorescence-tagged enzyme in Dictyostelium discoideum cells
gene odc, overexpression in HL-60 cells
-
gene odc, overexpression in Leishmania guayensis
gene Odc, real-time PCR enzyme expression analysis
gene odc, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21
gene ODC, sequence comparisons, recombinant expression of His-tagged wild-type and truncated mutant enzymes in Escherichia coli strain BL21(DE3)
gene ODC1, quantitative real-time PCR enzyme expression analysis
gene ODC1, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)
gene Odc1, site-directed mutated ODC is in vitro transcribed and translated in reticulocyte lysate, recombinant expression of His-tagged wild-type enzyme, point mutants, and mutant His6-TEV (tobacco etch virus)-FLAG-ODC construct in Escherichia coli
gene speC, DNA and amino acid sequence determination and analysis, speC promoter and speC/speF expression analysis, functional expression in Escherichia coli
-
gene speF, construction of a phage library, DNA and amino acid sequence determination and analysis, genetic organization and speF locus, overview, functional complementation of an Escherichia coli ODC-defective mutant strain strain HT414, elaboration of a hypothetical pathway for the acquisition of putrescine biosynthetic genes in some Enterobacteriaceae strains, overview
mutated ODC is in vitro transcribed and translated in reticulocyte lysate, expression of His-tagged ODC fused to the human dihydrofolate reductase, DHFR, in Escherichia coli
Myc plays a role in transcription of ODC, transcriptional regulation, overview
-
ODC expression analysis
-
ODC expression analysis, overview
-
ODC is encoded by a single-copy gene located on a 1900 kb chromosome, DNA and amino acid sequence determination and analysis, phylogenetic tree, overexpression of the His- and S-tagged enzyme in Escherichia coli
over-expression in transgenic mouse line
-
overexpression of ODC in human promyelocytic leukemia HL-60 parental cells
-
overexpression of ODC, expression analysis, overview
-
transfection of breast cancer cells with an adenoviral vector carrying antisense ODC, rAd-ODC/Ex3as, expression analysis
-
wild type and mutant enzymes C360A, K69A, and C70S
-
-
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression of wild-type and chimeric mutant enzymes in COS cells
expression of wild-type and chimeric mutant enzymes in COS cells
genotyping
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.