4.1.1.17: ornithine decarboxylase
This is an abbreviated version!
For detailed information about ornithine decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.17
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4.1.1.17
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polyamine
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spermidine
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alpha-difluoromethylornithine
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carcinogenesis
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antizyme
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chemopreventive
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12-o-tetradecanoylphorbol-13-acetate
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phorbol
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mucosa
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difluoromethylornithine
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diamine
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decarboxylases
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n1-acetyltransferase
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hyperplasia
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arginase
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c-myc
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antiproliferative
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tpa-induced
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prostaglandin
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testosterone
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3hthymidine
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tumorigenesis
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mitogen
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cycloheximide
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c-fos
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methylglyoxal
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tpa-treated
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1,2-dimethylhydrazine
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isoproterenol
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hairless
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degrons
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12-o-tetradecanoyl
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hepatectomy
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cadaverine
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s-adenosyl-l-methionine
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drug development
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azoxymethane
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protooncogene
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papilloma
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7,12-dimethylbenzaanthracene
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agmatine
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phorbol-13-acetate
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medicine
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tumor-promoting
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food industry
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diagnostics
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nitrilotriacetate
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pharmacology
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prolactin
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crypt
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trypanothione
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12-o-tetradecanoylphorbol
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ester-induced
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actinomycin
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mezerein
- 4.1.1.17
- polyamine
- spermidine
- alpha-difluoromethylornithine
- carcinogenesis
- antizyme
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chemopreventive
- 12-o-tetradecanoylphorbol-13-acetate
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phorbol
- mucosa
- difluoromethylornithine
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diamine
- decarboxylases
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n1-acetyltransferase
- hyperplasia
- arginase
- c-myc
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antiproliferative
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tpa-induced
- prostaglandin
- testosterone
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3hthymidine
- tumorigenesis
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mitogen
- cycloheximide
- c-fos
- methylglyoxal
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tpa-treated
- 1,2-dimethylhydrazine
- isoproterenol
- hairless
- degrons
-
12-o-tetradecanoyl
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hepatectomy
- cadaverine
- s-adenosyl-l-methionine
- drug development
- azoxymethane
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protooncogene
- papilloma
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7,12-dimethylbenzaanthracene
- agmatine
- phorbol-13-acetate
- medicine
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tumor-promoting
- food industry
- diagnostics
- nitrilotriacetate
- pharmacology
- prolactin
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crypt
- trypanothione
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12-o-tetradecanoylphorbol
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ester-induced
- actinomycin
- mezerein
Reaction
Synonyms
AdoMetDC/ODC, BN36_1212510, bODC, DDB_G0281109, DdODC, Decarboxylase, ornithine, dODC, LDC/ODC, LdODC, lysine/ornithine decarboxylase, ODC, ODC-paralogue, ODC1, ornithine decarboxylase, PfAdoMetDC-ODC, PfODC/AdoMetDC, S-adenosylmethionine decarboxylase/ornithine decarboxylase, SpeC, XODC1, XODC2, YODC
ECTree
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Substrates Products
Substrates Products on EC 4.1.1.17 - ornithine decarboxylase
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REACTION DIAGRAM
5alpha-dihydrotestosterone
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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
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L-2,4-Diaminobutyrate
1,3-Diaminopropane + CO2
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2% of the activity with L-Orn
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L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
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L-lysine
1,5-diaminopentane + CO2
very low activity
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L-lysine
cadaverine + CO2
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L-lysine is a poor substrate for ODC, with a Km approximately 100fold higher than that of L-ornithine
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L-Orn
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alteration in the key enzyme in the growth-associated pathway of polyamine biosynthesis may play a role in colon tumor progression
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L-Orn
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induced in mammary gland of fasted lactating rats by administration of 1,3-diaminopropan-2-ol
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L-Orn
Putrescine + CO2
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L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
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first step in polyamine biosynthesis
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L-ornithine
putrescine + CO2
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ODC is a key enzyme in the polyamine biosynthetic pathway
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L-ornithine
putrescine + CO2
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a key enzymes in polyamine synthesis, putrescin formation leads subsequently to spermidine and spermine
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L-ornithine
putrescine + CO2
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involved in polyamine biosynthesis
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L-ornithine
putrescine + CO2
ornithine decarboxylase, the first and rate-limiting enzyme in the polyamine biosynthetic pathway, is a highly regulated enzyme
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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
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L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
first step in polyamine biosynthesis
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L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
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L-arginine reduces cell proliferation and ornithine decarboxylase activity in patients with colorectal adenoma and adenocarcinoma, overview
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L-ornithine
putrescine + CO2
ODC is the first committed enzyme in the polyamine biosynthesis pathway
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L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
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ODC is the initial and rate-limiting enzyme in polyamine biosynthesis
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L-ornithine
putrescine + CO2
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the enzyme is involved in polyamine biosynthesis, polyamines participate in the cellular response to different structural classes of histone deacetylase inhibitors, overview
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L-ornithine
putrescine + CO2
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the enzyme is involved in polyamine biosynthesis, the enzyme is increased in cancer cells
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L-ornithine
putrescine + CO2
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rate-limiting enzyme in polyamine biosynthesis
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L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
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ODC is a key enzyme in mammalian polyamine biosynthesis that is up-regulated in various types of cancer
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L-ornithine
putrescine + CO2
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Odc is the first and rate-limiting enzyme of polyamine biosynthesis
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L-ornithine
putrescine + CO2
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ODC is the first rate-limiting enzyme in the polyamine biosynthesis pathway
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L-ornithine
putrescine + CO2
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ODC is the rate-limiting enzyme in polyamine biosynthesis
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L-ornithine
putrescine + CO2
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ODC is the rate-limiting enzyme in polyamine biosynthesis that decarboxylates ornithine to putrescine
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L-ornithine
putrescine + CO2
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ODC is the rate-limiting enzyme of the polyamine biosynthetic pathway, and plays an important role in cell cycle, tumor promotion and anti-apoptosis
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L-ornithine
putrescine + CO2
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ODC is a key enzyme in the polyamine biosynthetic pathway
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L-ornithine
putrescine + CO2
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ODC is the first committed enzyme in the polyamine biosynthesis pathway
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L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
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ODC is a key enzyme in the polyamine biosynthetic pathway
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L-ornithine
putrescine + CO2
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677508, 680214, 680257, 697094, 708244, 708546, 708797, 709519, 709568, 710340, 713681, 713718, 713733, 714920, 749065
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L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
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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
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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
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L-ornithine
putrescine + CO2
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Cys360 plays an essential role in ensuring correct protonation of the decarboxylated reaction intermediate at Calpha
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L-ornithine
putrescine + CO2
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key rate-limiting enzyme in polyamine biosynthesis, elevated levels of ODC and polyamines stimulate proliferation of keratinocytes
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L-ornithine
putrescine + CO2
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the enzyme is involved in putrescine biosynthesis, diurnal changes in enzyme activity and polyamine contents in leaves, overview
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L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
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ODC is a key enzyme in the polyamine biosynthetic pathway
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L-ornithine
putrescine + CO2
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ODC is a key enzyme in the polyamine biosynthetic pathway
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L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
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first step in polyamine biosynthesis
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L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
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L-ornithine
putrescine + CO2
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first step in polyamine biosynthesis
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L-ornithine
putrescine + CO2
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involved in polyamine biosynthesis
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L-ornithine
putrescine + CO2
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involved in polyamine biosynthesis
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?
L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
the enzyme is involved in the polyamine pathway
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L-ornithine
putrescine + CO2
the enzyme is involved in the polyamine pathway
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L-ornithine
putrescine + CO2
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involved in polyamine biosynthesis
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L-ornithine
putrescine + CO2
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first step in polyamine biosynthesis
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L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
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ODC is a key enzyme in the polyamine biosynthetic pathway
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L-ornithine
putrescine + CO2
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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
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L-ornithine
putrescine + CO2
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ODC activity increases abruptly in growing callus entire cells after 8 h, no change of activity in chloroplast
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the Arabidopsis rpS15 polypeptide interacts specifically with plant ODC
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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enzyme activity detection using radioactive-labeled substrate
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additional information
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no activity using arginine and lysine as substrates
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additional information
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no activity using arginine and lysine as substrates
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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curcumin-induced apoptosis occurs through a mechanism of down-regulating ODC and along a ROS-dependent mitochondria-mediated pathway
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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no substrate: L-arginine
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additional information
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ODC degradation is not triggered by ubiquitination, the polyamines induce the degradation of ODC by affecting the synthesis of antizyme
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additional information
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Leishmania donovani ODC has a very fast turnover in mammalian cells, but is a stable enzyme
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additional information
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Leishmania donovani ODC has a very fast turnover in mammalian cells, but is a stable enzyme
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additional information
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ODC degradation is not triggered by ubiquitination, the polyamines induce the degradation of ODC by affecting the synthesis of antizyme
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additional information
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no substrates: 2,4-diaminobutanoate, arginine
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additional information
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no substrates: 2,4-diaminobutanoate, arginine
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additional information
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the genes encoding the isozymes are involved in putrescine formation, which is an indicator of food process deterioration
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additional information
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circadian variations in ODC activity in female and male mice, influence of sex hormones, overview
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additional information
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circadian variations in ODC activity in female and male mice, influence of sex hormones, overview
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additional information
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the Raf/MEK/ERK pathway is involved in the regulation of ODC during skin tumorigenesis, overview
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additional information
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NAD(P)H quinone oxidoreductase binds to the enzyme and stabilizes it, this interaction is disrupted with dicoumarol, it sensitizes ODC monomers to degradation by the 20S proteasome in a manner independent of both antizyme and ubiquitin, overview
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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the enzyme induces phosphorylation of ataxia telangiectasia mutated and its substrate p53, which are significantly induced both in Ker/ODC and in K6/ODC transgenic skin, overview
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additional information
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bifunctional enzyme having both ODC and AdoMetDC, i.e. EC4.1.1.50, activity
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additional information
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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
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additional information
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the Raf/MEK/ERK pathway is involved in the regulation of ODC during skin tumorigenesis, overview
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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yeast antizyme mediates degradation of yeast ornithine decarboxylase by yeast but not by mammalian proteasome, overview
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additional information
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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
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additional information
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the enzyme shows ODC activity
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additional information
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the enzyme shows ODC activity
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additional information
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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
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additional information
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ODC degradation is not triggered by ubiquitination, the polyamines induce the degradation of ODC by affecting the synthesis of antizyme
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additional information
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ODC degradation is catalyzed by the 26S proteasome without prior polyubiquitination
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