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
-
diamine
- decarboxylases
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n1-acetyltransferase
- hyperplasia
- arginase
- c-myc
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antiproliferative
-
tpa-induced
- prostaglandin
- testosterone
-
3hthymidine
- tumorigenesis
-
mitogen
- cycloheximide
- c-fos
- methylglyoxal
-
tpa-treated
- 1,2-dimethylhydrazine
- isoproterenol
- hairless
- degrons
-
12-o-tetradecanoyl
-
hepatectomy
- cadaverine
- s-adenosyl-l-methionine
- drug development
- azoxymethane
-
protooncogene
- papilloma
-
7,12-dimethylbenzaanthracene
- agmatine
- phorbol-13-acetate
- medicine
-
tumor-promoting
- food industry
- diagnostics
- nitrilotriacetate
- pharmacology
- prolactin
-
crypt
- trypanothione
-
12-o-tetradecanoylphorbol
-
ester-induced
- actinomycin
- mezerein
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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Posttranslational Modification
Posttranslational Modification on EC 4.1.1.17 - ornithine decarboxylase
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additional information
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supplemental L-methionine or L-arginine induce a marked decrease in enzyme half-life concomitantly with an increase in the activity of enzyme inhibitory protein antizyme
additional information
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degradation of enzyme is accelerated antizyme extract as well as by Selenomonas ruminantium P22 protein, which is a counterpart of antizyme. Degradation occurs via 26S proteasome
additional information
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rapid turnover of ODC is brought about by the 26S proteasome, the structure of the COOH-terminal region needed for rapid degradation, ubiquitination is not required for this degradation, antizyme increases the degradation of ODC by enhancing its interaction with the proteasome but does not increase the rate of proteasomal processing, NAD(P)H quinone oxidoreductase binds to the enzyme and stabilizes it, this interaction is disrupted with dicoumarol, it sensitizes ODC monomers to degradation by the 20S proteasome in a manner independent of both antizyme and ubiquitin, overview
additional information
murine ODC (ornithine decarboxylase) is quickly degraded by the 26S proteasome in mammalian and fungal cells. Its degradation is independent of ubiquitin but requires a degradation signal composed of residues 425-461 at the ODC C-terminus, cODC (the last 37 amino acids of the ODC C-terminus). The presence of two essential elements in the degradation signal: the first consists of cysteine and alanine at residues 441 and 442 respectively, the second element is the C-terminus distal to residue 442. It has little or no sequence specificity, but is intolerant of insertions or deletions that alter its span. Reducing conditions, which preclude all well-characterized chemical reactions of the Cys441 thiol, are essential for in vitro degradation. The degradative function of Cys441 does not involve its participation in chemical reaction, instead, it functions within a structural element for recognition by the 26S proteasome. Rattus norvegicus AZ1-stimulated ODC degradation is conducted in reticulocyte lysate. The thiol group of Cys441 must be maintained in a reduced state to act as a recognition signal for the 26S proteasome, and does not act as a bonding partner with other residues
additional information
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. Yeast antizyme (yAz) stimulates the degradation of yeast ODC by the yeast proteasome, interaction with yAz provokes degradation of yODC by yeast but not by mammalian proteasomes
additional information
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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. Yeast antizyme (yAz) stimulates the degradation of yeast ODC by the yeast proteasome, interaction with yAz provokes degradation of yODC by yeast but not by mammalian proteasomes
additional information
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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. Yeast antizyme (yAz) stimulates the degradation of yeast ODC by the yeast proteasome, interaction with yAz provokes degradation of yODC by yeast but not by mammalian proteasomes
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