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
-
chemopreventive
- 12-o-tetradecanoylphorbol-13-acetate
-
phorbol
- mucosa
- difluoromethylornithine
-
diamine
- decarboxylases
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n1-acetyltransferase
- hyperplasia
- arginase
- c-myc
-
antiproliferative
-
tpa-induced
- prostaglandin
- testosterone
-
3hthymidine
- tumorigenesis
-
mitogen
- cycloheximide
- c-fos
- methylglyoxal
-
tpa-treated
- 1,2-dimethylhydrazine
- isoproterenol
- hairless
- degrons
-
12-o-tetradecanoyl
-
hepatectomy
- cadaverine
- s-adenosyl-l-methionine
- drug development
- azoxymethane
-
protooncogene
- papilloma
-
7,12-dimethylbenzaanthracene
- agmatine
- phorbol-13-acetate
- medicine
-
tumor-promoting
- food industry
- diagnostics
- nitrilotriacetate
- pharmacology
- prolactin
-
crypt
- trypanothione
-
12-o-tetradecanoylphorbol
-
ester-induced
- actinomycin
- mezerein
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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Subunits
Subunits on EC 4.1.1.17 - ornithine decarboxylase
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dimer
dodecamer
monomer
tetramer
additional information
?
x * 46000, about, sequence calculation, x * 48000, recombinant His- and S-tagged enzyme, SDS-PAGE
dimer
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antizyme binds to the monomeric form of ODC, preventing formation of the enzymatically active homodimer, and then targets ODC for degradation
dimer
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antizyme binds to the monomeric form of ODC, preventing formation of the enzymatically active homodimer, and then targets ODC for degradation
dimer
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antizyme binds to the monomeric form of ODC, preventing formation of the enzymatically active homodimer, and then targets ODC for degradation
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the dodecamer dissociates into dimers at high pH in the presence or absence of GTP
monomer
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1 * 50000, SDS-PAGE, the enzyme exists as monomer at high salt concentrations and in polymeric form at low salt concentrations
monomer
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1 * 50000, SDS-PAGE, the enzyme exists as monomer at high salt concentrations and in polymeric form at low salt concentrations
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4 * 41000, SDS-PAGE, or 3 * 41000 + 1 * 56000, SDS-PAGE
tertiary structure prediction of putative Dictyostelium discoideum ornithine decarboxylase (DdODC), overview
additional information
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tertiary structure prediction of putative Dictyostelium discoideum ornithine decarboxylase (DdODC), overview
additional information
the interface of the ODC homodimer contains two active sites for the ornithine decarboxylation reaction. Each active site is composed of one pyridoxal 5'-phosphate binding site, made up mainly of the N-terminal domain of one monomer, and one substrate binding site, made up mainly of the C-terminal domain of the second monomer
additional information
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the interface of the ODC homodimer contains two active sites for the ornithine decarboxylation reaction. Each active site is composed of one pyridoxal 5'-phosphate binding site, made up mainly of the N-terminal domain of one monomer, and one substrate binding site, made up mainly of the C-terminal domain of the second monomer
additional information
structural analysis of wild-type and truncated mutant enzymes by circular dichroism and fluorescence spectroscopy
additional information
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structural analysis of wild-type and truncated mutant enzymes by circular dichroism and fluorescence spectroscopy