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Information on EC 4.1.1.17 - ornithine decarboxylase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P08432
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4.1.1.17 ornithine decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 4.1.1.17
- polyamine
- spermidine
- alpha-difluoromethylornithine
- carcinogenesis
- antizyme
-
chemopreventive
- 12-o-tetradecanoylphorbol-13-acetate
-
phorbol
- mucosa
- difluoromethylornithine
-
diamine
- decarboxylases
-
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
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
odc, ornithine decarboxylase, ldodc, lysine/ornithine decarboxylase, s-adenosylmethionine decarboxylase/ornithine decarboxylase, ldc/odc, ddodc, odc-paralogue, xodc2, adometdc/odc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bODC
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Decarboxylase, ornithine
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-
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ODC
ODC-paralogue
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XODC1
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-
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XODC2
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-
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ODC
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
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-
PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -
SYSTEMATIC NAME
IUBMB Comments
L-ornithine carboxy-lyase (putrescine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
9024-60-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
yeast antizyme mediates degradation of yeast ornithine decarboxylase by yeast but not by mammalian proteasome, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
antizyme
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yeast, determination of sequences that are important for inhibiting ODC activity and promoting ODC degradation, the yeast ODC is not affected by mammalian antizyme
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additional information
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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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
-
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
-
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
expression in HEK-293 cells, co-expression with wild-type mammalian ODC and the yeast/mammlian enzyme chimera
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tyagi, A.K.; Tabor, C.W.; Tabor, H.
Ornithine decarboxylase (Saccharomyces cerevisiae)
Methods Enzymol.
94
135-139
1983
Saccharomyces cerevisiae
Fonzi, W.A.
Biochemical and genetic characterization of the structure of yeast ornithine decarboxylase
Biochem. Biophys. Res. Commun.
162
1409-1416
1989
Saccharomyces cerevisiae
Porat, Z.; Landau, G.; Bercovich, Z.; Krutauz, D.; Glickman, M.; Kahana, C.
Yeast antizyme mediates degradation of yeast ornithine decarboxylase by yeast but not by mammalian proteasome: new insights on yeast antizyme
J. Biol. Chem.
283
4528-4534
2008
Saccharomyces cerevisiae
Fogle, E.J.; Toney, M.D.
Analysis of catalytic determinants of diaminopimelate and ornithine decarboxylases using alternate substrates
Biochim. Biophys. Acta
1814
1113-1119
2011
Saccharomyces cerevisiae, Saccharomyces cerevisiae WDHT668
Chattopadhyay, M.K.; Fernandez, C.; Sharma, D.; McPhie, P.; Masison, D.C.
Yeast ornithine decarboxylase and antizyme form a 1:1 complex in vitro: purification and characterization of the inhibitory complex
Biochem. Biophys. Res. Commun.
406
177-182
2011
Saccharomyces cerevisiae
Porat, Z.; Landau, G.; Bercovich, Z.; Krutauz, D.; Glickman, M.; Kahana, C.
Yeast antizyme mediates degradation of yeast ornithine decarboxylase by yeast but not by mammalian proteasome - new insights on yeast antizyme
J. Biol. Chem.
283
4528-4534
2008
Saccharomyces cerevisiae (P08432), Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741 (P08432)
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