Cloned (Comment) | Organism |
---|---|
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 | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
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 | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-ornithine | Saccharomyces cerevisiae | - |
putrescine + CO2 | - |
? | |
L-ornithine | Saccharomyces cerevisiae BY4741 | - |
putrescine + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P08432 | from strain ATCC 204508 / S288c | - |
Saccharomyces cerevisiae BY4741 | P08432 | from strain ATCC 204508 / S288c | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
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 | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-ornithine | - |
Saccharomyces cerevisiae | putrescine + CO2 | - |
? | |
L-ornithine | - |
Saccharomyces cerevisiae BY4741 | putrescine + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ODC | - |
Saccharomyces cerevisiae |
YODC | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
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 | Saccharomyces cerevisiae |
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 | Saccharomyces cerevisiae |
physiological function | ornithine decarboxylase (ODC) is the first and rate-limiting enzyme in the biosynthesis pathway of polyamines. ODC decarboxylates ornithine to form putrescine | Saccharomyces cerevisiae |