Cloned (Comment) | Organism |
---|---|
gene Odc1, site-directed mutated ODC is in vitro transcribed and translated in reticulocyte lysate, recombinant expression of His-tagged wild-type enzyme, point mutants, and mutant His6-TEV (tobacco etch virus)-FLAG-ODC construct in Escherichia coli | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
A457W | site-directed mutagenesis, the mutation does not stabilize the enzyme | Mus musculus |
C441A | site-directed mutagenesis, the mutation stabilizes the enzyme but also profoundly reduces its activity | Mus musculus |
C441A/A442C | site-directed mutagenesis, swapping the cysteine residue with either of the two adjacent residues stabilizes ODC, reducing degradation from 25% to less than 5% in each case | Mus musculus |
additional information | purified [35S]methionine-labeled recombinant His6-TEV (tobacco etch virus)-FLAG-ODC is generated and degraded in vitro | Mus musculus |
S440C/C441S | site-directed mutagenesis, swapping the cysteine residue with either of the two adjacent residues stabilizes ODC, reducing degradation from 25% to less than 5% in each case. The stabilization of ODC by the C441S mutation implies that the hydroxy group cannot replicate the functional properties of the thiol of Cys441 | Mus musculus |
S456A | site-directed mutagenesis, the mutation does not stabilize the enzyme | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-ornithine | Mus musculus | - |
putrescine + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | P00860 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
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 | Mus musculus |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged wild-type an dmutant enzymes from Escherichia coli | Mus musculus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-ornithine | - |
Mus musculus | putrescine + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ODC | - |
Mus musculus |
ODC1 | - |
Mus musculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
metabolism | 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. Within cODC, Cys441 functions as a proteasome association element, while the C-terminal end of cODC initiates entry into the proteasome | Mus musculus |
additional information | enzyme residue Cys441 takes part in functionally significant side-chain interactions with an amino acid in this local neighbourhood. Cys441 is intolerant of positional change. Cys441 does not form an intramolecular disulfide bond | Mus musculus |