Literature summary for 4.1.1.17 extracted from

Takeuchi, J.; Chen, H.; Hoyt, M.A.; Coffino, P.
Structural elements of the ubiquitin-independent proteasome degron of ornithine decarboxylase (2008), Biochem. J., 410, 401-407 .

Search for more literature for 4.1.1.17

Cloned(Commentary)

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

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/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-ornithine	Mus musculus	-	putrescine + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	P00860	-	-

Posttranslational Modification

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 (Commentary)

Purification (Comment)	Organism
recombinant His-tagged wild-type an dmutant enzymes from Escherichia coli	Mus musculus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-ornithine	-	Mus musculus	putrescine + CO2	-	?

Synonyms

Synonyms	Comment	Organism
ODC	-	Mus musculus
ODC1	-	Mus musculus

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Mus musculus

General Information

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

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Release 2023.1 (January 2023)