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Literature summary for 4.1.1.17 extracted from

  • Pegg, A.E.
    Regulation of ornithine decarboxylase (2006), J. Biol. Chem., 281, 14529-14532.
    View publication on PubMed
Search for more literature for 4.1.1.17

Cloned(Commentary)

Cloned (Comment) Organism
Myc plays a role in transcription of ODC, transcriptional regulation, overview Mus musculus

Protein Variants

Protein Variants Comment Organism
C441S the isosteric alteration of the enzyme completely stabilizes ODC even in the presence of excess antizyme Mus musculus
additional information construction of enzyme overexpressing and enzyme-deficient transgenic mice, deletion of the 5 terminal residues 457-461 also stabilizes ODC but to a lesser extent than removing the terminal 37 residues or mutation of Cys441 Mus musculus

General Stability

General Stability Organism
NAD(P)H quinone oxidoreductase binds to the enzyme and stabilizes it Mus musculus
ODC initiates the polyamine biosynthetic pathway, rapid turnover of ODC is brought about by the 26S proteasome, ubiquitination is not required for this degradation, antizyme increases the degradation of ODC by enhancing its interaction with the proteasome but does not increase the rate of proteasomal processing Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
antizyme there are multiple antizyme genes with at least four members, all members, which are localized in different compartments or tissue, inhibit ODC activity, overview, the antizyme inhibitor blocks the effects of antizyme on the enzyme, overview Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-ornithine Mus musculus enzyme regulation, overview, ODC initiates the polyamine biosynthetic pathway, rapid turnover of ODC is brought about by the 26S proteasome, the structure of the COOH-terminal region needed for rapid degradation, ubiquitination is not required for this degradation, antizyme increases the degradation of ODC by enhancing its interaction with the proteasome but does not increase the rate of proteasomal processing, role of ODC and antizyme in carcinogenesis, overview putrescine + CO2
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Organism

Organism UniProt Comment Textmining
Mus musculus
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Posttranslational Modification

Posttranslational Modification Comment Organism
additional information rapid turnover of ODC is brought about by the 26S proteasome, the structure of the COOH-terminal region needed for rapid degradation, ubiquitination is not required for this degradation, antizyme increases the degradation of ODC by enhancing its interaction with the proteasome but does not increase the rate of proteasomal processing, NAD(P)H quinone oxidoreductase binds to the enzyme and stabilizes it, this interaction is disrupted with dicoumarol, it sensitizes ODC monomers to degradation by the 20S proteasome in a manner independent of both antizyme and ubiquitin, overview Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-ornithine enzyme regulation, overview, ODC initiates the polyamine biosynthetic pathway, rapid turnover of ODC is brought about by the 26S proteasome, the structure of the COOH-terminal region needed for rapid degradation, ubiquitination is not required for this degradation, antizyme increases the degradation of ODC by enhancing its interaction with the proteasome but does not increase the rate of proteasomal processing, role of ODC and antizyme in carcinogenesis, overview Mus musculus putrescine + CO2
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 ?
L-ornithine Cys360 plays an essential role in ensuring correct protonation of the decarboxylated reaction intermediate at Calpha Mus musculus putrescine + CO2
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 ?
additional information NAD(P)H quinone oxidoreductase binds to the enzyme and stabilizes it, this interaction is disrupted with dicoumarol, it sensitizes ODC monomers to degradation by the 20S proteasome in a manner independent of both antizyme and ubiquitin, overview Mus musculus ?
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 ?

Synonyms

Synonyms Comment Organism
ODC
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 Mus musculus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate the PLP cofactor is bound in a Schiff base linkage to Lys69 Mus musculus