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Literature summary extracted from

  • Kern, A.D.; Oliveira, M.A.; Coffino, P.; Hackert, M.L.
    Structure of mammalian ornithine decarboxylase at 1.6 A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases (1999), Structure Fold. Des., 7, 567-581.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.17 crystals of truncated ODC at 1.6 A resolution, 0.01 mM of silica hydrogel on a microbridge, sitting within a 3.25 ml well containing 1 ml 10% polyethylene glycol is gently covered with 0.01 ml 26% polyethylene glycol 3350, the microbridge is transferred to a well containing 1 ml 26% polyethylene glycol 3350, protein solution containing 12 mg/ml ODC, 2.5 mM dithiothreitol, 1 mM EDTA is added to the microbridge and the well is sealed with tape, plate is left undisturbed in the dark at room temperature for 2 weeks Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.17 L-ornithine Mus musculus first step in polyamine biosynthesis putrescine + CO2
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.17 Mus musculus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.17 L-ornithine
-
Mus musculus putrescine + CO2
-
?
4.1.1.17 L-ornithine first step in polyamine biosynthesis Mus musculus putrescine + CO2
-
?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.17 ODC
-
Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.17 pyridoxal 5'-phosphate
-
Mus musculus