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Literature summary for 4.1.1.17 extracted from

  • Qu, N.; Ignatenko, N.A.; Yamauchi, P.; Stringer, D.E.; Levenson, C.; Shannon, P.; Perrin, S.; Gerner, E.W.
    Inhibition of human ornithine decarboxylase activity by enantiomers of difluoromethylornithine (2003), Biochem. J., 375, 465-470.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.17

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
(DL)-difluoromethylornithine irreversible inactivation, 50% inhibition at 0.0075 mM D-difluoromethylornithine Homo sapiens
D-ornithine 1.5 mM, 50% inhibition Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-ornithine Homo sapiens first step in polyamine biosynthesis putrescine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant ODC Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 less than 0.0000001 mM of D-ornithine decarboxylate/min/mg Homo sapiens
6
-
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-ornithine very weak activity Homo sapiens putrescine + CO2
-
 ?
L-ornithine
-
 Homo sapiens putrescine + CO2
-
 ?
L-ornithine first step in polyamine biosynthesis Homo sapiens putrescine + CO2
-
 ?

Synonyms

Synonyms Comment Organism
ODC
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Homo sapiens