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Literature summary extracted from

  • Coleman, C.S.; Stanley, B.A.; Pegg, A.E.
    Effect of mutations at active site residues on the activity of ornithine decarboxylase and its inhibition by active site-directed irreversible inhibitors (1993), J. Biol. Chem., 268, 24572-24579.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.17 C360A mutation C360A 26fold reduces the specificity constant and 2fold decreases the Km Mus musculus
4.1.1.17 C360A mutant enzyme C360A is completely resistant to inactivation by (R,R)-delta-methyl-alpha-acetylenicputrescine and is much less sensitive than the wild type enzyme to alpha-monofluoromethyldehydromethylornithine Mus musculus
4.1.1.17 C70S mutant enzyme C70S has a 2fold increased Km-value Mus musculus
4.1.1.17 K69A mutant enzyme K69A shows a changed spectrum and a 550fold decrease in the turnover/Km value Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.17 0.03
-
 L-Orn mutant enzyme C360A Mus musculus
4.1.1.17 0.081
-
 L-Orn mutant enzyme K69A Mus musculus
4.1.1.17 0.086
-
 L-Orn wild type enzyme Mus musculus
4.1.1.17 0.15
-
 L-Orn mutant enzyme C70S Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.17 Mus musculus
-
 wild type and mutant enzymes C360A, K69A and C70S
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.17 L-Orn
-
 Mus musculus Putrescine + CO2
-
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