Literature summary for 4.1.1.17 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.

Search for more literature for 4.1.1.17

Protein Variants

Protein Variants	Comment	Organism
C360A	mutation C360A 26fold reduces the specificity constant and 2fold decreases the Km	Mus musculus
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
C70S	mutant enzyme C70S has a 2fold increased Km-value	Mus musculus
K69A	mutant enzyme K69A shows a changed spectrum and a 550fold decrease in the turnover/Km value	Mus musculus

KM Value [mM]

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

Organism

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

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)