Literature summary for 4.1.1.19 extracted from

Hanfrey, C.; Sommer, S.; Mayer, M.J.; Burtin, D.; Michael, A.J.
Arabidopsis polyamine biosynthesis: absence of ornithine decarboxylase and the mechanism of arginine decarboxylase activity (2001), Plant J., 27, 551-560.

Search for more literature for 4.1.1.19

Protein Variants

Protein Variants	Comment	Organism
C524A	91.8% reduction of activity compared to wild-type enzyme. When the k136A/pYES2 and C524A/pYX243 ADC1 plasmids are coexpressed in the same yeast cells, there is about 25% functional rescue of ADC activity	Arabidopsis thaliana
K136A	97.7% reduction of activity compared to wild-type enzyme. When the k136A/pYES2 and C524A/pYX243 ADC1 plasmids are coexpressed in the same yeast cells, there is about 25% functional rescue of ADC activity	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q9SI64	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	maximal activity of ADC1 in yeast requires the presence of general protease genes, and it is likely that dimer formation precedes proteolytic processing of the ADC pre-protein monomer	Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-arginine	amino acids K136 and C524 of ADC1 are essential for activity and participate in separate active sites	Arabidopsis thaliana	agmatine + CO2	-	?

Subunits

Subunits	Comment	Organism
dimer	the enzyme is a head-to-tail homodimer with two active sites acting in trans across the interface of the dimer	Arabidopsis thaliana

Synonyms

Synonyms	Comment	Organism
ADC1	-	Arabidopsis thaliana

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Release 2023.1 (January 2023)