Literature summary for 4.1.1.19 extracted from

Shah, R.; Coleman, C.S.; Mir, K.; Baldwin, J.; Van Etten, J.L.; Grishin, N.V.; Pegg, A.E.; Stanley, B.A.; Phillips, M.A.
Paramecium bursaria chlorella virus-1 encodes an unusual arginine decarboxylase that is a close homolog of eukaryotic ornithine decarboxylases (2004), J. Biol. Chem., 279, 35760-35767.

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Activating Compound

Activating Compound	Comment	Organism	Structure
pyridoxal 5'-phosphate	included in enzyme assay	Paramecium bursaria Chlorella virus-1

Cloned(Commentary)

Cloned (Comment)	Organism
expression as His-tag fusion protein in Escherichia coli	Paramecium bursaria Chlorella virus-1

Protein Variants

Protein Variants	Comment	Organism
D296E	responsible for changes in substrate specificity	Paramecium bursaria Chlorella virus-1
E296D	increased Km and decreased turnover with L-Arg, minor effect on Km with L-ornithine, decreased turnover with L-ornithine	Paramecium bursaria Chlorella virus-1

Inhibitors

Inhibitors	Comment	Organism	Structure
alpha-difluoromethylarginine	1 mM causes almost complete inhibition after 30 min incubation, irreversible	Paramecium bursaria Chlorella virus-1
alpha-difluoromethylornithine	10 mM causes 74% inhibition after 30 min incubation, irreversible	Paramecium bursaria Chlorella virus-1

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.45	-	L-Arg	pH 8.2, 37°C	Paramecium bursaria Chlorella virus-1
0.48	-	L-Arg	pH 9.0, 40°C	Paramecium bursaria Chlorella virus-1
46	-	L-ornithine	pH 9.0, 40°C	Paramecium bursaria Chlorella virus-1
180	-	L-ornithine	pH 8.2, 37°C	Paramecium bursaria Chlorella virus-1

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-arginine	Paramecium bursaria Chlorella virus-1	key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response	agmatine + CO2	-	?
L-ornithine	Paramecium bursaria Chlorella virus-1	-	putrescine + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Paramecium bursaria Chlorella virus-1	-	enzyme displays ornithine decarboxylase as well as arginine decarboxylase activity	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant protein using His-tag	Paramecium bursaria Chlorella virus-1

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-arginine	-	Paramecium bursaria Chlorella virus-1	agmatine + CO2	-	?
L-arginine	key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response	Paramecium bursaria Chlorella virus-1	agmatine + CO2	-	?
L-ornithine	-	Paramecium bursaria Chlorella virus-1	putrescine + CO2	-	?

Synonyms

Synonyms	Comment	Organism
PBCV-1 DC	-	Paramecium bursaria Chlorella virus-1

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Release 2023.1 (January 2023)