Literature summary for 4.1.1.17 extracted from

Bonnin-Jusserand, M.; Grandvalet, C.; David, V.; Alexandre, H.
Molecular cloning, heterologous expression, and characterization of ornithine decarboxylase from Oenococcus oeni (2011), J. Food Prot., 74, 1309-1314.

Search for more literature for 4.1.1.17

Application

Application	Comment	Organism
food industry	the enzyme is used in the wine making process	Oenococcus oeni

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Oenococcus oeni

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1	-	L-ornithine	at pH 5.5, 35°C	Oenococcus oeni

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
85000	-	x * 85000, SDS-PAGE	Oenococcus oeni

Organism

Organism	UniProt	Comment	Textmining
Oenococcus oeni	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-ornithine	the enzyme is speciic for L-ornithine	Oenococcus oeni	putrescine + CO2	-	?
additional information	the enzyme cannot decarboxylate L-lysine	Oenococcus oeni	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 85000, SDS-PAGE	Oenococcus oeni

Synonyms

Synonyms	Comment	Organism
ODC	-	Oenococcus oeni

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
35	-	-	Oenococcus oeni

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5.5	-	-	Oenococcus oeni

pI Value

Organism	Comment	pI Value Maximum	pI Value
Oenococcus oeni	isoelectric focusing	-	6.2

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Release 2023.1 (January 2023)