Literature summary for 4.1.1.19 extracted from

Graham, D.E.; Xu, H.; White, R.H.
Methanococcus jannaschii uses a pyruvoyl-dependent arginine decarboxylase in polyamine biosynthesis (2002), J. Biol. Chem., 277, 23500-23507.

Search for more literature for 4.1.1.19

General Stability

General Stability	Organism
enzyme resists proteolytic cleavage by trypsin, pepsin, carboxypeptidase A, or papain	Methanocaldococcus jannaschii
enzyme retains full activity in presence of 1% w/v SDS at 70°C	Methanocaldococcus jannaschii

Inhibitors

Inhibitors	Comment	Organism	Structure
agmatine	1.4 mM, 50% inhibition	Methanocaldococcus jannaschii
guanidine	5-10 mM, 50% inhibition	Methanocaldococcus jannaschii
L-argininamide	5 mM, complete inhibition	Methanocaldococcus jannaschii
L-arginine methyl ester	5 mM, complete inhibition	Methanocaldococcus jannaschii
methylguanidine	5-10 mM, 50% inhibition	Methanocaldococcus jannaschii
Urea	4 M, 80% inhibition	Methanocaldococcus jannaschii

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
4.7	-	L-Arg	pH 6.0, 70°C	Methanocaldococcus jannaschii
7.1	-	L-Arg	pH 6.0, 83°C	Methanocaldococcus jannaschii

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
55900	-	gel filtration	Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-arginine	Methanocaldococcus jannaschii	enzyme is involved in polyamine biosynthesis	agmatine + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Methanocaldococcus jannaschii	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	the enzyme is formed by self-cleavage of a proenzyme into a 5000 Da subunit and a 12000 Da subunit that contains a reactive pyruvoyl group	Methanocaldococcus jannaschii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
2.1	-	-	Methanocaldococcus jannaschii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-arginine	-	Methanocaldococcus jannaschii	agmatine + CO2	-	?
L-arginine	enzyme is involved in polyamine biosynthesis	Methanocaldococcus jannaschii	agmatine + CO2	-	?

Subunits

Subunits	Comment	Organism
hexamer	3 * alpha 11000-13000 + 3 * beta 5000-7000, SDS-PAGE	Methanocaldococcus jannaschii

Synonyms

Synonyms	Comment	Organism
PvlArgDC	-	Methanocaldococcus jannaschii
pyruvoyl-dependent arginine decarboxylase	-	Methanocaldococcus jannaschii

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
90	-	activity increases up to	Methanocaldococcus jannaschii

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
121	-	20 min, 50% loss of activity	Methanocaldococcus jannaschii
125	-	30 min, 84% loss of activity	Methanocaldococcus jannaschii

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
2.7	-	L-Arg	pH 6.0, 83°C	Methanocaldococcus jannaschii

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6	-	-	Methanocaldococcus jannaschii

pH Range

pH Minimum	pH Maximum	Comment	Organism
5	8	pH 5.0: about 60% of maximal activity, pH 8.0: about 60% of maximal activity	Methanocaldococcus jannaschii

Cofactor

Cofactor	Comment	Organism	Structure
additional information	the enzyme contains a reactive pyruvoyl group	Methanocaldococcus jannaschii

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Release 2023.1 (January 2023)