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Literature summary for 4.1.1.19 extracted from

  • Giles, T.N.; Graham, D.E.
    Crenarchaeal arginine decarboxylase evolved from an S-adenosylmethionine decarboxylase enzyme (2008), J. Biol. Chem., 283, 25829-25838.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.19

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli. The phylogeny of the crenarchaeal homologs suggests that the arginine decarboxylase gene evolves from a single duplication of an ancestral S-adenosylmethionine decarboxylase gene early in the crenarchaeota Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
additional information modeling and activity of a chimeric arginine decarboxylase/S-adenosylmethionine decarboxylase proteins. A chimeric protein containing the beta subunit of arginine decarboxylase (SSO0536) and the alpha subunit of S-adenosylmethionine decarboxylase (SSO0585) has arginine decarboxylase activity and no S-adenosylmethionine decarboxylase activity, implicating residues responsible for substrate specificity in the beta subunit Saccharolobus solfataricus

Inhibitors

Inhibitors Comment Organism Structure
difluoromethyl-L-arginine 1 mM, 80 °C, 15 min, 64% loss of activity, irreversible inhibition Saccharolobus solfataricus
difluoromethyl-L-ornithine 1 mM, reduces activity by 20% Saccharolobus solfataricus
L-argininamide 1 mM, almost completely abolished arginine decarboxylase activity Saccharolobus solfataricus
L-arginine methyl ester 1 mM, 70% loss of activity Saccharolobus solfataricus
L-canavanine 1 mM, 46% inhibition Saccharolobus solfataricus
L-histidine 1 mM, 20-30% inhibition Saccharolobus solfataricus
L-homoarginine 1 mM, 20-30% inhibition Saccharolobus solfataricus
additional information 1 mM phenylhydrazine does not inactivate the enzyme. No inhibition with D-arginine, L-citrulline, L-lysine, Nalpha-methyl-L-arginine, L-methionine, Nalpha-nitro-L-arginine methyl ester, or L-ornithine Saccharolobus solfataricus
Nalpha-acetyl-L-arginine 1 mM, 20-30% inhibition Saccharolobus solfataricus
O-(4-nitrobenzyl)hydroxylamine 1 mM, 50% inhibition, pyruvoyl group modification Saccharolobus solfataricus
O-Methylhydroxylamine 1 mM, 50% inhibition, pyruvoyl group modification Saccharolobus solfataricus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
 L-arginine pH 6.5, 70°C Saccharolobus solfataricus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no stimulation by KCl Saccharolobus solfataricus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6123
-
 4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE Saccharolobus solfataricus
11759
-
 4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE Saccharolobus solfataricus
17940
-
 inactive proenzyme, mass spectrometry Saccharolobus solfataricus
80000
-
 His10-tagged enzyme, gel filtration Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arginine Saccharolobus solfataricus
-
 agmatine + CO2
-
 ?
L-arginine Saccharolobus solfataricus P2
-
 agmatine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q9UWU1
-
-
Saccharolobus solfataricus P2 Q9UWU1
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification synthesized as an inactive proenzyme Saccharolobus solfataricus
pyruvoyl group formation the enzyme is synthesized as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue (Ser82) via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme Saccharolobus solfataricus

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginine
-
 Saccharolobus solfataricus agmatine + CO2
-
 ?
L-arginine the crenarchaeal arginine decarboxylase has no S-adenosylmethionine decarboxylase activity Saccharolobus solfataricus agmatine + CO2
-
 ?
L-arginine
-
 Saccharolobus solfataricus P2 agmatine + CO2
-
 ?
L-arginine the crenarchaeal arginine decarboxylase has no S-adenosylmethionine decarboxylase activity Saccharolobus solfataricus P2 agmatine + CO2
-
 ?
L-canavanine decarboxylation at 40% of the activity compared with L-arginine Saccharolobus solfataricus N-(3-aminopropoxy)guanidine + CO2
-
 ?
L-canavanine decarboxylation at 40% of the activity compared with L-arginine Saccharolobus solfataricus P2 N-(3-aminopropoxy)guanidine + CO2
-
 ?

Subunits

Subunits Comment Organism
octamer 4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
ARGDC
-
 Saccharolobus solfataricus
protein SSO0536
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
 assay at Saccharolobus solfataricus
80
-
-
 Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
90
-
 pH 6.0, 10 min, enzyme retains 80% of ist original activity Saccharolobus solfataricus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6
-
 L-arginine pH 6.5, 70°C Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Saccharolobus solfataricus
6.5
-
 assay at Saccharolobus solfataricus

pH Range

pH Minimum pH Maximum Comment Organism
4 6 pH 4.0: about 65% of maximal activity, pH 6.0: optimum Saccharolobus solfataricus

Cofactor

Cofactor Comment Organism Structure
Pyruvoyl group pyruvoyl-dependent decarboxylase, synthesised as zymogen. The pyruvoyl cofactor results from the self-modification of an internal serine (Ser82) residue of the proenzyme, the pyruvoyl group functions through the formation of a Schiff base with the substrate to promote decarboxylation Saccharolobus solfataricus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
13
-
 L-arginine pH 6.5, 70°C Saccharolobus solfataricus