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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.19 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
4.1.1.50 expression in Escherichia coli Saccharolobus solfataricus

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.19 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
4.1.1.50 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

EC Number Inhibitors Comment Organism Structure
4.1.1.19 difluoromethyl-L-arginine 1 mM, 80 °C, 15 min, 64% loss of activity, irreversible inhibition Saccharolobus solfataricus
4.1.1.19 difluoromethyl-L-ornithine 1 mM, reduces activity by 20% Saccharolobus solfataricus
4.1.1.19 L-argininamide 1 mM, almost completely abolished arginine decarboxylase activity Saccharolobus solfataricus
4.1.1.19 L-arginine methyl ester 1 mM, 70% loss of activity Saccharolobus solfataricus
4.1.1.19 L-canavanine 1 mM, 46% inhibition Saccharolobus solfataricus
4.1.1.19 L-histidine 1 mM, 20-30% inhibition Saccharolobus solfataricus
4.1.1.19 L-homoarginine 1 mM, 20-30% inhibition Saccharolobus solfataricus
4.1.1.19 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
4.1.1.19 Nalpha-acetyl-L-arginine 1 mM, 20-30% inhibition Saccharolobus solfataricus
4.1.1.19 O-(4-nitrobenzyl)hydroxylamine 1 mM, 50% inhibition, pyruvoyl group modification Saccharolobus solfataricus
4.1.1.19 O-Methylhydroxylamine 1 mM, 50% inhibition, pyruvoyl group modification Saccharolobus solfataricus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.19 0.2
-
 L-arginine pH 6.5, 70°C Saccharolobus solfataricus

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.19 6123
-
 4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE Saccharolobus solfataricus
4.1.1.19 11759
-
 4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE Saccharolobus solfataricus
4.1.1.19 17940
-
 inactive proenzyme, mass spectrometry Saccharolobus solfataricus
4.1.1.19 80000
-
 His10-tagged enzyme, gel filtration Saccharolobus solfataricus
4.1.1.50 16602
-
 2 * 16602, electrospray ionization mass spectrometry Saccharolobus solfataricus
4.1.1.50 16680
-
 2 * 16680, calculated from sequence Saccharolobus solfataricus
4.1.1.50 33000
-
 His10-tagged enzyme, gel filtration Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.19 L-arginine Saccharolobus solfataricus
-
 agmatine + CO2
-
 ?
4.1.1.19 L-arginine Saccharolobus solfataricus P2
-
 agmatine + CO2
-
 ?
4.1.1.50 S-adenosyl-L-methionine Saccharolobus solfataricus
-
 (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
-
 ?
4.1.1.50 S-adenosyl-L-methionine Saccharolobus solfataricus P2
-
 (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.19 Saccharolobus solfataricus Q9UWU1
-
-
4.1.1.19 Saccharolobus solfataricus P2 Q9UWU1
-
-
4.1.1.50 Saccharolobus solfataricus Q9UWY8
-
-
4.1.1.50 Saccharolobus solfataricus P2 Q9UWY8
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
4.1.1.19 proteolytic modification synthesized as an inactive proenzyme Saccharolobus solfataricus
4.1.1.19 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)

EC Number Purification (Comment) Organism
4.1.1.19
-
 Saccharolobus solfataricus
4.1.1.50
-
 Saccharolobus solfataricus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.50 0.11
-
 pH 8.0, 70°C Saccharolobus solfataricus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.19 L-arginine
-
 Saccharolobus solfataricus agmatine + CO2
-
 ?
4.1.1.19 L-arginine the crenarchaeal arginine decarboxylase has no S-adenosylmethionine decarboxylase activity Saccharolobus solfataricus agmatine + CO2
-
 ?
4.1.1.19 L-arginine
-
 Saccharolobus solfataricus P2 agmatine + CO2
-
 ?
4.1.1.19 L-arginine the crenarchaeal arginine decarboxylase has no S-adenosylmethionine decarboxylase activity Saccharolobus solfataricus P2 agmatine + CO2
-
 ?
4.1.1.19 L-canavanine decarboxylation at 40% of the activity compared with L-arginine Saccharolobus solfataricus N-(3-aminopropoxy)guanidine + CO2
-
 ?
4.1.1.19 L-canavanine decarboxylation at 40% of the activity compared with L-arginine Saccharolobus solfataricus P2 N-(3-aminopropoxy)guanidine + CO2
-
 ?
4.1.1.50 S-adenosyl-L-methionine
-
 Saccharolobus solfataricus (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
-
 ?
4.1.1.50 S-adenosyl-L-methionine the crenarchaeal S-adenosylmethionine decarboxylase has no arginine decarboxylase activity Saccharolobus solfataricus (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
-
 ?
4.1.1.50 S-adenosyl-L-methionine
-
 Saccharolobus solfataricus P2 (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
-
 ?
4.1.1.50 S-adenosyl-L-methionine the crenarchaeal S-adenosylmethionine decarboxylase has no arginine decarboxylase activity Saccharolobus solfataricus P2 (5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.19 octamer 4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE Saccharolobus solfataricus
4.1.1.50 dimer 2 * 16602, electrospray ionization mass spectrometry Saccharolobus solfataricus
4.1.1.50 dimer 2 * 16680, calculated from sequence Saccharolobus solfataricus

Synonyms

EC Number Synonyms Comment Organism
4.1.1.19 ARGDC
-
 Saccharolobus solfataricus
4.1.1.19 protein SSO0536
-
 Saccharolobus solfataricus
4.1.1.50 AdoMetDC
-
 Saccharolobus solfataricus
4.1.1.50 protein SSO0585
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.19 70
-
 assay at Saccharolobus solfataricus
4.1.1.19 80
-
-
 Saccharolobus solfataricus
4.1.1.50 70
-
 assay at Saccharolobus solfataricus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.1.19 90
-
 pH 6.0, 10 min, enzyme retains 80% of ist original activity Saccharolobus solfataricus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.19 2.6
-
 L-arginine pH 6.5, 70°C Saccharolobus solfataricus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.19 6
-
-
 Saccharolobus solfataricus
4.1.1.19 6.5
-
 assay at Saccharolobus solfataricus
4.1.1.50 8
-
 assay at Saccharolobus solfataricus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.1.1.19 4 6 pH 4.0: about 65% of maximal activity, pH 6.0: optimum Saccharolobus solfataricus

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.19 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]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.1.19 13
-
 L-arginine pH 6.5, 70°C Saccharolobus solfataricus
4.1.1.50 2.3
-
 S-adenosyl-L-methionine pH 8.0, 70°C Saccharolobus solfataricus