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Literature summary for 4.1.1.19 extracted from

  • Fukuda, W.; Morimoto, N.; Imanaka, T.; Fujiwara, S.
    Agmatine is essential for the cell growth of Thermococcus kodakaraensis (2008), FEMS Microbiol. Lett., 287, 113-120.
    View publication on PubMed
Search for more literature for 4.1.1.19

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Thermococcus kodakarensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
12600
-
 6 * 12600 + 6 * 4500, (alphabeta)6 complex, denaturant gel electrophoresis Thermococcus kodakarensis
99400
-
 gel filtration Thermococcus kodakarensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arginine Thermococcus kodakarensis first step of polyamine biosynthesis agmatine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis Q5JFI4
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification synthesized as an inactive proenzyme Thermococcus kodakarensis
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 (Ser44) 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 Thermococcus kodakarensis

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Thermococcus kodakarensis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.28
-
 pH 6.0, 70-90°C Thermococcus kodakarensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginine first step of polyamine biosynthesis Thermococcus kodakarensis agmatine + CO2
-
 ?
L-arginine no activity with ornithine and lysine Thermococcus kodakarensis agmatine + CO2
-
 ?

Subunits

Subunits Comment Organism
hexamer 6 * 12600 + 6 * 4500, (alphabeta)6 complex, denaturant gel electrophoresis Thermococcus kodakarensis

Synonyms

Synonyms Comment Organism
pyruvoyl-dependent arginine decarboxylase
-
 Thermococcus kodakarensis
Tk-PdaD
-
 Thermococcus kodakarensis
TK0149
-
 Thermococcus kodakarensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70 90 assay at Thermococcus kodakarensis
100
-
-
 Thermococcus kodakarensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Thermococcus kodakarensis

Cofactor

Cofactor Comment Organism Structure
additional information pyruvoyl-dependent decarboxylase, synthesised as zymogen. The pyruvoyl cofactor results from the self-modification of an internal serine (Ser44) residue of the proenzyme, the pyruvoyl group functions through the formation of a Schiff base with the substrate to promote decarboxylation Thermococcus kodakarensis

General Information

General Information Comment Organism
physiological function a gene disruptant lacking arginine decarboxylase is constructed, showing that it grows only in the medium in the presence of agmatine but not in the absence of agmatine. The results indicates that agmatine is essential for the cell growth of Thermococcus kodakaraensis Thermococcus kodakarensis