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Literature summary for 4.1.1.19 extracted from

  • Giles, T.N.; Graham, D.E.
    Characterization of an acid-dependent arginine decarboxylase enzyme from Chlamydophila pneumoniae (2007), J. Bacteriol., 189, 7376-7383.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.1.19

Cloned(Commentary)

Cloned (Comment) Organism
gene adiA, expression of untagged and N-terminally His10-tagged wild-type enzyme and inactivated mutant in strain BW25113 Escherichia coli
gene CPn1032, expression of untagged and N-terminally His10-tagged enzyme in Escherichia coli strain Bl21(DE3), CPn1032 expression complements the adiA null mutation in Escherichia coli strain DEG0121, which shows low arginine decarboxylase enzyme activity and is deficient in AdiC transporter Chlamydia pneumoniae

Protein Variants

Protein Variants Comment Organism
additional information construction of an enzyme deletion null mutant, complementation by expression of the enzyme from Chlamydophila pneumoniae Escherichia coli
T52S site-directed mutagenesis, the mutant enzyme is significantly impaired in proteolytic self-cleavage Chlamydia pneumoniae

Inhibitors

Inhibitors Comment Organism Structure
L-argininamide 33% inhibition at 2 mM Chlamydia pneumoniae
O-methyl hydroxylamine 69% inhibition at 2 mM Chlamydia pneumoniae
O-nitrobenzylhydroxylamine 75% inhibition at 2 mM Chlamydia pneumoniae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics Chlamydia pneumoniae
0.03
-
 L-arginine pH 8.4, 37°C, constitutive ArgDC Escherichia coli
0.65
-
 L-arginine pH 5.2, 37°C, inducible ArgDC Escherichia coli
5
-
 L-arginine pH 3.5, 37°C Chlamydia pneumoniae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
9000
-
 3 * 16000, alpha subunit, + 3 * 9000, beta-subunit, trimeric dimer, (alpha/beta)3, SDS-PAGE Chlamydia pneumoniae
16000
-
 3 * 16000, alpha subunit, + 3 * 9000, beta-subunit, trimeric dimer, (alpha/beta)3, SDS-PAGE Chlamydia pneumoniae
88000
-
 recombinant enzyme, gel filtration Chlamydia pneumoniae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-arginine Chlamydia pneumoniae
-
 agmatine + CO2
-
 ?
L-arginine Escherichia coli the AdiA enzyme is required by the AR3 arginine-dependent acid resistance system agmatine + CO2
-
 ?
L-arginine Chlamydia pneumoniae Kajaani 6
-
 agmatine + CO2
-
 ?
additional information Chlamydia pneumoniae acting together with a putative arginine-agmatine antiporter, the CPn1032 homologs may have evolved convergently to form an arginine-dependent acid resistance system, this system could reduce the host cell arginine concentration and produce inhibitors of nitric oxide synthase, obligately intracellular chlamydiae may encounter acidic conditions, overview ?
-
 ?
additional information Chlamydia pneumoniae Kajaani 6 acting together with a putative arginine-agmatine antiporter, the CPn1032 homologs may have evolved convergently to form an arginine-dependent acid resistance system, this system could reduce the host cell arginine concentration and produce inhibitors of nitric oxide synthase, obligately intracellular chlamydiae may encounter acidic conditions, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Chlamydia pneumoniae
-
 gene CPn1032
-
Chlamydia pneumoniae Kajaani 6
-
 gene CPn1032
-
Escherichia coli P28629 gene adiA, inducible and constitutive ArgDCs
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the recombinant enzyme self-cleaved to form a reactive pyruvoyl group, and the subunits assembled into a thermostable (alpha/beta)3 complex Chlamydia pneumoniae

Purification (Commentary)

Purification (Comment) Organism
recombinant His10-tagged enzyme from Escherichia coli strain Bl21(DE3) by nickel affinity chromatography, recombinant untagged enzyme from Escherichia coli strain Bl21(DE3) by anion exchange chromatography, most of the protein is found in the insoluble portion of cell lysate Chlamydia pneumoniae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 arginine-dependent acid resistance assay, overview Chlamydia pneumoniae
8.1
-
 purified recombinant enzyme Chlamydia pneumoniae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginine
-
 Chlamydia pneumoniae agmatine + CO2
-
 ?
L-arginine
-
 Escherichia coli agmatine + CO2
-
 ?
L-arginine the AdiA enzyme is required by the AR3 arginine-dependent acid resistance system Escherichia coli agmatine + CO2
-
 ?
L-arginine
-
 Chlamydia pneumoniae Kajaani 6 agmatine + CO2
-
 ?
L-canavanine
-
 Chlamydia pneumoniae gamma-guanidinoxypropylamine + CO2
-
 ?
L-canavanine
-
 Chlamydia pneumoniae Kajaani 6 gamma-guanidinoxypropylamine + CO2
-
 ?
additional information acting together with a putative arginine-agmatine antiporter, the CPn1032 homologs may have evolved convergently to form an arginine-dependent acid resistance system, this system could reduce the host cell arginine concentration and produce inhibitors of nitric oxide synthase, obligately intracellular chlamydiae may encounter acidic conditions, overview Chlamydia pneumoniae ?
-
 ?
additional information the enzyme is highly substrate specific, no activity with D-arginine, L-aspartate, L-citrulline, L-glutamine, L-histidine, L-homoarginine, L-lysine, N-methyl-Larginine, and L-ornithine Chlamydia pneumoniae ?
-
 ?
additional information acting together with a putative arginine-agmatine antiporter, the CPn1032 homologs may have evolved convergently to form an arginine-dependent acid resistance system, this system could reduce the host cell arginine concentration and produce inhibitors of nitric oxide synthase, obligately intracellular chlamydiae may encounter acidic conditions, overview Chlamydia pneumoniae Kajaani 6 ?
-
 ?
additional information the enzyme is highly substrate specific, no activity with D-arginine, L-aspartate, L-citrulline, L-glutamine, L-histidine, L-homoarginine, L-lysine, N-methyl-Larginine, and L-ornithine Chlamydia pneumoniae Kajaani 6 ?
-
 ?

Subunits

Subunits Comment Organism
hexamer 3 * 16000, alpha subunit, + 3 * 9000, beta-subunit, trimeric dimer, (alpha/beta)3, SDS-PAGE Chlamydia pneumoniae
More the recombinant enzyme self-cleaved to form a reactive pyruvoyl group, and the subunits assembled into a thermostable (alpha/beta)3 complex Chlamydia pneumoniae

Synonyms

Synonyms Comment Organism
AdiA
-
 Escherichia coli
ARGDC
-
 Chlamydia pneumoniae
ARGDC
-
 Escherichia coli
CPn1032 homolog
-
 Chlamydia pneumoniae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli
47
-
-
 Chlamydia pneumoniae

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 80 about 50% of maximal activity at 20°C and 80°C Chlamydia pneumoniae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 10 min, the purified enzyme retains 48% of maximal activity Chlamydia pneumoniae
100
-
 10 min, the purified enzyme retains 13% of maximal activity Chlamydia pneumoniae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.9
-
 L-arginine pH 3.5, 37°C Chlamydia pneumoniae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4
-
-
 Chlamydia pneumoniae
5.2
-
 inducible ArgDC Escherichia coli
8.4
-
 constitutive ArgDC Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
1.5 5.5 activity range Chlamydia pneumoniae

Cofactor

Cofactor Comment Organism Structure
additional information The serine residue at N terminus of the {alpha} subunit forms a reactive pyruvoyl group that functions analogously to pyridoxal 5'-phosphate Chlamydia pneumoniae
pyridoxal 5'-phosphate dependent on Escherichia coli