Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.10.3.2 extracted from

  • Uthandi, S.; Prunetti, L.; De Vera, I.M.; Fanucci, G.E.; Angerhofer, A.; Maupin-Furlow, J.A.
    Enhanced archaeal laccase production in recombinant Escherichia coli by modification of N-terminal propeptide and twin arginine translocation motifs (2012), J. Ind. Microbiol. Biotechnol., 39, 1523-1532.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.10.3.2

Cloned(Commentary)

Cloned (Comment) Organism
the lccA gene sequence is mutated to encode LccA with either a modified twin-arginine translocation (TAT) motif (R6K R7K R8K or Dtat) or deletion of its N-terminal propeptide (DMet1 to Ala31 of the deduced polypeptide or Dpro). With this approach, the enzyme is produced at high levels in recombinant Escherichia coli grown in medium supplemented with 0.25 mM CuSO4 Haloferax volcanii

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Haloferax volcanii
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ multicopper enzyme, copper is not fully incorporated into the type-I Cu center of Escherichia coli purified enzyme. Typical metal content of laccases includes a type-1 Cu site (T1), a type-2 Cu site (T2), and a dinuclear type-3 Cu site (T3), with T2 and T3 arranged in a trinuclear cluster. The T1 Cu site contains the blue copper, whose tight coordination to a cysteine is responsible for an intense SCys -> Cu(II) charge transfer transition at around 600 nm, giving the typical blue color to the enzyme. T2 shows a characteristic electron paramagnetic resonance (EPR) spectrum, clearly distinct from that of T1, whereas the T3 copper dimer is anti-ferromagnetically coupled and EPR-silent Haloferax volcanii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
74000
-
 1 * 74000 Haloferax volcanii

Organism

Organism UniProt Comment Textmining
Haloferax volcanii D4GPK6
-
-
Haloferax volcanii DSM 3757 D4GPK6
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Haloferax volcanii

Source Tissue

Source Tissue Comment Organism Textmining
culture medium
-
 Haloferax volcanii
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
25
-
 pH 8.4, 45°C Haloferax volcanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
syringaldazine + O2
-
 Haloferax volcanii ?
-
 ?
syringaldazine + O2
-
 Haloferax volcanii DSM 3757 ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 74000 Haloferax volcanii

Synonyms

Synonyms Comment Organism
Hvo_B0205
-
 Haloferax volcanii
LccA
-
 Haloferax volcanii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
 assay at Haloferax volcanii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.4
-
 assay at Haloferax volcanii