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Literature summary for 1.10.3.2 extracted from

  • Uthandi, S.; Saad, B.; Humbard, M.A.; Maupin-Furlow, J.A.
    LccA, an archaeal laccase secreted as a highly stable glycoprotein into the extracellular medium by Haloferax volcanii (2010), Appl. Environ. Microbiol., 76, 733-743.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.10.3.2

Activating Compound

Activating Compound Comment Organism Structure
EDTA 5 mM, 1.2fold activation Haloferax volcanii

Cloned(Commentary)

Cloned (Comment) Organism
the expression plasmids (pJAM822 and pJAM824) are transformed into Haloferax volcanii H26 to generate strains SB01 and US02 for high-level synthesis of LccA with and without a C-terminal StrepII tag Haloferax volcanii

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline 1 mM, 14.7% loss of activity. 10 mM, 89.1% loss of activity Haloferax volcanii
2,2-dipyridyl 1 mM, 13.4% loss of activity. 10 mM, 24.8% loss of activity Haloferax volcanii
DL-dithiothreitol 0.01 mM, 9.5% loss of activity. 0.1 mM, complete loss of activity Haloferax volcanii
L-cysteine 0.1 mM, 17% loss of activity. 1 mM, complete loss of activity Haloferax volcanii
Sodium azide 1 mM, 33.8% loss of activity Haloferax volcanii
Thiourea 1 mM, 4.5% loss of activity. 10 mM, 90.4% loss of activity Haloferax volcanii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.035
-
 syringaldazine 45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii
0.236
-
 bilirubin 45°C, pH 8.4, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii
0.67
-
 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) 45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular secreted as a highly stable glycoprotein into the extracellular medium Haloferax volcanii
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
copper the enzyme is modified posttranslationally, including removal of 31 amino acid residues from its N terminus, addition of glycan residues (glycosylation), and apparent coordination of four copper atoms into three types of copper-binding sites Haloferax volcanii
CuSO4 oxidation of dimethoxyphenol requires the addition of CuSO4 Haloferax volcanii
KCl activity is optimal at 200 mM salt, with 1.5fold greater activity in KCl than in NaCl, and the enzyme displays reduced activity after the removal of salt by dialysis Haloferax volcanii
NaCl activity is optimal at 200 mM salt, with 1.5fold greater activity in KCl than in NaCl, and the enzyme displays reduced activity after the removal of salt by dialysis. Also active at relatively high concentrations of salt, with 65% activity at 1 M NaCl Haloferax volcanii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
63397
-
 x * 63397, calculation from sequence Haloferax volcanii

Organic Solvent Stability

Organic Solvent Comment Organism
dimethyl sulfoxide 25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 50% of its activity Haloferax volcanii
dimethylformamide 25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 50% of its activity Haloferax volcanii
Ethanol 25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 75% of its activity Haloferax volcanii
Methanol 25% (v/v), 185 mM NaCl, 24 h, the enzyme retains nearly 75% of its activity Haloferax volcanii

Organism

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

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the enzyme is modified posttranslationally, including removal of 31 amino acid residues from its N terminus, addition of glycan residues (glycosylation), and apparent coordination of four copper atoms into three types of copper-binding sites Haloferax volcanii
proteolytic modification the enzyme is modified posttranslationally, including removal of 31 amino acid residues from its N terminus, addition of glycan residues (glycosylation), and apparent coordination of four copper atoms into three types of copper-binding sites Haloferax volcanii

Purification (Commentary)

Purification (Comment) Organism
-
 Haloferax volcanii

Source Tissue

Source Tissue Comment Organism Textmining
culture medium
-
 Haloferax volcanii
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) + O2
-
 Haloferax volcanii ?
-
 ?
2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) + O2
-
 Haloferax volcanii DSM 3757 ?
-
 ?
2,6-dimethoxyphenol + O2
-
 Haloferax volcanii ?
-
 ?
2,6-dimethoxyphenol + O2
-
 Haloferax volcanii DSM 3757 ?
-
 ?
bilirubin + O2
-
 Haloferax volcanii ?
-
 ?
bilirubin + O2
-
 Haloferax volcanii DSM 3757 ?
-
 ?
syringaldazine + O2
-
 Haloferax volcanii ?
-
 ?
syringaldazine + O2
-
 Haloferax volcanii DSM 3757 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 63397, calculation from sequence Haloferax volcanii
? x * 75000-80000, LccA protein isolated from Haloferax volcanii H26 strain US02, SDS-PAGE Haloferax volcanii

Synonyms

Synonyms Comment Organism
LccA
-
 Haloferax volcanii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
 optimal oxidation of syringaldazine and 2,2,-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) Haloferax volcanii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
21 60 21°C: 75% of maximal activity, 60°C: 40-50% of maximal activity Haloferax volcanii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
 2.5 d, the enzyme retains nearly all of its original activity Haloferax volcanii
45 50 the enzyme retains 35 to 60% of its activity at 45°C to 50°C after incubation for 2.5 days Haloferax volcanii
50
-
 fully active after 5 h at 50°C. Half-life: 1 day Haloferax volcanii
55
-
 the enzyme is fully active after 1 h at 55°C Haloferax volcanii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
10
-
 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) 45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii
22
-
 syringaldazine 45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii
29
-
 bilirubin 45°C, pH 8.4, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 optimal oxidation of 2,2,-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) Haloferax volcanii
8.5
-
 optimal oxidation of syringaldazine Haloferax volcanii

pI Value

Organism Comment pI Value Maximum pI Value
Haloferax volcanii calculated from sequence
-
 4.34

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
15
-
 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) 45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii
123
-
 bilirubin 45°C, pH 8.4, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii
628
-
 syringaldazine 45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii