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Literature summary 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

Activating Compound

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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.10.3.2 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

EC Number Inhibitors Comment Organism Structure
1.10.3.2 1,10-phenanthroline 1 mM, 14.7% loss of activity. 10 mM, 89.1% loss of activity Haloferax volcanii
1.10.3.2 2,2-dipyridyl 1 mM, 13.4% loss of activity. 10 mM, 24.8% loss of activity Haloferax volcanii
1.10.3.2 DL-dithiothreitol 0.01 mM, 9.5% loss of activity. 0.1 mM, complete loss of activity Haloferax volcanii
1.10.3.2 L-cysteine 0.1 mM, 17% loss of activity. 1 mM, complete loss of activity Haloferax volcanii
1.10.3.2 Sodium azide 1 mM, 33.8% loss of activity Haloferax volcanii
1.10.3.2 Thiourea 1 mM, 4.5% loss of activity. 10 mM, 90.4% loss of activity Haloferax volcanii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.10.3.2 0.035
-
 syringaldazine 45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii
1.10.3.2 0.236
-
 bilirubin 45°C, pH 8.4, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii
1.10.3.2 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

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.10.3.2 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
1.10.3.2 CuSO4 oxidation of dimethoxyphenol requires the addition of CuSO4 Haloferax volcanii
1.10.3.2 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
1.10.3.2 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.10.3.2 63397
-
 x * 63397, calculation from sequence Haloferax volcanii

Organic Solvent Stability

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

Organism

EC Number Organism UniProt Comment Textmining
1.10.3.2 Haloferax volcanii D4GPK6
-
-
1.10.3.2 Haloferax volcanii DSM 3757 D4GPK6
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.10.3.2 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
1.10.3.2 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)

EC Number Purification (Comment) Organism
1.10.3.2
-
 Haloferax volcanii

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.10.3.2 culture medium
-
 Haloferax volcanii
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.10.3.2 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) + O2
-
 Haloferax volcanii ?
-
 ?
1.10.3.2 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) + O2
-
 Haloferax volcanii DSM 3757 ?
-
 ?
1.10.3.2 2,6-dimethoxyphenol + O2
-
 Haloferax volcanii ?
-
 ?
1.10.3.2 2,6-dimethoxyphenol + O2
-
 Haloferax volcanii DSM 3757 ?
-
 ?
1.10.3.2 bilirubin + O2
-
 Haloferax volcanii ?
-
 ?
1.10.3.2 bilirubin + O2
-
 Haloferax volcanii DSM 3757 ?
-
 ?
1.10.3.2 syringaldazine + O2
-
 Haloferax volcanii ?
-
 ?
1.10.3.2 syringaldazine + O2
-
 Haloferax volcanii DSM 3757 ?
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.10.3.2 LccA
-
 Haloferax volcanii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.10.3.2 45
-
 optimal oxidation of syringaldazine and 2,2,-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) Haloferax volcanii

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.10.3.2 21 60 21°C: 75% of maximal activity, 60°C: 40-50% of maximal activity Haloferax volcanii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.10.3.2 37
-
 2.5 d, the enzyme retains nearly all of its original activity Haloferax volcanii
1.10.3.2 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
1.10.3.2 50
-
 fully active after 5 h at 50°C. Half-life: 1 day Haloferax volcanii
1.10.3.2 55
-
 the enzyme is fully active after 1 h at 55°C Haloferax volcanii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.10.3.2 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
1.10.3.2 22
-
 syringaldazine 45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii
1.10.3.2 29
-
 bilirubin 45°C, pH 8.4, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.10.3.2 6
-
 optimal oxidation of 2,2,-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) Haloferax volcanii
1.10.3.2 8.5
-
 optimal oxidation of syringaldazine Haloferax volcanii

pI Value

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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.10.3.2 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
1.10.3.2 123
-
 bilirubin 45°C, pH 8.4, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii
1.10.3.2 628
-
 syringaldazine 45°C, pH 6.0, LccA protein isolated from Haloferax volcanii H26 strain US02 Haloferax volcanii