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Literature summary extracted from

  • Vite-Vallejo, O.; Palomares, L.; Dantan-Gonzalez, E.; Ayala-Castro, H.; Marti­nez-Anaya, C.; Valderrama, B.; Folch-Mallol, J.
    The role of N-glycosylation on the enzymatic activity of a Pycnoporus sanguineus laccase (2009), Enzyme Microb. Technol., 45, 233-239.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.10.3.2 DNA and amino acid sequence determination and analysis Trametes sanguinea

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.10.3.2 Urea inactivation at 5 M, 50% inhibition at about 2 M Trametes sanguinea

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.10.3.2 0.015
-
 2-dianisidine pH 4.5, 22°C, deglycosylated enzyme Trametes sanguinea
1.10.3.2 0.044
-
 2-dianisidine pH 4.5, 22°C, native enzyme Trametes sanguinea
1.10.3.2 0.102
-
 2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid) pH 4.5, 22°C, deglycosylated enzyme Trametes sanguinea
1.10.3.2 0.102
-
 syringaldazine pH 4.5, 22°C, native enzyme Trametes sanguinea
1.10.3.2 0.106
-
 2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid) pH 4.5, 22°C, native enzyme Trametes sanguinea
1.10.3.2 0.156
-
 syringaldazine pH 4.5, 22°C, deglycosylated enzyme Trametes sanguinea
1.10.3.2 0.25
-
 guaiacol pH 4.5, 22°C, native enzyme Trametes sanguinea
1.10.3.2 0.367
-
 guaiacol pH 4.5, 22°C, deglycosylated enzyme Trametes sanguinea

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.10.3.2 Cu2+ the enzyme contains 4 copper molecules per enzyme molecule, structure overview Trametes sanguinea

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.10.3.2 68000
-
 x * 68000, SDS-PAGE Trametes sanguinea

Organism

EC Number Organism UniProt Comment Textmining
1.10.3.2 Trametes sanguinea C1JCL7
-
-
1.10.3.2 Trametes sanguinea CeIBMD001 C1JCL7
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.10.3.2 glycoprotein the enzyme is N-glycosylated, five possible N-glycosylation sites at N74, N237, N311, N354, and N362, profile, overview Trametes sanguinea

Purification (Commentary)

EC Number Purification (Comment) Organism
1.10.3.2 native enzyme by ammonium sulfate fractionation, cation exchange chromatography, ultrafiltration, and gel filtration to homogeneity Trametes sanguinea

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.10.3.2 mycelium
-
 Trametes sanguinea
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.10.3.2 69
-
 purified native enzyme, substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid Trametes sanguinea

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.10.3.2 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
-
 Trametes sanguinea ?
-
 ?
1.10.3.2 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
-
 Trametes sanguinea CeIBMD001 ?
-
 ?
1.10.3.2 2-dianisidine + O2
-
 Trametes sanguinea ?
-
 ?
1.10.3.2 2-dianisidine + O2
-
 Trametes sanguinea CeIBMD001 ?
-
 ?
1.10.3.2 guaiacol + O2
-
 Trametes sanguinea ?
-
 ?
1.10.3.2 guaiacol + O2
-
 Trametes sanguinea CeIBMD001 ?
-
 ?
1.10.3.2 syringaldazine + O2
-
 Trametes sanguinea ?
-
 ?
1.10.3.2 syringaldazine + O2
-
 Trametes sanguinea CeIBMD001 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.10.3.2 ? x * 68000, SDS-PAGE Trametes sanguinea
1.10.3.2 More three-dimensional structure modelling, overview Trametes sanguinea

Synonyms

EC Number Synonyms Comment Organism
1.10.3.2 More the enzyme is a blue laccase Trametes sanguinea

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.10.3.2 22
-
 assay at room temperature Trametes sanguinea

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.10.3.2 30 90 activity range Trametes sanguinea

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.10.3.2 20 70 temperature stability profiles of native and deglycosylated enzymes, overview Trametes sanguinea

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.10.3.2 2.05
-
 guaiacol pH 4.5, 22°C, native enzyme Trametes sanguinea
1.10.3.2 3
-
 guaiacol pH 4.5, 22°C, deglycosylated enzyme Trametes sanguinea
1.10.3.2 4.9
-
 2-dianisidine pH 4.5, 22°C, deglycosylated enzyme Trametes sanguinea
1.10.3.2 9.4
-
 2-dianisidine pH 4.5, 22°C, native enzyme Trametes sanguinea
1.10.3.2 39.9
-
 syringaldazine pH 4.5, 22°C, native enzyme Trametes sanguinea
1.10.3.2 48.6
-
 2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid) pH 4.5, 22°C, deglycosylated enzyme Trametes sanguinea
1.10.3.2 59.3
-
 2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid) pH 4.5, 22°C, native enzyme Trametes sanguinea
1.10.3.2 65.8
-
 syringaldazine pH 4.5, 22°C, deglycosylated enzyme Trametes sanguinea

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.10.3.2 4.5
-
 assay at, substrate 2,2'-azinobis(3-ethylbenzo-6-thiazolinesulfonic) acid Trametes sanguinea

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.10.3.2 3 10
-
 Trametes sanguinea

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.10.3.2 Trametes sanguinea isoelectric focussing
-
 4.5