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

BRENDA support

Literature summary extracted from

  • Garcia, T.A.; Santiago, M.F.; Ulhoa, C.J.
    Studies on the Pycnoporus sanguineus CCT-4518 laccase purified by hydrophobic interaction chromatography (2007), Appl. Microbiol. Biotechnol., 75, 311-318.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.10.3.2 2-mercaptoethanol 93% inhibition at 1 mM Trametes sanguinea
1.10.3.2 HgCl2 46% inhibition at 51 mM Trametes sanguinea
1.10.3.2 L-cysteine 98% inhibition at 1 mM Trametes sanguinea
1.10.3.2 additional information no inhibition by DMSO up to 25 mM Trametes sanguinea
1.10.3.2 NaF 53% inhibition at 0.1 mM Trametes sanguinea
1.10.3.2 NaN3 77% inhibition at 0.01 mM Trametes sanguinea

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.10.3.2 0.0083
-
 syringaldazine pH 4.2, 50°C Trametes sanguinea
1.10.3.2 0.058
-
 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) pH 4.2, 50°C Trametes sanguinea
1.10.3.2 0.37
-
 guaiacol pH 4.2, 50°C Trametes sanguinea

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.10.3.2 Cu2+ a multicopper oxidase Trametes sanguinea

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.10.3.2 68000
-
 gel filtration Trametes sanguinea
1.10.3.2 69000
-
 1 * 69000, SDS-PAGE Trametes sanguinea

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.10.3.2 additional information Trametes sanguinea laccase couples catalytic oxidation of lignin with the four electron reduction of oxygen, the final product is water without any harmful intermediate making laccase the best candidate for the environmentally benign bleaching process ?
-
 ?
1.10.3.2 additional information Trametes sanguinea CCT-4518 laccase couples catalytic oxidation of lignin with the four electron reduction of oxygen, the final product is water without any harmful intermediate making laccase the best candidate for the environmentally benign bleaching process ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.10.3.2 Trametes sanguinea
-
-
-
1.10.3.2 Trametes sanguinea CCT-4518
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.10.3.2 native enzyme purified 54.1fold by two steps of hydrophobic interaction chromatography 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 20
-
 purified enzyme, substrate syringaldazine Trametes sanguinea

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.10.3.2 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
-
 Trametes sanguinea ?
-
 ?
1.10.3.2 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
-
 Trametes sanguinea CCT-4518 ?
-
 ?
1.10.3.2 2,6-dimethoxyphenol + O2 preferred substrate Trametes sanguinea 3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O i.e. coerulignone ?
1.10.3.2 2,6-dimethoxyphenol + O2 preferred substrate Trametes sanguinea CCT-4518 3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O i.e. coerulignone ?
1.10.3.2 guaiacol + O2
-
 Trametes sanguinea ?
-
 ?
1.10.3.2 additional information laccase couples catalytic oxidation of lignin with the four electron reduction of oxygen, the final product is water without any harmful intermediate making laccase the best candidate for the environmentally benign bleaching process Trametes sanguinea ?
-
 ?
1.10.3.2 additional information substrate specificity, overview, no activity with tyrosine, phenol, vanillin, and gallic acid Trametes sanguinea ?
-
 ?
1.10.3.2 additional information laccase couples catalytic oxidation of lignin with the four electron reduction of oxygen, the final product is water without any harmful intermediate making laccase the best candidate for the environmentally benign bleaching process Trametes sanguinea CCT-4518 ?
-
 ?
1.10.3.2 additional information substrate specificity, overview, no activity with tyrosine, phenol, vanillin, and gallic acid Trametes sanguinea CCT-4518 ?
-
 ?
1.10.3.2 syringaldazine + O2
-
 Trametes sanguinea ?
-
 ?
1.10.3.2 syringaldazine + O2
-
 Trametes sanguinea CCT-4518 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.10.3.2 monomer 1 * 69000, SDS-PAGE Trametes sanguinea

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.10.3.2 50
-
 with substrate syringaldazine Trametes sanguinea

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.10.3.2 35 55
-
 Trametes sanguinea

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.10.3.2 50
-
 purified enzyme, 93% remaining activity after 24 h, 76% remaining activity after 48 h Trametes sanguinea
1.10.3.2 60
-
 purified enzyme, 2 h, 80% remaining activity Trametes sanguinea
1.10.3.2 70
-
 purified enzyme, 2 h, 40% remaining activity Trametes sanguinea
1.10.3.2 80
-
 purified enzyme, 2 h, 5% remaining activity, half-life at 80°C is 20 min Trametes sanguinea

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.10.3.2 4.2
-
 with substrate syringaldazine Trametes sanguinea