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Literature summary for 1.10.3.2 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

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?
-
?
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

Organism UniProt Comment Textmining
Trametes sanguinea
-
-
-
Trametes sanguinea CCT-4518
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme purified 54.1fold by two steps of hydrophobic interaction chromatography Trametes sanguinea

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
20
-
purified enzyme, substrate syringaldazine Trametes sanguinea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
-
Trametes sanguinea ?
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
-
Trametes sanguinea CCT-4518 ?
-
?
2,6-dimethoxyphenol + O2 preferred substrate Trametes sanguinea 3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O i.e. coerulignone ?
2,6-dimethoxyphenol + O2 preferred substrate Trametes sanguinea CCT-4518 3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O i.e. coerulignone ?
guaiacol + O2
-
Trametes sanguinea ?
-
?
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 ?
-
?
additional information substrate specificity, overview, no activity with tyrosine, phenol, vanillin, and gallic acid Trametes sanguinea ?
-
?
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 ?
-
?
additional information substrate specificity, overview, no activity with tyrosine, phenol, vanillin, and gallic acid Trametes sanguinea CCT-4518 ?
-
?
syringaldazine + O2
-
Trametes sanguinea ?
-
?
syringaldazine + O2
-
Trametes sanguinea CCT-4518 ?
-
?

Subunits

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

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

pH Optimum

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