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Literature summary for 1.11.1.14 extracted from

  • Min, K.; Yum, T.; Kim, J.; Woo, H.M.; Kim, Y.; Sang, B.I.; Yoo, Y.J.; Kim, Y.H.; Um, Y.
    Perspectives for biocatalytic lignin utilization cleaving 4-O-5 and Calpha-Cbeta bonds in dimeric lignin model compounds catalyzed by a promiscuous activity of tyrosinase (2017), Biotechnol. Biofuels, 10, 212 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.11.1.14

Application

Application Comment Organism
industry the enzyme can be used as biocatalytic in delignification (which is emerging owing to its superior selectivity, low energy consumption, and unparalleled sustainability) iIn the biorefinery utilizing lignocellulosic biomasses, lignin decomposition to value-added phenolic derivatives Agaricus bisporus
industry the enzyme can be used as biocatalytic in delignification (which is emerging owing to its superior selectivity, low energy consumption, and unparalleled sustainability) iIn the biorefinery utilizing lignocellulosic biomasses, lignin decomposition to value-added phenolic derivatives Phanerodontia chrysosporium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information comparison of kinetic parameters of tyrosinase (EC 1.14.18.1) and lignin peroxidase (EC 1.11.1.14) (LiP) using veratryl alcohol as the substrate, overview Agaricus bisporus
additional information
-
 additional information comparison of kinetic parameters of tyrosinase (EC 1.14.18.1) and lignin peroxidase (EC 1.11.1.14) (LiP) using veratryl alcohol as the substrate, overview Phanerodontia chrysosporium
0.31
-
 veratryl alcohol pH 6.5, 30°C Agaricus bisporus
3.54
-
 veratryl alcohol pH 6.5, 30°C Phanerodontia chrysosporium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Agaricus bisporus tyrosinase (EC 1.14.18.1) has a promiscuous activity for oxidizing the lignin-related nonphenolic substrate veratryl alcohol, catalyzing the reaction of heme-containing lignin peroxidase, LiP, EC 1.11.1.14. Tyrosinase exhibits a broad substrate specificity for various phenolic compounds ?
-
 ?
veratryl alcohol + H2O2 Agaricus bisporus
-
 veratraldehyde + H2O
-
 ?
veratryl alcohol + H2O2 Phanerodontia chrysosporium
-
 veratraldehyde + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Agaricus bisporus
-
-
-
Phanerodontia chrysosporium
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Agaricus bisporus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0525
-
 substrate veratryl alcohol, pH 6.5, 30°C Agaricus bisporus
0.77
-
 substrate 4-phenoxyphenol, pH 6.5, 30°C Agaricus bisporus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-phenoxyphenol + H2O2 cleavage of 4-O-5 bond in 4-phenoxyphenol by the catalytic promiscuity of tyrosinase Agaricus bisporus phenol + 1,4-benzoquinone
-
 ?
guaiacyl glycerol-beta-guaiacyl ether + H2O2 a dimeric lignin model compound, derivatization with tetramethylsilane is carried out to analyze guaiacyl glycerol-beta-guaiacyl ether, GGE. The catalytic promiscuity of tyrosinase seemed to cleave the Calpha-Cbeta bond in GGE, yielding vanillin and possibly an unstable o-(2-hydroxyethyl)guaiacol radical. The unstable o-(2-hydroxyethyl)guaiacol radical might be further catalyzed to guaiacol and 2-hydroxyacetaldehyde by the tyrosinase, and then guaiacol might be polymerized to an unidentified product Agaricus bisporus vanillin + guaiacol + 2-hydroxyacetaldehyde + H2O
-
 ?
additional information tyrosinase (EC 1.14.18.1) has a promiscuous activity for oxidizing the lignin-related nonphenolic substrate veratryl alcohol, catalyzing the reaction of heme-containing lignin peroxidase, LiP, EC 1.11.1.14. Tyrosinase exhibits a broad substrate specificity for various phenolic compounds Agaricus bisporus ?
-
 ?
veratryl alcohol + H2O2
-
 Agaricus bisporus veratraldehyde + H2O
-
 ?
veratryl alcohol + H2O2
-
 Phanerodontia chrysosporium veratraldehyde + H2O
-
 ?

Synonyms

Synonyms Comment Organism
heme-containing lignin peroxidase
-
 Phanerodontia chrysosporium
heme-containing peroxidase
-
 Phanerodontia chrysosporium
LIP
-
 Phanerodontia chrysosporium
mushroom tyrosinase
-
 Agaricus bisporus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Agaricus bisporus
30
-
 assay at Phanerodontia chrysosporium

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.12
-
 veratryl alcohol pH 6.5, 30°C Agaricus bisporus
13.72
-
 veratryl alcohol pH 6.5, 30°C Phanerodontia chrysosporium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 assay at Agaricus bisporus
6.5
-
 assay at Phanerodontia chrysosporium

Cofactor

Cofactor Comment Organism Structure
heme
-
 Phanerodontia chrysosporium

General Information

General Information Comment Organism
physiological function the promiscuous activity of tyrosinase not only oxidizes veratryl alcohol, a commonly used nonphenolic substrate for assaying ligninolytic activity, to veratraldehyde but also cleaves the 4-O-5 and Calpha-Cbeta bonds in 4-phenoxyphenol and guaiacyl glycerol-beta-guaiacyl ether (GGE) that are dimeric lignin model compounds. The promiscuous activity oxidizes lignin-related high redox potential substrates Agaricus bisporus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.39
-
 veratryl alcohol pH 6.5, 30°C Agaricus bisporus
3.88
-
 veratryl alcohol pH 6.5, 30°C Phanerodontia chrysosporium