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Literature summary for 1.14.18.1 extracted from

  • Selinheimo, E.; Saloheimo, M.; Ahola2, E.; Westerholm-Parvinen, A.; Kalkkinen, N.; Buchert, J.; Kruus, K.
    Production and characterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei (2006), FEBS J., 273, 4322-4335.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene tyr2, DNA and amino acid sequence determination and analysis, overexpression in the native host under the strong cbh1 promoter, secretion of the recombinant enzyme into the culture supernatant Trichoderma reesei

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ copper-containing metalloprotein Trichoderma reesei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43200
-
x * 43200, recombinant enzyme, SDS-PAGE, x * 61 151, unprocessed enzyme, sequence calculation, 43 124-43 204, recombinant enzyme, mass spectrometry Trichoderma reesei

Organism

Organism UniProt Comment Textmining
Trichoderma reesei
-
gene tyr2
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein recombinant secreted enzyme, glycosylated at its only potential N-glycosylation site, with a glycan consisting of two N-acetylglucosamines and five mannoses, low amounts of shorter glycan forms can be detected at this site Trichoderma reesei
proteolytic modification the mature protein is processed from the C-terminus by a cleavage of a peptide fragment of about 20 kDa Trichoderma reesei

Purification (Commentary)

Purification (Comment) Organism
recombinant secreted enzyme 4.9fold from culture supernatant by gel filtration, cation exchange chromatography, and size exclusion chromatography to homogeneity Trichoderma reesei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-coumaric acid + O2
-
Trichoderma reesei ?
-
?
4-tyrosol + O2
-
Trichoderma reesei ?
-
?
glycyl-glycyl-L-tyrosine + O2 3.4fold higher activity compared to Tyr Trichoderma reesei ?
-
?
glycyl-L-tyrosine + O2 2.9fold higher activity compared to Tyr Trichoderma reesei ?
-
?
L-tyrosine + O2 + AH2 nearly no activity with the D-isomer, 7% of the activity with the L-isomer Trichoderma reesei L-dopa + H2O + A
-
?
additional information broad substrate specificity, overview, no or poor activity with 4-aminophenol, 3-hydroxyanthranilic acid, tyramine, 2-coumaric acid, ferulic acid, and aniline, tyrosinase is a mono-oxygenase and a bifunctional enzyme that catalyzes the o-hydroxylation of monophenols and subsequent oxidation of o-diphenols to quinones, the enzyme thus accepts monophenols and diphenols as substrates, and the monophenolase activity is the initial rate-determining reaction Trichoderma reesei ?
-
?
phenol + O2 low activity Trichoderma reesei ?
-
?

Subunits

Subunits Comment Organism
? x * 43200, recombinant enzyme, SDS-PAGE, x * 61 151, unprocessed enzyme, sequence calculation, 43 124-43 204, recombinant enzyme, mass spectrometry Trichoderma reesei
More N-terminal and C-terminal structural analyses by fragmentation, chromatography, MS and peptide sequencing of the purified recombinant enzyme, overview Trichoderma reesei

Synonyms

Synonyms Comment Organism
cresolase
-
Trichoderma reesei
monophenol, o-diphenol:oxygen oxidoreductase
-
Trichoderma reesei
monophenolase
-
Trichoderma reesei
tyrosinase
-
Trichoderma reesei

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
recombinant enzyme Trichoderma reesei

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30
-
purified recombinant enzyme, half-life: 18 h Trichoderma reesei
40
-
purified recombinant enzyme, half-life: 3,75 h Trichoderma reesei
50
-
purified recombinant enzyme, half-life: 15 min Trichoderma reesei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
recombinant enzyme Trichoderma reesei

pH Range

pH Minimum pH Maximum Comment Organism
6 9.5 highest activity and stability within a neutral and alkaline pH range Trichoderma reesei

pH Stability

pH Stability pH Stability Maximum Comment Organism
additional information
-
highest activity and stability within a neutral and alkaline pH range Trichoderma reesei
4
-
1 h, purified recombinant enzyme, complete loss of activity Trichoderma reesei
5
-
1 h, purified recombinant enzyme, loss of 50% activity Trichoderma reesei
7
-
stable at Trichoderma reesei

pI Value

Organism Comment pI Value Maximum pI Value
Trichoderma reesei isoelectric focusing
-
9.5