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

BRENDA support

Literature summary 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)

EC Number Cloned (Comment) Organism
1.10.3.1 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
1.14.18.1 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.10.3.1 benzaldehyde
-
Trichoderma reesei
1.10.3.1 EDTA
-
Trichoderma reesei
1.10.3.1 additional information no inhibition by kojic acid and 2-mercaptoethanol Trichoderma reesei
1.10.3.1 NaCl
-
Trichoderma reesei
1.10.3.1 SDS
-
Trichoderma reesei
1.10.3.1 Sodium azide
-
Trichoderma reesei

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.10.3.1 Cu2+ copper-containing metalloprotein Trichoderma reesei
1.14.18.1 Cu2+ copper-containing metalloprotein Trichoderma reesei

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.10.3.1 43200
-
x * 43200, recombinant enzyme, SDS-PAGE, x * 61151, unprocessed enzyme, sequence calculation, 43 124-43 204, recombinant enzyme, mass spectrometry Trichoderma reesei
1.10.3.1 61151
-
x * 43200, recombinant enzyme, SDS-PAGE, x * 61151, unprocessed enzyme, sequence calculation, 43 124-43 204, recombinant enzyme, mass spectrometry Trichoderma reesei
1.14.18.1 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

EC Number Organism UniProt Comment Textmining
1.10.3.1 Trichoderma reesei
-
gene tyr2
-
1.14.18.1 Trichoderma reesei
-
gene tyr2
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.10.3.1 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
1.10.3.1 proteolytic modification the mature protein is processed from the C-terminus by a cleavage of a peptide fragment of about 20 kDa Trichoderma reesei
1.14.18.1 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
1.14.18.1 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)

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.10.3.1 18.18
-
purified recombinant enzyme Trichoderma reesei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.10.3.1 (+)-catechin hydrate + O2
-
Trichoderma reesei ?
-
?
1.10.3.1 (-)-epicatechin + O2
-
Trichoderma reesei ?
-
?
1.10.3.1 L-dopa + 1/2 O2 low activity with the D-isomer, 18% of the activity with the L-isomer Trichoderma reesei L-dopaquinone + H2O
-
?
1.10.3.1 additional information broad substrate specificity, overview, 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 ?
-
?
1.10.3.1 pyrocatechol + O2
-
Trichoderma reesei ?
-
?
1.10.3.1 pyrogallol + O2
-
Trichoderma reesei ?
-
?
1.14.18.1 4-coumaric acid + O2
-
Trichoderma reesei ?
-
?
1.14.18.1 4-tyrosol + O2
-
Trichoderma reesei ?
-
?
1.14.18.1 glycyl-glycyl-L-tyrosine + O2 3.4fold higher activity compared to Tyr Trichoderma reesei ?
-
?
1.14.18.1 glycyl-L-tyrosine + O2 2.9fold higher activity compared to Tyr Trichoderma reesei ?
-
?
1.14.18.1 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
-
?
1.14.18.1 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 ?
-
?
1.14.18.1 phenol + O2 low activity Trichoderma reesei ?
-
?

Subunits

EC Number Subunits Comment Organism
1.10.3.1 ? x * 43200, recombinant enzyme, SDS-PAGE, x * 61151, unprocessed enzyme, sequence calculation, 43 124-43 204, recombinant enzyme, mass spectrometry Trichoderma reesei
1.10.3.1 More N-terminal and C-terminal structural analyses by fragmentation, chromatography, MS and peptide sequencing of the purified recombinant enzyme, overview Trichoderma reesei
1.14.18.1 ? x * 43200, recombinant enzyme, SDS-PAGE, x * 61 151, unprocessed enzyme, sequence calculation, 43 124-43 204, recombinant enzyme, mass spectrometry Trichoderma reesei
1.14.18.1 More N-terminal and C-terminal structural analyses by fragmentation, chromatography, MS and peptide sequencing of the purified recombinant enzyme, overview Trichoderma reesei

Synonyms

EC Number Synonyms Comment Organism
1.10.3.1 catecholase
-
Trichoderma reesei
1.10.3.1 diphenolase
-
Trichoderma reesei
1.14.18.1 cresolase
-
Trichoderma reesei
1.14.18.1 monophenol, o-diphenol:oxygen oxidoreductase
-
Trichoderma reesei
1.14.18.1 monophenolase
-
Trichoderma reesei
1.14.18.1 tyrosinase
-
Trichoderma reesei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.10.3.1 30
-
recombinant enzyme Trichoderma reesei
1.14.18.1 30
-
recombinant enzyme Trichoderma reesei

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.10.3.1 30
-
purified recombinant enzyme, half-life: 18 h Trichoderma reesei
1.10.3.1 40
-
purified recombinant enzyme, half-life: 3,75 h Trichoderma reesei
1.10.3.1 50
-
purified recombinant enzyme, half-life: 15 min Trichoderma reesei
1.14.18.1 30
-
purified recombinant enzyme, half-life: 18 h Trichoderma reesei
1.14.18.1 40
-
purified recombinant enzyme, half-life: 3,75 h Trichoderma reesei
1.14.18.1 50
-
purified recombinant enzyme, half-life: 15 min Trichoderma reesei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.10.3.1 9
-
recombinant enzyme Trichoderma reesei
1.14.18.1 9
-
recombinant enzyme Trichoderma reesei

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.10.3.1 6 9.5 highest activity and stability within a neutral and alkaline pH range Trichoderma reesei
1.14.18.1 6 9.5 highest activity and stability within a neutral and alkaline pH range Trichoderma reesei

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.10.3.1 additional information
-
highest activity and stability within a neutral and alkaline pH range Trichoderma reesei
1.10.3.1 4
-
1 h, purified recombinant enzyme, complete loss of activity Trichoderma reesei
1.10.3.1 5
-
1 h, purified recombinant enzyme, loss of 50% activity Trichoderma reesei
1.10.3.1 7
-
stable at Trichoderma reesei
1.14.18.1 additional information
-
highest activity and stability within a neutral and alkaline pH range Trichoderma reesei
1.14.18.1 4
-
1 h, purified recombinant enzyme, complete loss of activity Trichoderma reesei
1.14.18.1 5
-
1 h, purified recombinant enzyme, loss of 50% activity Trichoderma reesei
1.14.18.1 7
-
stable at Trichoderma reesei

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.10.3.1 Trichoderma reesei isoelectric focusing
-
9.5
1.14.18.1 Trichoderma reesei isoelectric focusing
-
9.5