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Literature summary for 1.10.3.1 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

Inhibitors

Inhibitors Comment Organism Structure
benzaldehyde
-
Trichoderma reesei
EDTA
-
Trichoderma reesei
additional information no inhibition by kojic acid and 2-mercaptoethanol Trichoderma reesei
NaCl
-
Trichoderma reesei
SDS
-
Trichoderma reesei
Sodium azide
-
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 * 61151, unprocessed enzyme, sequence calculation, 43 124-43 204, recombinant enzyme, mass spectrometry Trichoderma reesei
61151
-
x * 43200, recombinant enzyme, SDS-PAGE, x * 61151, 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 cation exchange chromatography and gel filtration to homogeneity Trichoderma reesei

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(+)-catechin hydrate + O2
-
Trichoderma reesei ?
-
?
(-)-epicatechin + O2
-
Trichoderma reesei ?
-
?
L-dopa + 1/2 O2 low activity with the D-isomer, 18% of the activity with the L-isomer Trichoderma reesei L-dopaquinone + H2O
-
?
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 ?
-
?
pyrocatechol + O2
-
Trichoderma reesei ?
-
?
pyrogallol + O2
-
Trichoderma reesei ?
-
?

Subunits

Subunits Comment Organism
? x * 43200, recombinant enzyme, SDS-PAGE, x * 61151, 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
catecholase
-
Trichoderma reesei
diphenolase
-
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