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Literature summary for 1.14.18.1 extracted from
- Expression of the Trichoderma reesei tyrosinase 2 in Pichia pastoris: isotopic labeling and physicochemical characterization (2007), Protein Expr. Purif., 55, 147-158.
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | the produced enzyme has similar properties as the one produced in the native Trichoderma reesei host and expression in the Pichia pastoris provides good opportunities for future protein engineering, screening and functional studies of this important class of enzymes | Trichoderma reesei |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Pichia pastoris | Trichoderma reesei |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| copper | correct copper concentration in the growth medium is critical for the expression of this copper containing enzyme. Optimization of the copper concentration and the expression conditions lead to a 10fold increase in the expression level of processed active histidine tagged TYR2 | Trichoderma reesei |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 45000 | - |
a protein of approximately 45 kDa could be detected in samples from most of the transformants. The full length of the TYR2 has a predicted molecular weight of 60.4 kDa, so the enzyme detected by Western blot analysis has a significantly lower mass | Trichoderma reesei |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Trichoderma reesei | A0ZXZ4 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | TYR2 expressed in Pichia pastoris is post-translationally modified. The C-terminal domain of 153 amino acids of the protein is proteolytically cleaved off from the catalytic domain and the only potential N-glycosylation site is glycosylated | Trichoderma reesei |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni2+ Sepharose FF column and further purified by gel filtration on a Sephacryl-S 100 HR gel filtration column | Trichoderma reesei |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-dopa + 1/2 O2 | - |
Trichoderma reesei | L-dopaquinone + H2O | - |
? | |
| L-tyrosine + O2 + AH2 | - |
Trichoderma reesei | L-dopa + H2O + A | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| monophenol, o-diphenol: oxygen oxidoreductase | - |
Trichoderma reesei |
| TYR2 | - |
Trichoderma reesei |
| tyrosinase 2 | - |
Trichoderma reesei |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
PpTYR2 has an optimum at pH 6, whereas TrTYR2 has a broader pH optimum | Trichoderma reesei |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 8 | determination of the pH optimum of TYR2 is carried out with 2 mM L-tyrosine as the substrate, at a pH range of 5-8, and measuring the enzyme activity spectrophotometrically | Trichoderma reesei |
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