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