KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics. The Michaelis-Menten (MM) analogous model suitable for oxidation degradation reaction of lignin containing two parameters, including the apparent maximum rate (ma,max) and apparent Michael constant (ka,m), is deduced. The oxidation degradation of lignin in lignocellullosic biomass in a dilute solution system follows the MM analogous model | Aspergillus oryzae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Aspergillus oryzae | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 veratryl alcohol + H2O2 | Aspergillus oryzae | - |
2 veratryl aldehyde + 2 H2O | - |
? | |
2 veratryl alcohol + H2O2 | Aspergillus oryzae CGMCC5992 | - |
2 veratryl aldehyde + 2 H2O | - |
? | |
additional information | Aspergillus oryzae | oxidation degradation reaction of lignin in the corn stover (CS) is catalyzed by LiP from Aspergillus oryzae, optimization of a biodegradation process, overview | ? | - |
- |
|
additional information | Aspergillus oryzae CGMCC5992 | oxidation degradation reaction of lignin in the corn stover (CS) is catalyzed by LiP from Aspergillus oryzae, optimization of a biodegradation process, overview | ? | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus oryzae | - |
- |
- |
Aspergillus oryzae CGMCC5992 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 veratryl alcohol + H2O2 | - |
Aspergillus oryzae | 2 veratryl aldehyde + 2 H2O | - |
? | |
2 veratryl alcohol + H2O2 | - |
Aspergillus oryzae CGMCC5992 | 2 veratryl aldehyde + 2 H2O | - |
? | |
additional information | oxidation degradation reaction of lignin in the corn stover (CS) is catalyzed by LiP from Aspergillus oryzae, optimization of a biodegradation process, overview | Aspergillus oryzae | ? | - |
- |
|
additional information | LiP uses H2O2 to catalyze one-electron oxidation of chemicals to free radicals. Hydrogen peroxide oxidizes the heme-LiP by two electrons to LiP I, a ferryl (Fe(IV)) n-porphyrin cation radical of LiP. A substrate molecule can then be oxidized by one electron to a radical, and LiP I is reduced by one electron to LiP II. A subsequent oxidation of another substrate molecule by LiP II returns the LiP to its ferric resting state. The presence of excess H2O2 or slow reduction of LiP II to resting state may lead to the oxidation of LiP II to LiP III, an inactivated enzyme form. This is called LiP cycle. Optimization of enzyme activity measurement and assay condition, overview. The optimum combination of parameters for the maximum is as follows, including pretreatment temperature of 120°C, pretreatment time of 5 min, reaction temperature of 30°C, enzyme amount of 3.75 U/100 ml, 50 mM sodium lactate-hydrochloric acid buffer of pH 1.5, H2O2 concentration of 20 mM and H2O2 amount of 1 ml | Aspergillus oryzae | ? | - |
- |
|
additional information | oxidation degradation reaction of lignin in the corn stover (CS) is catalyzed by LiP from Aspergillus oryzae, optimization of a biodegradation process, overview | Aspergillus oryzae CGMCC5992 | ? | - |
- |
|
additional information | LiP uses H2O2 to catalyze one-electron oxidation of chemicals to free radicals. Hydrogen peroxide oxidizes the heme-LiP by two electrons to LiP I, a ferryl (Fe(IV)) n-porphyrin cation radical of LiP. A substrate molecule can then be oxidized by one electron to a radical, and LiP I is reduced by one electron to LiP II. A subsequent oxidation of another substrate molecule by LiP II returns the LiP to its ferric resting state. The presence of excess H2O2 or slow reduction of LiP II to resting state may lead to the oxidation of LiP II to LiP III, an inactivated enzyme form. This is called LiP cycle. Optimization of enzyme activity measurement and assay condition, overview. The optimum combination of parameters for the maximum is as follows, including pretreatment temperature of 120°C, pretreatment time of 5 min, reaction temperature of 30°C, enzyme amount of 3.75 U/100 ml, 50 mM sodium lactate-hydrochloric acid buffer of pH 1.5, H2O2 concentration of 20 mM and H2O2 amount of 1 ml | Aspergillus oryzae CGMCC5992 | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
LIP | - |
Aspergillus oryzae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Aspergillus oryzae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
2.5 | - |
assay at | Aspergillus oryzae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Aspergillus oryzae |