Application | Comment | Organism |
---|---|---|
molecular biology | glycoprotein labeling using engineered variants of galactose oxidase, overview | Fusarium sp. |
Protein Variants | Comment | Organism |
---|---|---|
additional information | glycoprotein labeling using engineered variants of galactose oxidase obtained by directed evolution, overview. The methodology can also be applied to the labeling of cells. Pichia pastoris cells, which express mannosylated glycoproteins on their surface | Fusarium sp. |
P463I | random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme | Fusarium sp. |
P463V | random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme | Fusarium sp. |
R330K | the mutant shows increased activity with D-fructose compared to the wild-type enzyme | Fusarium sp. |
R330K/W290F/Q406E/Y405F | the mutant shows 136fold increased activity with D-fructose, and increased activity with mannose and N-acetylglucosamine compared to the wild-type enzyme | Fusarium sp. |
S10P/M70 V/P136/G195E/V494A/N535D | random mutagenesis, the enzyme mutant shows improved levels of recombinant expression of a more active and stable enzyme in Escherichia coli without any change in substrate range compared to the wild-type enzyme | Fusarium sp. |
W290F/R330K/Q406T | random mutagenesis, the mutant shows improved activity toward Glc compared to the wild-type enzyme | Fusarium sp. |
Y405F/Q406E | random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme | Fusarium sp. |
Y405F/Q406Y | random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme | Fusarium sp. |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | required, copper enzyme | Fusarium sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-galactose + O2 | Fusarium sp. | - |
D-galacto-hexodialdose + H2O2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Fusarium sp. | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-galactose + O2 | - |
Fusarium sp. | D-galacto-hexodialdose + H2O2 | - |
? | |
methyl alpha-D-galactopyranoside + O2 | - |
Fusarium sp. | methyl alpha-D-galacto-hexodialdose + H2O2 | - |
? | |
additional information | the enzyme is highly selective for galactose and talose but will not oxidize other sugars commonly found on glycoproteins. It oxidizes galactose residues as either monosaccharides or glycoconjugates that contain galactose at the nonreducing end, GC-MS analysis, overview | Fusarium sp. | ? | - |
? | |
talose + O2 | - |
Fusarium sp. | ? + H2O2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GOase | - |
Fusarium sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Fusarium sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Fusarium sp. |