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Literature summary extracted from

  • Rannes, J.B.; Ioannou, A.; Willies, S.C.; Grogan, G.; Behrens, C.; Flitsch, S.L.; Turner, N.J.
    Glycoprotein labeling using engineered variants of galactose oxidase obtained by directed evolution (2011), J. Am. Chem. Soc., 133, 8436-8439.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.3.9 molecular biology glycoprotein labeling using engineered variants of galactose oxidase, overview Fusarium sp.

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.9 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.
1.1.3.9 P463I random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme Fusarium sp.
1.1.3.9 P463V random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme Fusarium sp.
1.1.3.9 R330K the mutant shows increased activity with D-fructose compared to the wild-type enzyme Fusarium sp.
1.1.3.9 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.
1.1.3.9 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.
1.1.3.9 W290F/R330K/Q406T random mutagenesis, the mutant shows improved activity toward Glc compared to the wild-type enzyme Fusarium sp.
1.1.3.9 Y405F/Q406E random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme Fusarium sp.
1.1.3.9 Y405F/Q406Y random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme Fusarium sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.3.9 Cu2+ required, copper enzyme Fusarium sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.9 D-galactose + O2 Fusarium sp.
-
 D-galacto-hexodialdose + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.9 Fusarium sp.
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.9 D-galactose + O2
-
 Fusarium sp. D-galacto-hexodialdose + H2O2
-
 ?
1.1.3.9 methyl alpha-D-galactopyranoside + O2
-
 Fusarium sp. methyl alpha-D-galacto-hexodialdose + H2O2
-
 ?
1.1.3.9 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. ?
-
 ?
1.1.3.9 talose + O2
-
 Fusarium sp. ? + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.3.9 GOase
-
 Fusarium sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.3.9 30
-
 assay at Fusarium sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.9 7
-
 assay at Fusarium sp.