1.1.3.9: galactose oxidase
This is an abbreviated version!
For detailed information about galactose oxidase, go to the full flat file.
Word Map on EC 1.1.3.9
-
1.1.3.9
-
neuraminidase
-
copper
-
borohydride
-
lymphocyte
-
lectin
-
sialic
-
tritiated
-
mitogen
-
concanavalin
-
glycolipids
-
galactosyl
-
glycoconjugates
-
agglutinin
-
nab3h4
-
ganglioside
-
dendroides
-
phenoxyl
-
hydrazide
-
sialylation
-
borotritide
-
graminearum
-
one-electron
-
sialoglycoproteins
-
sialidase
-
galactosamine
-
copper-containing
-
n-acetylgalactosaminyl
-
desialylated
-
naio4
-
synthesis
-
lactoperoxidase
-
galactose-containing
-
degradation
-
diagnostics
-
molecular biology
-
energy production
-
analysis
-
biotechnology
- 1.1.3.9
- neuraminidase
- copper
- borohydride
- lymphocyte
- lectin
-
sialic
-
tritiated
-
mitogen
-
concanavalin
- glycolipids
-
galactosyl
- glycoconjugates
- agglutinin
-
nab3h4
- ganglioside
- dendroides
-
phenoxyl
- hydrazide
-
sialylation
-
borotritide
- graminearum
-
one-electron
-
sialoglycoproteins
- sialidase
- galactosamine
-
copper-containing
-
n-acetylgalactosaminyl
-
desialylated
- naio4
- synthesis
- lactoperoxidase
-
galactose-containing
- degradation
- diagnostics
- molecular biology
- energy production
- analysis
- biotechnology
Reaction
Synonyms
AOd, At1g14430, At1g19900, At1g67290, At1g75620, At3g53950, At3g57620, At5g19580, beta-galactose oxidase, D-galactose oxidase, F5K20_250, FgrGalOx, galactose 6-oxidase, galactose oxidase, GalOx, GAO, GAOA, GAOX, GLOX1, Glox2, Glox3, GLOX4, GLOX5, GLOX6, GO, GOase, RUBY, RUBY PARTICLES IN MUCILAGE
ECTree
Advanced search results
Engineering
Engineering on EC 1.1.3.9 - galactose oxidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
C383A
-
site-directed mutagenesis, the mutant shows 39% of wild-typ enzyme activity
C383D
-
site-directed mutagenesis, the mutant shows 26% of wild-typ enzyme activity
C383E
-
site-directed mutagenesis, the mutant shows 130% of wild-typ enzyme activity
C383F
-
site-directed mutagenesis, the mutant shows 8% of wild-typ enzyme activity
C383G
-
site-directed mutagenesis, the mutant shows 70% of wild-typ enzyme activity
C383H
-
site-directed mutagenesis, the mutant shows 35% of wild-typ enzyme activity
C383I
-
site-directed mutagenesis, the mutant shows 3% of wild-typ enzyme activity
C383K
-
site-directed mutagenesis, the mutant shows 115% of wild-typ enzyme activity
C383L
-
site-directed mutagenesis, the mutant shows 41% of wild-typ enzyme activity
C383M
-
site-directed mutagenesis, the mutant shows 75% of wild-typ enzyme activity
C383N
-
site-directed mutagenesis, the mutant shows 6% of wild-typ enzyme activity
C383P
-
site-directed mutagenesis, the mutant shows 18% of wild-typ enzyme activity
C383Q
-
site-directed mutagenesis, the mutant shows 13% of wild-typ enzyme activity
C383R
-
site-directed mutagenesis, the mutant shows 0.2% of wild-typ enzyme activity
C383S
-
site-directed mutagenesis, the mutant shows 160% of wild-typ enzyme activity
C383T
-
site-directed mutagenesis, the mutant shows 32% of wild-typ enzyme activity
C383V
-
site-directed mutagenesis, the mutant shows 4% of wild-typ enzyme activity
C383W
-
site-directed mutagenesis, the mutant shows 0.001% of wild-typ enzyme activity
G195E
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
M70V
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
N535D
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
V494A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
W290F
W290G
W290H
kcat/KM for D-galactose is 1180fold lower than wild-type value
C383S/Y436A
-
decrease in Km-value, decrease in kcat-value of 1-methyl-alpha-D-galactose, increase in kcat-value of D-galactose
P463I
-
random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme
P463V
-
random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme
R330K
-
the mutant shows increased activity with D-fructose compared to the wild-type enzyme
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
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
W290F/R330K/Q406T
-
random mutagenesis, the mutant shows improved activity toward Glc compared to the wild-type enzyme
Y405F/Q406E
-
random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme
Y405F/Q406Y
-
random mutagenesis, the mutant shows altered substrate specificity with several substrates compared to the wild-type enzyme
Y436H/V494A
-
slight decrease in kcat-value of 1-methyl-alpha-D-galactose, slight increase in kcat-value of D-galactose
C228G
additional information
kcat/KM for D-galactose is 49fold lower than wild-type value, kcat/Km for 2-methylene-1,3-propanediol is 1.2fold higher than wild-type value
W290F
structure PDB ID 2EIC, comparison to the wild-type enzyme. The activity of Trp290 mutants of FgrGalOx show a dramatic loss of oxidative capacity compared to wild-type, which is correlated to significantly higher Km values for the natural substrate galactose with the FgrGalOx W290G/F mutants, presumably because of the loss of a hydrogen-bonding interaction between W290 and a remote hydroxyl group of the substrate. Trp290 in FgrGalOx is implicated in stabilizing the radical form of the Cys-Tyr cofactor, although substitution with either Phe or Gly also stabilizes the tyrosine radical with retention of catalytic activity, while other substitutions were detrimental to the enzyme
kcat/KM for D-galactose is 6370fold lower than wild-type value
W290G
the activity of Trp290 mutants of FgrGalOx show a dramatic loss of oxidative capacity compared to wild-type, which is correlated to significantly higher Km values for the natural substrate galactose with the FgrGalOx W290G/F mutants, presumably because of the loss of a hydrogen-bonding interaction between W290 and a remote hydroxyl group of the substrate. Trp290 in FgrGalOx is implicated in stabilizing the radical form of the Cys-Tyr cofactor, although substitution with either Phe or Gly also stabilizes the tyrosine radical with retention of catalytic activity, while other substitutions were detrimental to the enzyme
C228G
-
the oxidized C228G mutant shows a higher reduction potential than the wild-type enzyme
-
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
-
introduction of silent mutations within codons 2-7 of the mature enzyme coding sequence to enhance enzyme translation and have combined these with other expression-enhancing mutations
additional information
a family 29 glucomannan binding module, CBM29-1-2, from Piromyces equi is separately linked to the N- and C-termini of GaO, effects on enzyme activity and binding of GaO towards various polysaccharides. The chimeric enzyme mutants demonstrate enhanced binding to galactomannan, galactoglucomannan and galactoxyloglucan compared to the wild-type enzyme. The position of the CBM29 fusion affects the enzyme function. Particularly, C-terminal fusion leads to greatest increases in galactomannan binding and catalytic efficiency, where relative to wild-type GaO, kcat/Km values increases by 7.5 and 19.8times on guar galactomannan and locust bean galactomannan, respectively. The fusion of CBM29 also induces oligomerization of GaOCBM29. Removing CBM32 from wild-type GaO leads to complete loss in enzyme activity, and substituting the native CBM32 for CBM29-1-2 does not regain GaO function
additional information
-
a family 29 glucomannan binding module, CBM29-1-2, from Piromyces equi is separately linked to the N- and C-termini of GaO, effects on enzyme activity and binding of GaO towards various polysaccharides. The chimeric enzyme mutants demonstrate enhanced binding to galactomannan, galactoglucomannan and galactoxyloglucan compared to the wild-type enzyme. The position of the CBM29 fusion affects the enzyme function. Particularly, C-terminal fusion leads to greatest increases in galactomannan binding and catalytic efficiency, where relative to wild-type GaO, kcat/Km values increases by 7.5 and 19.8times on guar galactomannan and locust bean galactomannan, respectively. The fusion of CBM29 also induces oligomerization of GaOCBM29. Removing CBM32 from wild-type GaO leads to complete loss in enzyme activity, and substituting the native CBM32 for CBM29-1-2 does not regain GaO function
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
genetic incorporation of 3,5-dichlorotyrosine (Cl2-Tyr) and 3,5-difluorotyrosine (F2-Tyr) to replace Tyr272 in the GAOV variant (i.e. A3.E7) optimized for expression through directed evolution. The proteins with an unnatural tyrosine residue are catalytically competent
additional information
-
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
-
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
-
identification of variants of GOase that possess good activity towards a range of secondary alcohols based upon the 1-phenylethanol template and high enantioselectivity in the kinetic resolution of (+/-)-3-fluoro-1-phenylethanol
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
additional information
-
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
-
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
additional information
-
engineering galactose oxidase for enhanced expression and altered specificity, properties of GAO mutant variants, overview
-
additional information
the enzyme is immobilized in a nanoscale chemical environment provided by mesoporous silicas (MPS). Two types of MPS, i.e. SBA-15 and MCF, are synthesized and used to accommodate GAOX. SBA-15-ROD are rod-shaped particles with periodically ordered nanopores (9.5 nm), while MCF has a mesocellular foam-like structure with randomly distributed pores (23 nm) interconnected by smaller windows (8.8 nm). GAOX is non-covalently bound to SBA-15-ROD, while it is covalently immobilized on MCF. Relatively high loadings in the range of 50-60 mg/g are achieved. The catalytic kinetics is reduced, mainly attributed to the diffusion limitation of substrate and product in the nanoscale channels. The apparent KM of the enzyme is largely unchanged upon immobilization, while the turnover number (kcat) is slightly reduced. The overall catalytic efficiency, represented by the ratio of kcat/KM, is retained around 70% and 60% for SBA-15 and MCF immobilization, respectively. The thermal resistance is enhanced up to 60°C, but with no further enhancement above 60°C. Three-dimensional structure analysis of immobilzed enzyme, overview