3.2.1.38: beta-D-fucosidase
This is an abbreviated version!
For detailed information about beta-D-fucosidase, go to the full flat file.
Word Map on EC 3.2.1.38
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3.2.1.38
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beta-glucosidase
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glycosidases
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beta-d-galactosides
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3.2.1.21
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beta-d-glucoside
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beta-n-acetylglucosaminidase
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beta-d-xylosidase
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alpha-d-mannosidase
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beta-n-acetylgalactosaminidase
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d-fucose
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alpha-l-fucosidase
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beta-d-glucuronidase
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4-methylumbelliferyl
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achatina
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balteata
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alpha-l-arabinosidase
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alpha-d-glucosidase
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constellatus
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synthesis
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industry
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biofuel production
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analysis
- 3.2.1.38
- beta-glucosidase
- glycosidases
- beta-d-galactosides
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3.2.1.21
- beta-d-glucoside
- beta-n-acetylglucosaminidase
- beta-d-xylosidase
- alpha-d-mannosidase
- beta-n-acetylgalactosaminidase
- d-fucose
- alpha-l-fucosidase
- beta-d-glucuronidase
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4-methylumbelliferyl
- achatina
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balteata
- alpha-l-arabinosidase
- alpha-d-glucosidase
- constellatus
- synthesis
- industry
- biofuel production
- analysis
Reaction
Synonyms
1,4-beta-fucoside hydrolase, beta-D-fucosidase, beta-D-fucoside fucohydrolase, beta-D-galactosidase/beta-D-fucosidase, beta-D-gluco/fuco/galactosidase, beta-D-glucosidase/beta-D-fucosidase, beta-fucosidase, beta-fucosidase I, beta-fucosidase II, BglMKg, colanase, FucA, M8 mutant of glycoside hydrolase GK3214, MeBglD2, More, Pb280, PRGH1
ECTree
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Engineering
Engineering on EC 3.2.1.38 - beta-D-fucosidase
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E446N
beta-fucosidase activity is 26.49% compared to wild-type activity, beta-glucosidase activity is 21.37% compared to wild-type activity, beta-galactosidase activity is 15.7% compared to wild-type activity
N172A
beta-fucosidase activity is 18.38% compared to wild-type activity, beta-glucosidase activity is 17.65% compared to wild-type activity, beta-galactosidase activity is 13.4% compared to wild-type activity
D206N
catalytically active mutant enzyme, similar temperature optimum like wild-type enzyme. The high-catalytic turn-over rate by D206N for beta-glucosidase activity makes it a useful enzyme in cellulose degradation at high temperatures
D206Q
mutant enzyme shows less than 10% hydrolytic activity than the wild-type toward 4-nitrophenyl glycosides
Q77R
mutant enzyme shows less than 10% hydrolytic activity than the wild-type toward 4-nitrophenyl glycosides
additional information
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site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of beta-fucosidase from beta-galactosidase, random mutagenesis of beta-galactosidase active site residues D201, H540, and N604, and high-throughput screening, the mutants show increased kcat/KM in beta-fucosidase reaction, and decreased activity in beta-galactosidase reaction, overview
additional information
an overproducing mutant is isolated by UV mutagenesis and screening on agar plates containing X-Gal substrate. Cytoplasmic extracts of the mutant contain 25fold higher enzyme levels than the parent
additional information
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an overproducing mutant is isolated by UV mutagenesis and screening on agar plates containing X-Gal substrate. Cytoplasmic extracts of the mutant contain 25fold higher enzyme levels than the parent
additional information
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an overproducing mutant is isolated by UV mutagenesis and screening on agar plates containing X-Gal substrate. Cytoplasmic extracts of the mutant contain 25fold higher enzyme levels than the parent
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