1.1.5.14: fructose 5-dehydrogenase
This is an abbreviated version!
For detailed information about fructose 5-dehydrogenase, go to the full flat file.
Word Map on EC 1.1.5.14
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1.1.5.14
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electrode
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biosensors
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amperometric
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gluconobacter
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5-ketofructose
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oxydans
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biocathode
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bioelectrode
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bioanode
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tetrathiafulvalene
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5-keto-d-fructose
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biotechnology
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food industry
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analysis
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synthesis
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biofuel production
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industry
- 1.1.5.14
-
electrode
-
biosensors
-
amperometric
-
gluconobacter
- 5-ketofructose
-
oxydans
-
biocathode
-
bioelectrode
-
bioanode
-
tetrathiafulvalene
- 5-keto-d-fructose
- biotechnology
- food industry
- analysis
- synthesis
- biofuel production
- industry
Reaction
Synonyms
D-fructose dehydrogenase, dehydrogenase, fructose 5- (acceptor), FDH, FdhL, FdhS, fdhSCL, fructose 5-dehydrogenase, fructose dehydrogenase
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Engineering
Engineering on EC 1.1.5.14 - fructose 5-dehydrogenase
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M450Q
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the mutant shows a drastic decrease of the overpotential in the oxidation of D-fructose due to a negative shift in the formal potential of heme 2c as the electron-donating site of the variant
M450Q/DELTA1cFDH
M450Q
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the mutant shows a drastic decrease of the overpotential in the oxidation of D-fructose due to a negative shift in the formal potential of heme 2c as the electron-donating site of the variant
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additional information
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the direct electron transfer-type bioelectrocatalytic activity of the mutant is higher than that of recombinant native enzyme
M450Q/DELTA1cFDH
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the direct electron transfer-type bioelectrocatalytic activity of the mutant is higher than that of recombinant native enzyme
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an enzyme variant (DELTA1c2cFDH) which lacks 199 amino acid residues including two heme c moieties from N-terminus transports the electrons to the electrode via heme 3c at a more negative potential and at more improved kinetics than the recombinant (native) enzyme
additional information
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in mutant M450QDELTA1cFDH, 143 amino acid residues involving heme 1c are removed and M450 as the sixth axial ligand of heme 2c is replaced with glutamine to negatively shift the formal potential of heme 2c
additional information
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in mutant M450QDELTA1cFDH, 143 amino acid residues involving heme 1c are removed and M450 as the sixth axial ligand of heme 2c is replaced with glutamine to negatively shift the formal potential of heme 2c
-
additional information
-
an enzyme variant (DELTA1c2cFDH) which lacks 199 amino acid residues including two heme c moieties from N-terminus transports the electrons to the electrode via heme 3c at a more negative potential and at more improved kinetics than the recombinant (native) enzyme
-