1.2.5.2: aldehyde dehydrogenase (quinone)
This is an abbreviated version!
For detailed information about aldehyde dehydrogenase (quinone), go to the full flat file.
Word Map on EC 1.2.5.2
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1.2.5.2
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dehydrogenases
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quinoprotein
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synthesis
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ferricyanide
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acetobacter
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acetaldehyde
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pqq-adh
- 1.2.5.2
- dehydrogenases
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quinoprotein
- synthesis
- ferricyanide
- acetobacter
- acetaldehyde
- pqq-adh
Reaction
Synonyms
ADH I, ADH IIB, ADH IIG, aldehyde dehydrogenase (acceptor), ALDH, BOH, dehydrogenase, aldehyde (acceptor), EC 1.2.99.3, FOE, formaldehyde-oxidizing enzyme, glucose sorbosone dehydrogenase, NAD+-independent, PQQ-containing alcohol dehydrogenase, PQQ-AldDH, PQQ-AlDH, pyrroloquinoline quinone-dependent aldehyde dehydrogenase, quinohemoprotein dehydrogenase, Swit_4395, tetrahydrofurfuryl alcohol dehydrogenase
ECTree
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Application
Application on EC 1.2.5.2 - aldehyde dehydrogenase (quinone)
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synthesis
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application in direct bioelectrocatalysis via site specific immobilization to form a monolayer of biocatalysts with a uniform orientation toward the gold electrode. Six-histidine tags at the N- or C-terminus of each of the three subunits are utilized as linking sites to performsite specific immobilization. The orientation of multi-subunit enzymes can affect direct electron transfer greatly by varying the electron tunneling distances. The favorable orientation allowing for a minimal heme c electron transfer distance shows a direct electron transfer rate 6.6fold higher than that with the orientation closest to the active site of the enzyme
synthesis
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bioelectrooxidation of ethanol using pyrroloquinoline quinone-dependent alcohol and aldehyde dehydrogenase enzymes for biofuel cell applications. A modified Nafion membrane provides the best electrical communication between enzymes and the electrode surface,with catalytic currents as high as 16.8 mA/cm2. Direct electron transfer using the pyrroloquinoline quinone-dependent alcohol and aldehyde dehydrogenase still lacks high current density, while the bioanodes that operate via mediated electron transfer employing ferrocene-modified linear polyethyleneimine redox polymers show efficient energy conversion capability in ethanol/air biofuelcells
synthesis
-
application in direct bioelectrocatalysis via site specific immobilization to form a monolayer of biocatalysts with a uniform orientation toward the gold electrode. Six-histidine tags at the N- or C-terminus of each of the three subunits are utilized as linking sites to performsite specific immobilization. The orientation of multi-subunit enzymes can affect direct electron transfer greatly by varying the electron tunneling distances. The favorable orientation allowing for a minimal heme c electron transfer distance shows a direct electron transfer rate 6.6fold higher than that with the orientation closest to the active site of the enzyme
-
synthesis
-
bioelectrooxidation of ethanol using pyrroloquinoline quinone-dependent alcohol and aldehyde dehydrogenase enzymes for biofuel cell applications. A modified Nafion membrane provides the best electrical communication between enzymes and the electrode surface,with catalytic currents as high as 16.8 mA/cm2. Direct electron transfer using the pyrroloquinoline quinone-dependent alcohol and aldehyde dehydrogenase still lacks high current density, while the bioanodes that operate via mediated electron transfer employing ferrocene-modified linear polyethyleneimine redox polymers show efficient energy conversion capability in ethanol/air biofuelcells
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