1.2.1.4: aldehyde dehydrogenase (NADP+)
This is an abbreviated version!
For detailed information about aldehyde dehydrogenase (NADP+), go to the full flat file.
Word Map on EC 1.2.1.4
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1.2.1.4
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voltage-gated
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kvbeta1
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voltage-dependent
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pore-forming
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juxtaparanodal
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paranodal
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caspr
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medicine
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retinaldehyde
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synthesis
- 1.2.1.4
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voltage-gated
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kvbeta1
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voltage-dependent
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pore-forming
-
juxtaparanodal
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paranodal
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caspr
- medicine
- retinaldehyde
- synthesis
Reaction
Synonyms
AKR1A4, ALD6, aldehyde dehydrogenase (NADP+), aldehyde dehydrogenase 3A1, aldehyde dehydrogenase 6, aldehyde reductase, ALDH, ALDH1, ALDH1F1, ALDH3A1, ALDH6, AlDHPyr1147, dehydrogenase, aldehyde (nicotinamide adenine dinucleotide phosphate), Kvbeta2, NADP dependent aldehyde dehydrogenase, NADP+-dependent Ald6, NADP-acetaldehyde dehydrogenase, NADP-dependent aldehyde dehydrogenase, Seegmiller enzyme, Ta0439, TaAlDH
ECTree
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Application
Application on EC 1.2.1.4 - aldehyde dehydrogenase (NADP+)
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medicine
synthesis
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ALDH3A1 contributes to the detoxification of various aldehydes produced in response to oxidative stress
medicine
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ALDH3A1 contributes to the detoxification of various aldehydes produced in response to oxidative stress
medicine
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ALDH3A1 contributes to the detoxification of various aldehydes produced in response to oxidative stress
medicine
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ALDH3A1 contributes to the detoxification of various aldehydes produced in response to oxidative stress
the aldehyde dehydrogenase from Thermoplasma acidophilum implemented as a key enzyme in a synthetic cellfree reaction cascade for the production of alcohols. Thermoplasma acidophilum enzyme TaALDH matches the cascade equirements regarding temperature stability, efficient heterologous expression in Escherichia coli, and exclusive activity for D-glyceraldehyde (not active on acetaldehyde). The remaining drawback is its cofactor preference toward NADP+ resulting in high KM for NAD+ and a rather low overall activity under cascade conditions
synthesis
-
the aldehyde dehydrogenase from Thermoplasma acidophilum implemented as a key enzyme in a synthetic cellfree reaction cascade for the production of alcohols. Thermoplasma acidophilum enzyme TaALDH matches the cascade equirements regarding temperature stability, efficient heterologous expression in Escherichia coli, and exclusive activity for D-glyceraldehyde (not active on acetaldehyde). The remaining drawback is its cofactor preference toward NADP+ resulting in high KM for NAD+ and a rather low overall activity under cascade conditions
-
synthesis
-
the aldehyde dehydrogenase from Thermoplasma acidophilum implemented as a key enzyme in a synthetic cellfree reaction cascade for the production of alcohols. Thermoplasma acidophilum enzyme TaALDH matches the cascade equirements regarding temperature stability, efficient heterologous expression in Escherichia coli, and exclusive activity for D-glyceraldehyde (not active on acetaldehyde). The remaining drawback is its cofactor preference toward NADP+ resulting in high KM for NAD+ and a rather low overall activity under cascade conditions
-
synthesis
-
the aldehyde dehydrogenase from Thermoplasma acidophilum implemented as a key enzyme in a synthetic cellfree reaction cascade for the production of alcohols. Thermoplasma acidophilum enzyme TaALDH matches the cascade equirements regarding temperature stability, efficient heterologous expression in Escherichia coli, and exclusive activity for D-glyceraldehyde (not active on acetaldehyde). The remaining drawback is its cofactor preference toward NADP+ resulting in high KM for NAD+ and a rather low overall activity under cascade conditions
-
synthesis
-
the aldehyde dehydrogenase from Thermoplasma acidophilum implemented as a key enzyme in a synthetic cellfree reaction cascade for the production of alcohols. Thermoplasma acidophilum enzyme TaALDH matches the cascade equirements regarding temperature stability, efficient heterologous expression in Escherichia coli, and exclusive activity for D-glyceraldehyde (not active on acetaldehyde). The remaining drawback is its cofactor preference toward NADP+ resulting in high KM for NAD+ and a rather low overall activity under cascade conditions
-