1.2.1.89: D-glyceraldehyde dehydrogenase (NADP+)
This is an abbreviated version!
For detailed information about D-glyceraldehyde dehydrogenase (NADP+), go to the full flat file.
Word Map on EC 1.2.1.89
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1.2.1.89
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enolase
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thermoplasma
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acidophilum
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entner-doudoroff
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beta-sitosterol
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stigmasterol
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synthesis
- 1.2.1.89
- enolase
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thermoplasma
- acidophilum
-
entner-doudoroff
- beta-sitosterol
- stigmasterol
- synthesis
Reaction
Synonyms
AldA, ALDH, GADH, GLD, glyceraldehyde dehydrogenase, Pto0332, Ta0809, TaAlDH
ECTree
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Engineering
Engineering on EC 1.2.1.89 - D-glyceraldehyde dehydrogenase (NADP+)
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N286E
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
N286H
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
N286T
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde. Compared to L-lactaldehyde, N286T has a one-third lower Km value to glyceraldehyde.
34M/Y399C/S405N
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 55.7
F34L
the mutation enhances enzyme activity with the cofactor NAD+ by a factor of 3.2
F34M/D372N/S405N
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 7.2
F34M/D372N/Y399C/S405N
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 35.1
F34M/S405N
F34M/W271R/S405N
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 22.6
F34M/W271S/S405N
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 42.5
F34M/W271S/Y399C/S405N
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 1.1
F34M/Y399C/S405N
enhances enzyme activity with the cofactor NAD+ by a factor of eight and enhances solubilty
S405C
the mutation enhances enzyme activity with the cofactor NAD+ by a factor of 6
S405N
the mutation enhances enzyme activity with the cofactor NAD+ by a factor of 7.4
W271S
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 17.1
Y399C
F34M/S405N
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the mutant shows a slight increase in NAD+ acceptance and a 9fold improvement in catalytic efficiency with NAD+ compared with the wild type enzyme
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F34M/S405N
enhances enzyme activity with the cofactor NAD+ by a factor of eight
F34M/S405N
the mutations enhance enzyme activity with the cofactor NAD+ by a factor of 8.5 while impacts on enzyme stability and substrate specificity are negligible
F34M/S405N
the mutant shows a slight increase in NAD+ acceptance and a 9fold improvement in catalytic efficiency with NAD+ compared with the wild type enzyme
enhances the protein solubility after recombinant expression in Escherichia coli 6fold
Y399C
the mutation enhances the protein solubility after recombinant expression in Escherichia coli 6fold and enhances enzyme activity with the cofactor NAD+ by a factor of 6.4