1.2.1.22: lactaldehyde dehydrogenase
This is an abbreviated version!
For detailed information about lactaldehyde dehydrogenase, go to the full flat file.
Word Map on EC 1.2.1.22
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1.2.1.22
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aldolase
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l-lactate
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l-rhamnose
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glycol
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l-fucose
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dehydrogenases
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1-phosphate
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methylglyoxal
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glycolaldehyde
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nad+-dependent
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l-1,2-propanediol
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propanediol
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non-phosphorylated
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permease
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dissimilate
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dihydroxyacetone
- 1.2.1.22
- aldolase
- l-lactate
- l-rhamnose
- glycol
- l-fucose
- dehydrogenases
- 1-phosphate
- methylglyoxal
- glycolaldehyde
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nad+-dependent
- l-1,2-propanediol
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propanediol
-
non-phosphorylated
-
permease
-
dissimilate
- dihydroxyacetone
Reaction
Synonyms
ALD, AldA, aldehyde dehyrogenase, ALDH, AN0544, AvLADH, dehydrogenase, lactaldehyde, L-lactaldehyde dehydrogenase, L-lactaldehyde:NAD oxidoreductase, Lactaldehyde dehydrogenase, LADH, MJ1411, More, NAD-dependent lactaldehyde dehydrogenase, nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase, PsLADH, SSO3117
ECTree
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Engineering
Engineering on EC 1.2.1.22 - lactaldehyde dehydrogenase
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F180T
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renders an enzyme with the ability to use NADP+. NADP+ activity is higher than that attained with NAD+. Exhibits a 16fold increase in the Vm/Km ratio with NAD+ as the coenzyme. Absence of Mg2+ inhibitory effect on F180T activity
N286E
N286H
N286T
additional information
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
N286E
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme and is able to oxidate glyceraldehyde and methylglyoxal
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
N286H
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme and is able to oxidate glyceraldehyde and methylglyoxal, as well as acetaldehyde
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.
N286T
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme and is able to oxidate glyceraldehyde and methylglyoxal, as well as acetaldehyde
calculated Gibbs free energy of protein-substrate interaction of enzyme mutants with D-glyceraldehyde as substrate
additional information
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calculated Gibbs free energy of protein-substrate interaction of enzyme mutants with D-glyceraldehyde as substrate