1.2.1.26: 2,5-dioxovalerate dehydrogenase
This is an abbreviated version!
For detailed information about 2,5-dioxovalerate dehydrogenase, go to the full flat file.
Word Map on EC 1.2.1.26
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1.2.1.26
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dehydratase
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azospirillum
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aldhs
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3-hydroxypropionic
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brasilense
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l-arabinose
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aldolase
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d-glucarate
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watanabe
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crescentus
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tricarboxylic
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makino
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d-xylose
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degradation
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isozymes
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caulobacter
- 1.2.1.26
- dehydratase
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azospirillum
-
aldhs
-
3-hydroxypropionic
- brasilense
- l-arabinose
- aldolase
- d-glucarate
-
watanabe
- crescentus
-
tricarboxylic
-
makino
- d-xylose
- degradation
- isozymes
-
caulobacter
Reaction
Synonyms
2-oxoglutarate semialdehyde dehydrogenase, AbKGSADH, aldehyde dehydrogenase, ALDH, alpha-ketoglutarate semialdehyde dehydrogenase, alpha-ketoglutarate-semialdehyde dehydrogenase, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-KGSA dehydrogenase, alphaKGSA dehydrogenase, alphaKGSADH, araE, DopDH, KGSADH, KGSADH-I, KGSADH-II, KGSADH-III, More, SSO3117, ycbD protein
ECTree
1.2.1.26 2,5-dioxovalerate dehydrogenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.2.1.26 - 2,5-dioxovalerate dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A110S/K273A/A442P/P444T
random mutagenesis, the mutant shows reduced activity with 3-hydroxypropionaldehyde and altered cofactor kinetics compared to the wild-type enzyme, no activity with NADP+
A110S/K273A/R334Q/A337R/A442P/P444T
random mutagenesis, the mutant shows increased activity with 3-hydroxypropionaldehyde and altered cofactor kinetics compared to the wild-type enzyme
A442P/P444T
random mutagenesis, the mutant shows reduced activity with 3-hydroxypropionaldehyde and altered cofactor kinetics compared to the wild-type enzyme, no activity with NADP+
C287A
site-directed mutagenesis, the mutant is almost inactive
E253A
site-directed mutagenesis, the mutant is almost inactive
F156A
site-directed mutagenesis, the mutant is almost inactive
F450A
site-directed mutagenesis, the mutant is almost inactive
I288A
site-directed mutagenesis, the mutant is almost inactive
K273A/A442P/T443E/P444A
random mutagenesis, the mutant shows increased activity with 3-hydroxypropionaldehyde and altered cofactor kinetics compared to the wild-type enzyme, no activity with NADP+
K273A/R334Q/A337R/A442P/T443E/P444A
random mutagenesis, the mutant shows strongly increased activity with 3-hydroxypropionaldehyde and altered cofactor kinetics compared to the wild-type enzyme
N159A
site-directed mutagenesis, the mutant shows 50% increased activity compared to wild-type enzyme
Q160A
site-directed mutagenesis, the mutant shows 30% increased activity compared to wild-type enzyme
R163A
site-directed mutagenesis, the mutant shows 10% reduced activity compared to wild-type enzyme
R334Q/A337R
random mutagenesis, the mutant shows increased activity with 3-hydroxypropionaldehyde and altered cofactor kinetics compared to the wild-type enzyme
R334Q/A337R/A442P/P444T
random mutagenesis, the mutant shows increased activity with 3-hydroxypropionaldehyde and altered cofactor kinetics compared to the wild-type enzyme
V286A
site-directed mutagenesis, the mutant shows 50% reduced activity compared to wild-type enzyme
additional information
additional information
alpha-KGSA dehydrogenase activity in cell extracts from the mutant DELTAACIAD0131 grown on succinate as the sole carbon source is undetectable
additional information
engineering of alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH) from Azospirillum brasilense for prodduction of 3-hydroxypropanoate (HP) from 3-hydroxypropionaldehyde (3-HPA). A directed evolutionary strategy is adopted as the engineering approach for modifying the substrate-binding sites of KGSADH. The residues in the binding sites for the substrates, 3-HPA and NAD+, are randomized, and the resulting libraries are screened for higher activity. Isolated KGSADH variants have significantly lower Km values for both the substrates. The enzymes also show higher substrate specificities for aldehyde and NAD+, less inhibition by NADH, and greater resistance to inactivation by 3-HPA than the wild-type enzyme. A recombinant Pseudomonas denitrificans strain expressing one of the engineered KGSADH variants exhibits less accumulation of 3-HPA, decreased levels of inactivation of the enzymes, and higher cell growth than that expressing the wild-type KGSADH. The flask culture of the Pseudomonas denitrificans strain with the mutant KGSADH results in about 40% increase of 3-HP titer (53 mM) compared with that using the wild-type enzyme (37 mM). Mutant structure modeling, overview
