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Information on EC 1.2.1.26 - 2,5-dioxovalerate dehydrogenase and Organism(s) Azospirillum brasilense and UniProt Accession Q1JUP4
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EC Tree
1.2.1.26 2,5-dioxovalerate dehydrogenaseSpecify your search results
Word Map
- 1.2.1.26
- dehydratase
-
azospirillum
-
aldhs
-
3-hydroxypropionic
- brasilense
- l-arabinose
- aldolase
- d-glucarate
-
watanabe
- crescentus
-
tricarboxylic
-
makino
- d-xylose
- degradation
- isozymes
-
caulobacter
The taxonomic range for the selected organisms is: Azospirillum brasilense
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
kgsadh, kgsadh-ii, kgsadh-iii, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-ketoglutarate semialdehyde dehydrogenase, abkgsadh, kgsadh-i, ycbd protein, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-oxoglutarate semialdehyde dehydrogenase
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-
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alpha-ketoglutaric semialdehyde dehydrogenase
additional information
alpha-ketoglutaric semialdehyde dehydrogenase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
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oxidation
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-
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
2,5-dioxopentanoate:NADP+ 5-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
37250-92-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,5-dioxopentanoate + NAD+ + H2O
2-oxoglutarate + NADH + H+
-
-
-
r
2-oxoglutaric semialdehyde + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H + H+
-
-
-
?
2-oxoglutaric semialdehyde + NAD+ + H2O
2-oxoglutarate + NADH + H+
-
-
-
?
3-hydroxypropionaldehyde + NADP+
3-hydroxypropionate + NADPH + H+
very low activity
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-
?
alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
-
-
-
?
2,5-dioxopentanoate + NAD+ + H2O
2-oxoglutarate + NADH + H+
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-
-
r
alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
-
-
-
?
3-hydroxypropionaldehyde + NAD+
3-hydroxypropionate + NADH + H+
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-
-
?
3-hydroxypropionaldehyde + NAD+
3-hydroxypropionate + NADH + H+
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-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
activity of EC 1.2.1.24
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-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
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activity of EC 1.2.1.24
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-
?
additional information
?
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substrate and cofactor binding structures analysis, overview. The enzyme shows poor activity with NADP+ as a cofactor
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additional information
?
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substrate and cofactor binding structures analysis, overview. The enzyme shows poor activity with NADP+ as a cofactor
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutaric semialdehyde + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H + H+
-
-
-
?
2-oxoglutaric semialdehyde + NAD+ + H2O
2-oxoglutarate + NADH + H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
activity of EC 1.2.1.24
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
activity of EC 1.2.1.24
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
no significant preference between NAD+ and NADP+ in activity
NAD+
NAD+-enzyme binding mode and structure, overview. The NAD+-binding pocket is constituted by seven loops (beta7-alpha4, beta8-alpha5, beta10-alpha7, beta11-beta12, alpha8-beta13, alpha9-alpha10, and alpha11-beta16) and four alpha-helices (alpha4, alpha6, alpha7, and alpha10). The adenine ring is stabilized in the hydrophobic pocket that is formed by Phe151, Pro211, Ala212, Phe229, Val235 and Leu239, and a hydrogen bond with Ser215 also contributes to the binding of the ring. Residues Lys178, Glu181, and Pro211 constitute a suitable space for binding of the ribose ring, and stabilize the 2'-hydroxyl-group of the ring. The formation of the ribose ring binding site does not seem to be large enough to accommodate the phosphorylated ribose ring. Therefore the enzyme shows poor activity with NADP+ as a cofactor. The diphosphate moiety is stabilized by residues Asn331, Arg333, and Arg334 through directly and water-mediated hydrogen bond networks. Residues Arg334 and Glu384 stabilize the ribose moiety of NAD+, and the nicotinamide ring is stabilized by residues Gln160 and Glu253 by hydrogen bonding
NAD+
preferred cofactor, residues chosen for generating the NAD+ binding pocket library are shown using the crystal structure of KGSADH complexed with NAD+ (PDB ID 5X5U), overview
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.17
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A
0.29
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T
0.43
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T
0.55
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant R334Q/A337R
0.78
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant K273A/A442P/T443E/P444A
1.4
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A442P/P444T
1.6
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant wild-type enzyme
2.2
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A110S/K273A/A442P/P444T
0.025
NAD+
pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T
0.033
NAD+
pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T
0.037
NAD+
pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A
0.27
NAD+
pH 8.0, 25°C, recombinant mutant K273A/A442P/T443E/P444A
0.28
NAD+
pH 8.0, 25°C, recombinant mutant A110S/K273A/A442P/P444T
0.54
NADP+
pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T
0.66
NADP+
pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A
0.7
NADP+
pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T
0.0065
alpha-Ketoglutaric semialdehyde
with NAD+ as cofactor
0.0075
alpha-Ketoglutaric semialdehyde
with NADP+ as cofactor
0.011
alpha-Ketoglutaric semialdehyde
with NADP+ as cofactor
0.0246
alpha-Ketoglutaric semialdehyde
with NAD+ as cofactor
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T
6
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A
6.7
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T
6.8
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant R334Q/A337R
11
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant K273A/A442P/T443E/P444A
12
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A442P/P444T
15
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant wild-type enzyme
15
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A110S/K273A/A442P/P444T
4.8
NAD+
pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T
5.9
NAD+
pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T
6.1
NAD+
pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A
18
NAD+
pH 8.0, 25°C, recombinant mutant K273A/A442P/T443E/P444A
19
NAD+
pH 8.0, 25°C, recombinant mutant A110S/K273A/A442P/P444T
4
NADP+
pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T
4.5
NADP+
pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A
4.7
NADP+
pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T
15.4
alpha-Ketoglutaric semialdehyde
with NADP+ as cofactor
21.3
alpha-Ketoglutaric semialdehyde
with NAD+ as cofactor
23
alpha-Ketoglutaric semialdehyde
with NADP+ as cofactor
53.9
alpha-Ketoglutaric semialdehyde
with NAD+ as cofactor
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.818
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A110S/K273A/A442P/P444T
8.571
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A442P/P444T
9.375
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant wild-type enzyme
12.364
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant R334Q/A337R
14.103
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant K273A/A442P/T443E/P444A
15.581
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T
17.241
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T
35.294
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A
66.67
NAD+
pH 8.0, 25°C, recombinant mutant K273A/A442P/T443E/P444A
67.86
NAD+
pH 8.0, 25°C, recombinant mutant A110S/K273A/A442P/P444T
164.87
NAD+
pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A
178.79
NAD+
pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T
192
NAD+
pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T
0.74
NADP+
pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T
6.71
NADP+
pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T
6.82
NADP+
pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
low ALDH activity has been reported to cause intracellular accumulation of highly toxic 3-hydroxypropionaldehyde (3-HPA) seriously hampering the cell growth
metabolism
3-hydroxypropionate biosynthesis pathway from glycerol involves enzymes coenzyme B12-dependent glycerol dehydratase (DhaB) and aldehyde dehydrogenase (ALDH), overview. alpa-Ketoglutarate-semialdehyde dehydrogenase from Azospirillum basilensis (AbKGSADH) can catalyze the ALDH reaction forming 3-hydroxypropionate
physiological function
alpa-ketoglutarate-semialdehyde dehydrogenase from Azospirillum basilensis (AbKGSADH) can catalyze the ALDH reaction forming 3-hydroxypropionate, but it is not its physiological substrate
additional information
additional information
molecular docking simulations of AbKGSADH with 2-oxoglutaric semialdehyde (alpha-KGSA) and succinate semialdehyde (SSA). Molecular docking simulations reveal that these two substrates fit well into the somewhat positively charged substrate binding pocket. The aldehyde-groups of these substrates, which are the sites of enzyme reaction, are located in the same place around the catalytic residues. The aldehyde-group of alpha-KGSA is stabilized by Gln160 and Arg163 through hydrogen bonds, and two catalytic residues, Glu253 and Cys287, also assist the binding of the molecule. The 4'-oxo-group of alpha-KGSA is stabilized by hydrogen bonds with Arg281, and the carboxyl-group of the molecule is stabilized by Glu106 and Gln160. The substrate binding pocket is also formed by several hydrophobic residues, such as Phe156, Val286, Ile288, Pro444, and Phe450, which seem to contribute to the stabilization of the hydrophobic part of alpha-KGSA. The binding of SSA is similar to that of alpha-KGSA, however, the stabilization of the carboxyl-group of SSA is quite different. Arg281, a residue that is involved in the stabilization of the 4'-oxo-group of alpha-KGSA, forms a hydrogen bond with the carboxyl-group of SSA instead. These observations explain how AbKGSADH can accommodate both alpha-KGSA and SSA as real substrates
additional information
-
molecular docking simulations of AbKGSADH with 2-oxoglutaric semialdehyde (alpha-KGSA) and succinate semialdehyde (SSA). Molecular docking simulations reveal that these two substrates fit well into the somewhat positively charged substrate binding pocket. The aldehyde-groups of these substrates, which are the sites of enzyme reaction, are located in the same place around the catalytic residues. The aldehyde-group of alpha-KGSA is stabilized by Gln160 and Arg163 through hydrogen bonds, and two catalytic residues, Glu253 and Cys287, also assist the binding of the molecule. The 4'-oxo-group of alpha-KGSA is stabilized by hydrogen bonds with Arg281, and the carboxyl-group of the molecule is stabilized by Glu106 and Gln160. The substrate binding pocket is also formed by several hydrophobic residues, such as Phe156, Val286, Ile288, Pro444, and Phe450, which seem to contribute to the stabilization of the hydrophobic part of alpha-KGSA. The binding of SSA is similar to that of alpha-KGSA, however, the stabilization of the carboxyl-group of SSA is quite different. Arg281, a residue that is involved in the stabilization of the 4'-oxo-group of alpha-KGSA, forms a hydrogen bond with the carboxyl-group of SSA instead. These observations explain how AbKGSADH can accommodate both alpha-KGSA and SSA as real substrates
additional information
residues E253 and C287 are predicted as the catalytic residues
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
57000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
dimer
tetramer
although there are two AbKGSADH molecules in the asymmetric unit of our present structures, the tetrameric structure can be easily generated by one of the two folds from the P4322 crystallographic symmetry operation, structure modeling, overview. The monomeric structure of AbKGSADH consists of three domains: two core domains and one oligomerization domain (OGD). The core domains consist of the N-terminal domain (NTD) (Met1-Arg123 and Val145-Leu253) and the C-terminal domain (CTD) (Gly254-Pro469). The NTD is composed of seven alpha-helices (alpha1-alpha7) and nine beta-strands (beta1-beta4 and beta7-beta11), and forms the NAD(P)-binding Rossmann fold, where seven beta-strands (beta1-beta2 and beta7-beta11) form a large beta-sheet packed in the middle of the domain and other two beta-strands (beta3-beta4) are located on the surface of the domain. The three alpha-helices (alpha1, alpha6 and alpha7) and the four alpha-helices (alpha2-alpha5) occupy both sides of the central beta-sheet. The CTD consists of seven alpha-helices (alpha8-alpha14) and seven beta-strands (beta12-beta18). Seven beta-strands are also packed as a large beta-sheet in the middle of the domain. Six alpha-helices surround the central beta-sheet and one alpha-helix (alpha14) is located between the NTD and the OGD. The OGD (Val124-Pro144 and Tyr470-Val481) has two long beta-strands (beta6 and beta19) and one short beta-strand (beta5), which are packed in a line and protrude from the NTD
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in apoform and in complex with NAD+, sitting-drop vapor diffusion method, mixing of 0.001 ml of 60 mg/ml protein in 40 mM Tris-HCl pH 8.0 with 0.001 ml of reservoir solution containing 16% PEG 3350, 0.1 M sodium cacodylate, pH 6.5, and 0.2 M magnesium chloride hexahydrate, equilibration against 0.05 ml of reservoir solution, X-ray diffraction structure determination and analysis at 2.25 A and 2.30 A resolution, molecular replacement structure modeling using the structure of succinic semialdehyde dehydrogenase (SSADH) from Homo sapiens (PDB ID 2W8R) as a search model for the apoenzyme, and the crystal structure of the apoform of AbKGSADH as a template for the NAD+-complexed AbKGSADH structure
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
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)-T1 by nickel affinity chromatography, gel filtration, and ultrafiltration
recombinant N-terminally His6-tagged wild-type and mutant KGSADH enzymes from Escherichia coli strain DH10beta by nickel affinity chromatography and ultrafiltration
KGSADH-II purified on nickel-nitrilotriacetic acid spin column and by gel filtration
KGSADH-III purified on nickel-nitrilotriacetic acid spin column and by gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene araE, sequence comparisons of 3-hydroxypropionate producing ALDHs, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)-T1
recombinant expression of N-terminally His6-tagged wild-type and mutant KGSADH enzymes in Escherichia coli strain DH10beta
KGSADH-II overexpressed as His6-tagged protein in Escherichia coli DH5alpha
KGSADH-III overexpressed as His6-tagged protein in Escherichia coli DH5alpha
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
-
three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
-
three different types of KGSADH appear in the bacterial evolutional stage convergently
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Watanabe, S.; Yamada, M.; Ohtsu, I.; Makino, K.
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, D-galactarate, and hydroxy-L-proline. Molecular and metabolic convergent evolution
J. Biol. Chem.
282
6685-6695
2007
Azospirillum brasilense (Q08IB7), Azospirillum brasilense (Q08IC0), Azospirillum brasilense (Q1JUP4), Azospirillum brasilense, Azospirillum brasilense ATCC 29145 (Q08IB7), Azospirillum brasilense ATCC 29145 (Q08IC0), Azospirillum brasilense ATCC 29145 (Q1JUP4), Bacillus subtilis
Park, Y.S.; Choi, U.J.; Nam, N.H.; Choi, S.J.; Nasir, A.; Lee, S.G.; Kim, K.J.; Jung, G.Y.; Choi, S.; Shim, J.Y.; Park, S.; Yoo, T.H.
Engineering an aldehyde dehydrogenase toward its substrates, 3-hydroxypropanal and NAD+, for enhancing the production of 3-hydroxypropionic acid
Sci. Rep.
7
17155
2017
Azospirillum brasilense (Q1JUP4)
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