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Information on EC 1.2.1.77 - 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+) for references in articles please use BRENDA:EC1.2.1.77
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EC Tree
IUBMB Comments This enzyme catalyses a step in the aerobic benzoyl-coenzyme A catabolic pathway in Azoarcus evansii and Burkholderia xenovorans.
The enzyme appears in viruses and cellular organisms
Synonyms
nadp+-dependent aldehyde dehydrogenase, 3,4-dehydroadipyl-coa semialdehyde dehydrogenase,
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3,4-dehydroadipyl-CoA semialdehyde dehydrogenase
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NADP+-dependent aldehyde dehydrogenase
BoxD
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NADP+-dependent aldehyde dehydrogenase
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NADP+-dependent aldehyde dehydrogenase
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3,4-didehydroadipyl-CoA semialdehyde + NADP+ + H2O = 3,4-didehydroadipyl-CoA + NADPH + H+
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3,4-dehydroadipyl-CoA semialdehyde:NADP+ oxidoreductase
This enzyme catalyses a step in the aerobic benzoyl-coenzyme A catabolic pathway in Azoarcus evansii and Burkholderia xenovorans.
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3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
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cis-3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
cis-3,4-dehydroadipyl-CoA + NADPH + H+
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catalytic mechanism proposed in detail
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formaldehyde + NADP+ + H2O
formate + NADPH + H+
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heptaldehyde + NADP+ + H2O
heptanoate + NADPH + H+
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isovaleraldehyde + NADP+ + H2O
isovalerate + NADPH + H+
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propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
valeraldehyde + NADP+ + H2O
valerate + NADPH + H+
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additional information
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the native substrate (3,4-dehydroadipyl-CoA semialdehyde) is not tested as it is commercially unavailable. The enzyme is preferentially active towards linear medium-chain to long-chain aldehydes as compared to branched-chain, short-chain or aromatic aldehydes
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3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
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3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
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enzyme of the aerobic benzoyl-coenzyme A catabolic pathway
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3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
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the molar ratio of mol of converted substrate per mol of NADPH formed is estimated to be 1
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3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
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3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
the enzyme is involved in the benzoate oxidation (box) pathway
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propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
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propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
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propionaldehyde is used as the aldehydic substrate in enzyme assay because of commercial unavailability of the native substrate
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3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
cis-3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
cis-3,4-dehydroadipyl-CoA + NADPH + H+
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catalytic mechanism proposed in detail
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3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
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enzyme of the aerobic benzoyl-coenzyme A catabolic pathway
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3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
Q13WK4
the enzyme is involved in the benzoate oxidation (box) pathway
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NAD+
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the enzyme is more active in the presence of NADP+ relative to NAD+. Crystallographic data show that cofactor selectivity is governed by a complex network of hydrogen bonds between the oxygen atoms of the 2'-phosphoryl moiety of NADP+ and a threonine/lysine pair on the enzyme
NADP+
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the enzyme is more active in the presence of NADP+ relative to NAD+. Crystallographic data show that cofactor selectivity is governed by a complex network of hydrogen bonds between the oxygen atoms of the 2'-phosphoryl moiety of NADP+ and a threonine/lysine pair on the enzyme
NADP+
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no activity (below 2%) with NAD+. The molar ratio of mol of converted substrate per mol of NADPH formed is estimated to be 1
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additional information
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salt concentrations up to 500 mM KCl have no effect on enzyme activity
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additional information
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salt concentrations up to 500 mM KCl and EDTA concentrations up to 50 mM have no effect on enzyme activity
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0.025
3,4-dehydroadipyl-CoA semialdehyde
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pH 7.2
4.15
benzaldehyde
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in 50 mM Tris-HCl (pH 7.5), at 25°C
1.9
formaldehyde
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in 50 mM Tris-HCl (pH 7.5), at 25°C
0.042
heptaldehyde
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in 50 mM Tris-HCl (pH 7.5), at 25°C
1.66
Isovaleraldehyde
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in 50 mM Tris-HCl (pH 7.5), at 25°C
0.501
NAD+
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in 50 mM Tris-HCl (pH 7.5), at 25°C
1.21
propionaldehyde
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in 50 mM Tris-HCl (pH 7.5), at 25°C
0.3
Valeraldehyde
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in 50 mM Tris-HCl (pH 7.5), at 25°C
0.016
NADP+
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pH 7.2
0.04
NADP+
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in 50 mM Tris-HCl (pH 7.5), at 25°C
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45
3,4-dehydroadipyl-CoA semialdehyde
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pH 7.2
0.019
benzaldehyde
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in 50 mM Tris-HCl (pH 7.5), at 25°C
0.046
formaldehyde
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in 50 mM Tris-HCl (pH 7.5), at 25°C
29.9
heptaldehyde
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in 50 mM Tris-HCl (pH 7.5), at 25°C
0.074
Isovaleraldehyde
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in 50 mM Tris-HCl (pH 7.5), at 25°C
0.501
NAD+
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in 50 mM Tris-HCl (pH 7.5), at 25°C, cosubstrate: propionaldehyde
2.32 - 162
propionaldehyde
5.16
Valeraldehyde
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in 50 mM Tris-HCl (pH 7.5), at 25°C
additional information
additional information
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no activities detectable for C296A and E257Q mutant enzymes
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0.04
NADP+
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in 50 mM Tris-HCl (pH 7.5), at 25°C, cosubstrate: propionaldehyde
2.32
propionaldehyde
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in 50 mM Tris-HCl (pH 7.5), at 25°C
5.75
propionaldehyde
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H485A mutant enzyme, pH 7.5, temperature not specified in the publication
12.1
propionaldehyde
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K168A mutant enzyme, pH 7.5, temperature not specified in the publication
14.6
propionaldehyde
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E400A mutant enzyme, pH 7.5, temperature not specified in the publication
16.2
propionaldehyde
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E496A mutant enzyme, pH 7.5, temperature not specified in the publication
36.8
propionaldehyde
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E167A mutant enzyme, pH 7.5, temperature not specified in the publication
162
propionaldehyde
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wild type enzyme, pH 7.5, temperature not specified in the publication
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0.17
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extracts of cells grown aerobically on benzoate
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6.2 - 8.8
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50% of maximal activity at pH 6.2 and pH 8.8
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brenda
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brenda
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Uniprot
brenda
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metabolism
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enzyme catalyzes an essential step in the metabolism of benzoate in Burkholderia xenovorans LB400
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forms a dimer in solution with a molecular mass of 110000, SDS-PAGE
homodimer
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2 * 54000
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E257Q-NADP+ mutant at 1.4 A resolution, C296A-NADP+ at 1.4 A resolution, E167A mutant at 1.6 A resolution, E496A mutant at 1.65 A resolution
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sitting drop vapour diffusion method, at 18°C in 29% PEG 3350K and 100 mM bis-Tris (pH 6.0), 1.6 A crystal structure of ALDHC in complex with NADPH bound in the cofactor-binding pocket and an ordered fragment of a polyethylene glycol molecule bound in the substrate tunnel
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C296A
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same purification behavior as the native enzyme indicating that the mutation does not alter basic enzyme structure, but no catalytic activity detected consistent with a critical nucleophilic role for C296
E167A
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significant reduction in enzyme activity but not perturbing the overall structure, significant reduction in activity of 77%, likely candidate to present the catalytic water to the general base E257 that leads to deacylation and product release
E257Q
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tolerated with respect to overall protein stability, but dramatic reduction in kcat value and no activity detectable, E257 serves probably as the primary general base to deprotonate the nucleophilic C296
E400A
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91% reduction in kcat value, E400 plays an essential role in facilitating the acquisition of the hydride conformation
E496A
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significant reduction in enzyme activity but not perturbing the overall structure, significant reduction in activity of 90%
H485A
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dramatic reduction in enzyme solubility
H485Q
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completely recalcitrant to purification, H485 may be important in stabilizing the nicotinamide amide moiety of NADP+
K168A
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significant reduction in enzyme activity but not perturbing the overall structure, significant reduction in activity of 92.5%, K168 likely serves to stabilize charges and tune pKa of the active site glutamate side-chains
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-20°C, enzyme could be stored without appreciable loss of activity for months at -20°C in the presence of 10% (v/v) glycerol
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by nickel affinity column and gel filtration
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expressed in Escherichia coli BL21 Star (DE3) cells
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expression in Escherichia coli as a protein tagged at its N terminus with maltose-binding protein
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mutations confirmed by sequence analysis
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Bajns J., Boulanger MJ.
Structural and biochemical characterization of a novel aldehyde dehydrogenase encoded by the benzoate oxidation pathway in Burkholderia xenovorans LB400
J. Mol. Biol.
379
597-608
2008
Paraburkholderia xenovorans (Q13WK4)
brenda
Gescher, J.; Ismail, W.; Olgeschläger, E.; Eisenreich, W.; Wörth, J.; Fuchs, G.
Aerobic benzoyl-coenzyme A (CoA) catabolic pathway in: conversion of ring cleavage product by 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase
J. Bacteriol.
188
2919-2927
2006
Azoarcus evansii
brenda
Rather, L.J.; Knapp, B.; Haehnel, W.; Fuchs, G.
Coenzyme A-dependent aerobic metabolism of benzoate via epoxide formation
J. Biol. Chem.
285
20615-20624
2010
Azoarcus evansii, Azoarcus evansii KB740
brenda
Bains, J.; Leon, R.; Temke, K.G.; Boulanger, M.J.
Elucidating the reaction mechanism of the benzoate oxidation pathway encoded aldehyde dehydrogenase from Burkholderia xenovorans LB400
Protein Sci.
20
1048-1059
2011
Paraburkholderia xenovorans (Q13WK4)
brenda
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1.2.1.77 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)
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