BRENDA home
History
Information on EC 1.2.1.77 - 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.2.1.77Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.2.1.77 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)IUBMB Comments
This enzyme catalyses a step in the aerobic benzoyl-coenzyme A catabolic pathway in Azoarcus evansii and Burkholderia xenovorans.
Specify your search results
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase, ALDH, ALDHC, BoxD, NADP+-dependent aldehyde dehydrogenase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BoxD
NADP+-dependent aldehyde dehydrogenase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3,4-didehydroadipyl-CoA semialdehyde + NADP+ + H2O = 3,4-didehydroadipyl-CoA + NADPH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
3,4-didehydroadipyl-CoA semialdehyde + NAD+ + H2O
3,4-didehydroadipyl-CoA + NADH + H+
-
-
-
r
cis-3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
cis-3,4-dehydroadipyl-CoA + NADPH + H+
catalytic mechanism proposed in detail
-
-
?
heptaldehyde + NADP+ + H2O
heptanoate + NADPH + H+
-
-
-
?
isovaleraldehyde + NADP+ + H2O
isovalerate + NADPH + H+
-
-
-
?
additional information
?
-
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
-
-
?
3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
-
-
-
-
?
3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
-
enzyme of the aerobic benzoyl-coenzyme A catabolic pathway
-
-
?
3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
-
the molar ratio of mol of converted substrate per mol of NADPH formed is estimated to be 1
-
-
?
3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
-
-
-
-
?
3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
the enzyme is involved in the benzoate oxidation (box) pathway
-
-
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
-
-
-
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
propionaldehyde is used as the aldehydic substrate in enzyme assay because of commercial unavailability of the native substrate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
cis-3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
cis-3,4-dehydroadipyl-CoA + NADPH + H+
catalytic mechanism proposed in detail
-
-
?
3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
-
enzyme of the aerobic benzoyl-coenzyme A catabolic pathway
-
-
?
3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O
3,4-dehydroadipyl-CoA + NADPH + H+
the enzyme is involved in the benzoate oxidation (box) pathway
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
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+
-
no activity (below 2%) with NAD+. The molar ratio of mol of converted substrate per mol of NADPH formed is estimated to be 1
NADP+
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
salt concentrations up to 500 mM KCl have no effect on enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
salt concentrations up to 500 mM KCl and EDTA concentrations up to 50 mM have no effect on enzyme activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.66
Isovaleraldehyde
in 50 mM Tris-HCl (pH 7.5), at 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.074
Isovaleraldehyde
in 50 mM Tris-HCl (pH 7.5), at 25°C
0.501
NAD+
in 50 mM Tris-HCl (pH 7.5), at 25°C, cosubstrate: propionaldehyde
additional information
additional information
no activities detectable for C296A and E257Q mutant enzymes
-
0.04
NADP+
in 50 mM Tris-HCl (pH 7.5), at 25°C, cosubstrate: propionaldehyde
5.75
propionaldehyde
H485A mutant enzyme, pH 7.5, temperature not specified in the publication
12.1
propionaldehyde
K168A mutant enzyme, pH 7.5, temperature not specified in the publication
14.6
propionaldehyde
E400A mutant enzyme, pH 7.5, temperature not specified in the publication
16.2
propionaldehyde
E496A mutant enzyme, pH 7.5, temperature not specified in the publication
36.8
propionaldehyde
E167A mutant enzyme, pH 7.5, temperature not specified in the publication
162
propionaldehyde
wild type enzyme, pH 7.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
enzyme catalyzes an essential step in the metabolism of benzoate in Burkholderia xenovorans LB400
Show AA Sequence and Transmembrane Helices (273 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
forms a dimer in solution with a molecular mass of 110000, SDS-PAGE
homodimer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C296A
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
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
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
91% reduction in kcat value, E400 plays an essential role in facilitating the acquisition of the hydride conformation
E496A
significant reduction in enzyme activity but not perturbing the overall structure, significant reduction in activity of 90%
H485Q
completely recalcitrant to purification, H485 may be important in stabilizing the nicotinamide amide moiety of NADP+
K168A
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, enzyme could be stored without appreciable loss of activity for months at -20°C in the presence of 10% (v/v) glycerol
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as a protein tagged at its N terminus with maltose-binding protein
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Aromatoleum 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
Aromatoleum evansii, Aromatoleum 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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.2.1.77)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
About BRENDA
Help
Download
Contribution
member of
curated at
curated at
Server: brenda6 Ver: 69ad221-main (2022-06-24 14:26:09 +0200)