Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating) and Organism(s) Paraburkholderia xenovorans and UniProt Accession Q79AF6

for references in articles please use BRENDA:EC1.2.1.10
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Also acts, more slowly, on glycolaldehyde, propanal and butanal. In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87, propanal dehydrogenase (propanoylating). Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols. NADP+ can replace NAD+ but the rate of reaction is much slower .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Paraburkholderia xenovorans
UNIPROT: Q79AF6
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Paraburkholderia xenovorans
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
acetaldehyde
+
CoA
+
NAD+
=
acetyl-CoA
+
NADH
+
H+
+
+
=
+
+
Synonyms
dmpfg, coa-dependent aldehyde dehydrogenase, acetyl-coa reductase, tthb247, aldehyde dehydrogenase (acylating), nonphosphorylating acylating aldehyde dehydrogenase, coenzyme a linked aldehyde dehydrogenase, 4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nonphosphorylating acylating aldehyde dehydrogenase
-
ACDH
-
-
-
-
Acetaldehyde dehydrogenase [acetylating]
-
-
-
-
acetyl-CoA reductase
-
-
-
-
aldehyde dehydrogenase (acylating)
-
-
-
-
CoA-dependent aldehyde dehydrogenase
-
-
-
-
coenzyme A linked aldehyde dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetaldehyde:NAD+ oxidoreductase (CoA-acetylating)
Also acts, more slowly, on glycolaldehyde, propanal and butanal. In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87, propanal dehydrogenase (propanoylating). Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols. NADP+ can replace NAD+ but the rate of reaction is much slower [3].
CAS REGISTRY NUMBER
COMMENTARY hide
9028-91-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
show the reaction diagram
-
-
-
?, r
butyraldehyde + CoA + NAD+
butyryl-CoA + NADH + H+
show the reaction diagram
-
-
-
r
pentaldehyde + CoA + NAD+
pentyl-CoA + NADH + H+
show the reaction diagram
-
-
-
r
picolinaldehyde + CoA + NAD+
picolinyl-CoA + NADH + H+
show the reaction diagram
-
-
-
r
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
show the reaction diagram
-
-
-
r
additional information
?
-
BphJ forms a heterotetrameric complex with the class II aldolase BphI that channels aldehydes produced in the aldol cleavage reaction to the dehydrogenase via a molecular tunnel
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17 - 133
acetaldehyde
4.6 - 31.7
Butyraldehyde
8.2
pentaldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
3.2 - 18.2
picolinaldehyde
20.4 - 79.5
propionaldehyde
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.9 - 37.9
acetaldehyde
7.1 - 16.7
Butyraldehyde
13
pentaldehyde
mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)
1.9 - 3.2
picolinaldehyde
3.4 - 24.9
propionaldehyde
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.147 - 2.224
acetaldehyde
0.0433 - 2.763
Butyraldehyde
0.0265 - 1.584
pentaldehyde
0.00011 - 0.597
picolinaldehyde
0.0425 - 1.219
propionaldehyde
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D208A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
I171A
level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover. The mutation results in a 35% reduction in acetaldehyde channeling efficiency
I171F
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
I195A
the variant has a 20fold higher catalytic efficiency for butyraldehyde and pentaldehyde compared to the catalytic efficiency of the wild type toward its natural substrate acetaldehyde. The mutation results in a 35% reduction in acetaldehyde channeling efficiency
I195F
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
I195W
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
N170A
the mutation does not substantially alter aldehyde channeling efficiencies. The level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover
N170D
level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baker, P.; Carere, J.; Seah, S.Y.
Substrate specificity, substrate channeling, and allostery in BphJ: an acylating aldehyde dehydrogenase associated with the pyruvate aldolase BphI
Biochemistry
51
4558-4567
2012
Paraburkholderia xenovorans (Q79AF6)
Manually annotated by BRENDA team