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Information on EC 1.2.1.87 - propanal dehydrogenase (CoA-propanoylating) and Organism(s) Paraburkholderia xenovorans and UniProt Accession Q79AF6

for references in articles please use BRENDA:EC1.2.1.87
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EC Tree
IUBMB Comments
The enzyme forms a bifunctional complex with EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase, with a tight channel connecting the two subunits [1,2,3]. Also acts, more slowly, on glycolaldehyde and butanal. In Pseudomonas species the 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 1.2.1.10, acetaldehyde dehydrogenase (acetylating). NADP+ can replace NAD+ with a much slower rate .
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Paraburkholderia xenovorans
UNIPROT: Q79AF6
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The taxonomic range for the selected organisms is: Paraburkholderia xenovorans
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
propanal
+
CoA
+
NAD+
=
propanoyl-CoA
+
NADH
+
H+
+
+
=
+
+
Synonyms
BphJ, CoA-acylating aldehyde dehydrogenase, coenzyme A-acylating aldehyde dehydrogenase, More, PduP, TTHB247, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
propanal:NAD+ oxidoreductase (CoA-propanoylating)
The enzyme forms a bifunctional complex with EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase, with a tight channel connecting the two subunits [1,2,3]. Also acts, more slowly, on glycolaldehyde and butanal. In Pseudomonas species the 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 1.2.1.10, acetaldehyde dehydrogenase (acetylating). NADP+ can replace NAD+ with a much slower rate [3].
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
-
-
-
?
acetaldehyde + CoA + NADP+
acetyl-CoA + NADPH + H+
show the reaction diagram
BphJ is able to utilize NAD+ and NADP+ with comparable kcat values, but the apparent Km-value for NAD+ is 16fold lower than for NADP+
-
-
?
butyraldehyde + CoA + NAD+
butyryl-CoA + NADH + H+
show the reaction diagram
-
-
-
?
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH + H+
show the reaction diagram
-
-
-
?
pentaldehyde + CoA + NAD+
pentanoyl-CoA + NADH + H+
show the reaction diagram
-
-
-
?
propanal + CoA + NAD+
propanoyl-CoA + NADH + H+
show the reaction diagram
-
-
-
?
propionaldehyde + CoA + NAD+
propanoyl-CoA + NADH + H+
show the reaction diagram
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
?
propionaldehyde + CoA + NAD+
propanoyl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
no activity with succinic semialdehyde and picolinaldehyde
-
-
?
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
propanal + CoA + NAD+
propanoyl-CoA + NADH + H+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
BphJ is able to utilize NAD+ and NADP+ with comparable kcat values, but the apparent Km-value for NAD+ is 16fold lower than for NADP+
NADP+
BphJ is able to utilize NAD+ and NADP+ with comparable kcat values, but the apparent Km-value for NAD+ is 16fold lower than for NADP+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
23.6
acetaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
31.7
Butyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
7.7
Isobutyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
0.0348
NAD+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
0.561
NADP+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
23.1
propionaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
7.4 - 35
acetaldehyde
2 - 48
propionaldehyde
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17.2
acetaldehyde
pH 8.0 and 25°C, NAD+
9.5
Butyraldehyde
pH 8.0 and 25°C, NAD+
11.2
Isobutyraldehyde
pH 8.0 and 25°C, NAD+
14.1
NAD+
with acetaldehyde as substrate, pH 8.0 and 25°C
12.9
NADP+
with acetaldehyde as substrate, pH 8.0 and 25°C
16.3
propionaldehyde
pH 8.0 and 25°C, NAD+
16 - 42
acetaldehyde
8.9 - 46
propionaldehyde
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.73
acetaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
0.3
Butyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
1.4
Isobutyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
405.2
NAD+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
22.99
NADP+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
0.076
pentaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
0.7
propionaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
enzyme forms a bifunctional complex with EC 4.1.3.43 (BphI), 4-hydroxy-2-oxohexanoate aldolase and is part of the polychlorinated biphenyl degradation pathway
metabolism
-
enzyme is part of the BphI-BphJ-complex, an aldolase-dehydrogenase-complex from the polychlorinated biphenyl degradation pathway
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
native molecular mass of the purified BphI-BphJ-complex, estimated by gel filtration
32000
SDS-PAGE, in agreement with the predicted molecular mass calculated from amino acid sequence
37000
BphI-BphJ-complex, alpha2beta2, 2 * 32000 BphJ, 2 * 37000 BphI, estimated by gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
BphI-BphJ-complex, alpha2beta2, 2 * 32000 BphJ, 2 * 37000 BphI, estimated by gel filtration
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I195F
-
created by site-specific mutagenesis, no significant reduction of channeling efficiency of the enzyme complex toward acetaldehyde or propionaldehyde
I195L
-
created by site-specific mutagenesis
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme can be stored at -80°C, without loss of activity for at least 12 months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
BphI and BphJ form a stable complex as they bind and coelute from Ni2+-NTA column, although only BphJ has the histidine tag. After purification, the N-terminal histidine tag of BphJ is proteolytically cleaved by thrombin digestion
BphI and BphJ form a stable complex as they bind and coelute from Ni2+-NTA column, after purification N-terminal histidine tag of BphJ is proteolytically cleaved by thrombin digestion
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpression of bphI and bphJ in Escherichia coli using two compatible plasmids (pBTL4 and pET28a) yield soluble proteins
bphI and bphJ cloned into the plasmids pBTL4-T7 and pET28a
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baker, P.; Pan, D.; Carere, J.; Rossi, A.; Wang, W.; Seah, S.Y.K.
Characterization of an aldolase-dehydrogenase complex that exhibits substrate channeling in the polychlorinated biphenyls degradation pathway
Biochemistry
48
6551-6558
2009
Paraburkholderia xenovorans (Q79AF6)
Manually annotated by BRENDA team
Carere, J.; Baker, P.; Seah, S.Y.K.
Investigating the molecular determinants for substrate channeling in BphI-BphJ, an aldolase-dehydrogenase complex from the polychlorinated biphenyls degradation pathway
Biochemistry
50
8407-8416
2011
Paraburkholderia xenovorans
Manually annotated by BRENDA team