Information on EC 1.2.1.87 - propanal dehydrogenase (CoA-propanoylating)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.1.87
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RECOMMENDED NAME
GeneOntology No.
propanal dehydrogenase (CoA-propanoylating)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
propanal + CoA + NAD+ = propanoyl-CoA + NADH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,2-propanediol biosynthesis from lactate (engineered)
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androstenedione degradation
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L-1,2-propanediol degradation
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androgen and estrogen metabolism
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propanol degradation
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Xylene degradation
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Propanoate metabolism
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Metabolic pathways
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Microbial metabolism in diverse environments
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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+
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?
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
show the reaction diagram
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
show the reaction diagram
butyraldehyde + CoA + NAD+
butyryl-CoA + NAD+ + H+
show the reaction diagram
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?
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NAD+ + H+
show the reaction diagram
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?
pentaldehyde + CoA + NAD+
pentanoyl-CoA + NADH + H+
show the reaction diagram
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?
propanal + CoA + NAD+
propanoyl-CoA + NADH + H+
show the reaction diagram
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?
propanoyl-CoA + NADH + H+
propanal + CoA + NAD+
show the reaction diagram
propionaldehyde + CoA + NAD+
propanoyl-CoA + NADH + H+
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
show the reaction diagram
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
show the reaction diagram
propanal + CoA + NAD+
propanoyl-CoA + NADH + H+
show the reaction diagram
Q79AF6
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?
propanoyl-CoA + NADH + H+
propanal + CoA + NAD+
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
5.5 - 35
acetaldehyde
0.0926 - 0.342
acetyl-CoA
0.056 - 0.087
Butanoyl-CoA
31.7
Butyraldehyde
app. Km-value, pH 8.0 and 25C, NAD+
7.7
Isobutyraldehyde
app. Km-value, pH 8.0 and 25C, NAD+
0.0348
NAD+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25C
0.561
NADP+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25C
2 - 48
propionaldehyde
additional information
additional information
Michaelis-Menten kientics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2 - 42
acetaldehyde
4.63 - 14.81
acetyl-CoA
7.02 - 25.38
Butanoyl-CoA
9.5
Butyraldehyde
pH 8.0 and 25C, NAD+
11.2
Isobutyraldehyde
pH 8.0 and 25C, NAD+
14.1
NAD+
with acetaldehyde as substrate, pH 8.0 and 25C
12.9
NADP+
with acetaldehyde as substrate, pH 8.0 and 25C
2.3 - 46
propionaldehyde
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14 - 1.35
acetaldehyde
25 - 122
acetyl-CoA
125 - 292
Butanoyl-CoA
0.3
Butyraldehyde
app. Km-value, pH 8.0 and 25C, NAD+
1.4
Isobutyraldehyde
app. Km-value, pH 8.0 and 25C, NAD+
405.2
NAD+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25C
22.99
NADP+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25C
0.076
pentaldehyde
app. Km-value, pH 8.0 and 25C, NAD+
0.14 - 1.31
propionaldehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.9
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with butanoyl-CoA, pH 7.15, 30C
17
with butanoyl-CoA, pH 7.15, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
SDS-PAGE, in agreement with the predicted molecular mass calculated from amino acid sequence
33000
estimated by SDS-PAGE, in agreement with predicted molecular mass calculated from amino acid sequences; native molecular mass of TTHB247, determined by static light scattering
37000
BphI-BphJ-complex, alpha2beta2, 2 * 32000 BphJ, 2 * 37000 BphI, estimated by gel filtration
40000
native molecular mass of TTHB247, determined by gel filtration
137000
molecular mass of BphI-TTHB247 chimeric complex, determined by static light scattering
140000
native molecular mass of the purified BphI-BphJ-complex, estimated by gel filtration
142000
native molecular mass of TTHB246-TTHB247 complex, determined by gel filtration
144000
molecular mass of BphI-TTHB247 chimeric complex, determined by gel filtration
152000
native molecular mass of TTHB246-TTHB247 complex, determined by static light scattering
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
BphI-BphJ-complex, alpha2beta2, 2 * 32000 BphJ, 2 * 37000 BphI, estimated by gel filtration
monomer
1 * 33000, SDS-PAGE, enzyme can form a stable heterotetrameric complex with TTHB246 in vitro, consisting of two aldolase and two dehydrogenase subunits
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
half-life in complex with TTHB246 is 5.9 h; half-life of chimeric BphI-TTHB247 complex is 0.54 h for BphI activity and 2.47 for TTHB247 activity; half-life of single enzyme is 1.6 h
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is oxygen-tolerant
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme can be stored at -80C, 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, after purification N-terminal histidine tag of BphJ is proteolytically cleaved by thrombin digestion
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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
purified to homogeneity using Ni2+-NTA chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bphI and bphJ cloned into the plasmids pBTL4-T7 and pET28a
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chimeric complexes of Burkholderia xenovorans and Thermus thermophilus enzymes, TTHB246-BphJ and BphI-TTHB247 created by coexpression of the relevant genes in Escherichia coli using separate expression plasmids; separate expression of TTHB247 in recombinant Escherichia coli
coexpression of bphI and bphJ in Escherichia coli using two compatible plasmids (pBTL4 and pET28a) yield soluble proteins
gene pduP, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 results in autotrophic n-butanol production. PduP from Klebsiella pneumoniae produces more n-butanol than ethanol
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gene pduP, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 results in autotrophic n-butanol production. PduP from Listeria monocytogenes produces more ethanol than n-butanol
gene pduP, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 results in autotrophic n-butanol production. PduP from Salmonella enterica produces more ethanol than n-butanol
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I195F
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created by site-specific mutagenesis, no significant reduction of channeling efficiency of the enzyme complex toward acetaldehyde or propionaldehyde
I195L
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created by site-specific mutagenesis
additional information
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design of a coenzyme A (CoA) dependent n-butanol biosynthesis pathway tailored to the metabolic physiology of the cyanobacterium Synechococcus elongatus PCC 7942 by incorporating an ATP driving force and a kinetically irreversible trap. Oxygen-sensitive CoA-acylating butyraldehyde dehydrogenase (Bldh) is exchanged for the oxygen-tolerant PduP from Salmonella enterica. Replacing Bldh with PduP in the n-butanol synthesis pathway results in n-butanol production to a cumulative titer of 404 mg/l with peak productivity of 51 mg/l per day, exceeding the base strain by 20fold. Anaerobic growth rescue of Escherichia coli strain JCL166 by overexpression of the Clostridium butanol pathway with different aldehyde dehydrogenases PduP