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Information on EC 1.2.1.87 - propanal dehydrogenase (CoA-propanoylating) and Organism(s) Thermus thermophilus and UniProt Accession Q53WH9

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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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Thermus thermophilus
UNIPROT: Q53WH9
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The taxonomic range for the selected organisms is: Thermus thermophilus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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
-
-
-
?
propionaldehyde + CoA + NAD+
propanoyl-CoA + NADH + H+
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.5 - 23.6
acetaldehyde
6.4 - 23.1
propionaldehyde
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2 - 17.2
acetaldehyde
2.3 - 16.3
propionaldehyde
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14 - 1.35
acetaldehyde
0.14 - 1.31
propionaldehyde
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
together with TTHB246, EC 4.1.3.43, the enzyme forms a bacterial aldolase-dehydrogenase complex catalyzing the last steps in the meta cleavage pathway of aromatic hydrocarbon degradation
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
137000
molecular mass of BphI-TTHB247 chimeric complex, determined by static light scattering
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
33000
40000
native molecular mass of TTHB247, determined by gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified to homogeneity using Ni2+-NTA chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baker, P.; Hillis, C.; Carere, J.; Seah, S.Y.K.
Protein-protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes
Biochemistry
51
1942-1952
2012
Thermus thermophilus (Q53WH9)
Manually annotated by BRENDA team