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Information on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating) and Organism(s) Pseudomonas sp. and UniProt Accession Q52060

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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 .
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This record set is specific for:
Pseudomonas sp.
UNIPROT: Q52060
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Word Map
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The taxonomic range for the selected organisms is: Pseudomonas sp.
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), 4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase, nonphosphorylating acylating aldehyde dehydrogenase, coenzyme a linked aldehyde dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase
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bifunctional enzyme
ACDH
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Acetaldehyde dehydrogenase [acetylating]
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acetyl-CoA reductase
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aldehyde dehydrogenase (acylating)
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CoA-dependent aldehyde dehydrogenase
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-
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coenzyme A linked aldehyde dehydrogenase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
show the reaction diagram
part of a bifunctional enzyme complex that also displays 4-hydroxy-2-ketovalerate aldolase activity
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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-
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reduction
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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
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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
show the reaction diagram
formaldehyde + CoA + NAD+
formyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
show the reaction diagram
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-
-
-
?
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
show the reaction diagram
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-
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-
?
propanal + CoA + NAD+
propionyl-CoA + NADH
show the reaction diagram
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initial rate of reaction with propanal is 2.7fold slower than that with acetaldehyde
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-
?
additional information
?
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DmpFG is a bifunctional enzyme comprised of an aldolase subunit, DmpG, and a dehydrogenase subunit, DmpF. The aldehyde intermediate produced by the aldolase is channeled directly through a buried molecular channel in the protein structure from the aldolase to the dehydrogenase active site. Binding and channeling of alternative substrates in the enzyme DmpFG, molecular dynamics, overview
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?
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
show the reaction diagram
additional information
?
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DmpFG is a bifunctional enzyme comprised of an aldolase subunit, DmpG, and a dehydrogenase subunit, DmpF. The aldehyde intermediate produced by the aldolase is channeled directly through a buried molecular channel in the protein structure from the aldolase to the dehydrogenase active site. Binding and channeling of alternative substrates in the enzyme DmpFG, molecular dynamics, overview
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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rate of reaction with NADP+ is only 7% of that with NAD+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
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activity increases gradually over pH range from 6.5 to 8.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
dmpF
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
DmpFG catalyzes the final two steps of the meta-cleavage pathway of catechol and its methylated substituents. This pathway breaks down toxic waste products such as naphthalenes, salicylates, and benzoates to harmless metabolites
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
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148000
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gel filtration, molecular mass of enzyme complex, occurs in complex with 4-hydroxy-2-ketovalerate
32500
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2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate
39000
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2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
additional information
DmpFG is a microbial enzyme comprised of two subunits DmpG and DmpF
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method, streak-seeding
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I159A
site-directed mutagenesis, the barrier into the dehydrogenase active site region has been virtually eliminated such that acetaldehyde is transported from one active site to the other in a downhill process
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity is highest in HEPES buffer and somewhat lower in phosphate buffer, activity in Tris buffer is about half the rate in HEPES buffer
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 10 mM phosphate buffer, pH 7.5, 1 mM dithiothreitol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Powlowski, J.; Sahlman, L.; Shingler, V.
Purification and properties of the physically associated meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600
J. Bacteriol.
175
377-385
1993
Pseudomonas sp., Pseudomonas sp. CF 600
Manually annotated by BRENDA team
Manjasetty, B.A.; Croteau, N.; Powlowski, J.; Vrielink, A.
Crystallization and preliminary x-ray analysis of dmpFG-encoded 4-hydroxy-2-ketovalerate aldolase-aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600
Acta Crystallogr. Sect. D
57
582-585
2001
Pseudomonas sp., Pseudomonas sp. CF 600
Manually annotated by BRENDA team
Platt, A.; Shingler, V.; Taylor, S.C.; Williams, P.A.
The 4-hydroxy-2-oxovalerate aldolase and acetaldehyde dehydrogenase (acylating) encoded by the nahM and nahO genes of the naphthalene catabolic plasmid pWW60-22 provide further evidence of conservation of meta-cleavage pathway gene sequences
Microbiology
141
223-233
1995
Pseudomonas sp., Pseudomonas sp. NCIMB9816
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Manually annotated by BRENDA team
Manjasetty, B.A.; Powlowski, J.; Vrielink, A.
Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate
Proc. Natl. Acad. Sci. USA
100
6992-6997
2003
Pseudomonas sp., Pseudomonas sp. CF 600
Manually annotated by BRENDA team
Smith, N.E.; Vrielink, A.; Attwood, P.V.; Corry, B.
Binding and channeling of alternative substrates in the enzyme DmpFG: a molecular dynamics study
Biophys. J.
106
1681-1690
2014
Pseudomonas sp. (Q52060), Pseudomonas sp. CF 600 (Q52060)
Manually annotated by BRENDA team