Information on EC 1.2.1.57 - butanal dehydrogenase

for references in articles please use BRENDA:EC1.2.1.57
Word Map on EC 1.2.1.57
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.1.57
-
RECOMMENDED NAME
GeneOntology No.
butanal dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
butanal + CoA + NAD(P)+ = butanoyl-CoA + NAD(P)H + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pyruvate fermentation to butanol I
-
-
pyruvate fermentation to butanol II (engineered)
-
-
Butanoate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
butanal:NAD(P)+ oxidoreductase (CoA-acylating)
Also acts on acetaldehyde, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
116412-25-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly Clostridium thermosaccharolyticum
UniProt
Manually annotated by BRENDA team
formerly Clostridium thermosaccharolyticum
UniProt
Manually annotated by BRENDA team
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
4-hydroxybutanoyl-CoA + NADH + H+
4-hydroxybutanal + CoA + NAD+
show the reaction diagram
4-hydroxybutanoyl-CoA + NADPH + H+
4-hydroxybutanal + CoA + NADP+
show the reaction diagram
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
show the reaction diagram
butanal + CoA + NAD+
butanoyl-CoA + NADH
show the reaction diagram
butanal + CoA + NADP+
butanoyl-CoA + NADPH
show the reaction diagram
butanoyl-CoA + FADH2
butanal + CoA + FAD
show the reaction diagram
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
show the reaction diagram
butanoyl-CoA + NADPH + H+
butanal + CoA + NADP+
show the reaction diagram
hexanal + CoA + NAD+
hexanoyl-CoA + NADH
show the reaction diagram
-
-
-
-
r
propionaldehyde + NAD+
propanoyl-CoA + NADH
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
substrate chain length specificity of the enzyme is C2-C12, highest activity with C6 substrate, overview
-
-
-
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
4-hydroxybutanoyl-CoA + NADH + H+
4-hydroxybutanal + CoA + NAD+
show the reaction diagram
4-hydroxybutanoyl-CoA + NADPH + H+
4-hydroxybutanal + CoA + NADP+
show the reaction diagram
acetyl-CoA + NADH + H+
acetaldehyde + CoA + NAD+
show the reaction diagram
butanoyl-CoA + NADH + H+
butanal + CoA + NAD+
show the reaction diagram
butanoyl-CoA + NADPH + H+
butanal + CoA + NADP+
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoASH
-
at 0.3 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.2
acetaldehyde
-
-
0.055 - 0.076
acetyl-CoA
0.045 - 0.534
Butanoyl-CoA
6.7
propionaldehyde
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26
acetyl-CoA
-
recombinant enzyme, pH 7.15, 30°C
3.37
Butanoyl-CoA
-
recombinant enzyme, pH 7.15, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
acetyl-CoA
-
recombinant enzyme, pH 7.15, 30°C
6
Butanoyl-CoA
-
recombinant enzyme, pH 7.15, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.49
-
with butanoyl-CoA, pH 7.15, 30°C
0.67
pH 7.0, 55°C, substrate butanoyl-CoA
2.5
-
with butanoyl-CoA, pH 7.15, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
formation of butyryl-CoA
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
-
2 * 56000, SDS-PAGE
115000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 56000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol or dithiothreitol helps to maintain enzyme activity
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen sensitivity of CoA-acylating aldehyde dehydrogenase
-
742372
the enzyme is oxygen-tolerant
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, half-life: 3 days, enzyme in crude extract
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene bcd, the genes (crt, bcd, etfB, etfA, hbd, and thl) responsible for butyryl-CoA formation occur as a multi-gene operon, plasmid construction map for expressing individual genes of the n-butanol pathway, plasmids pHBD,pCRT,pBCD-etfAB, and pADHE, overview
gene bld, butyraldehyde dehydrogenase gene of Clostridium saccharoperbutylacetonicum is coexpresses with diverse involved genes in Escherichia coli for the reconstruction of 1,4-butanediol biosynthesis pathway in Escherichia coli, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene bldh, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis
-
gene bldh, 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
-
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 Lactobacillus brevis produces more n-butanol than ethanol
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A176T
-
random mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
A467S
-
random mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
K279R
-
random mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L273C
-
site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
L273I
-
random mutagenesis, the mutant shows about 3.5fold increased activity compared to the wild-type enzyme
L273M
-
site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
L273S
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
L273T
-
site-directed mutagenesis, the mutant shows about 4fold increased activity compared to the wild-type enzyme
L273V
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
M371R
-
random mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N409T
-
random mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
L273C
-
site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
-
L273I
-
random mutagenesis, the mutant shows about 3.5fold increased activity compared to the wild-type enzyme
-
L273M
-
site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
-
L273T
-
site-directed mutagenesis, the mutant shows about 4fold increased activity compared to the wild-type enzyme
-
additional information