Information on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
1.2.1.10
-
RECOMMENDED NAME
GeneOntology No.
acetaldehyde dehydrogenase (acetylating)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
show the reaction diagram
bi-uni-uni-uni-ping-pong mechanism
-
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
show the reaction diagram
bi-uni-uni-uni-ping-pong mechanism
-
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
show the reaction diagram
bi-uni-uni-uni-ping-pong mechanism
-
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
-
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
show the reaction diagram
bi-uni-uni-uni-ping-pong mechanism
Clostridium beijerinckii NRRL B592
-
-
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
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2'-deoxy-alpha-D-ribose 1-phosphate degradation
-
-
2-aminoethylphosphonate degradation I
-
-
2-oxopentenoate degradation
-
-
3-phenylpropionate degradation
-
-
acetylene degradation
-
-
Benzoate degradation
-
-
Butanoate metabolism
-
-
Dioxin degradation
-
-
ethanol degradation I
-
-
ethanol fermentation
-
-
heterolactic fermentation
-
-
L-threonine degradation IV
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
mixed acid fermentation
-
-
Phenylalanine metabolism
-
-
pyruvate fermentation to ethanol I
-
-
pyruvate fermentation to ethanol III
-
-
Pyruvate metabolism
-
-
superpathway of fermentation (Chlamydomonas reinhardtii)
-
-
threonine metabolism
-
-
triethylamine degradation
-
-
Xylene degradation
-
-
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].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ACDH
-
-
-
-
Acetaldehyde dehydrogenase [acetylating]
-
-
-
-
acetyl-CoA reductase
-
-
-
-
aldehyde dehydrogenase (acylating)
-
-
-
-
CoA-dependent aldehyde dehydrogenase
-
-
-
-
coenzyme A linked aldehyde dehydrogenase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-91-5
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain NRRL B592
-
-
Manually annotated by BRENDA team
Clostridium beijerinckii NRRL B592
strain NRRL B592
-
-
Manually annotated by BRENDA team
grown anaerobically
-
-
Manually annotated by BRENDA team
NCIB 8114
-
-
Manually annotated by BRENDA team
strain B
-
-
Manually annotated by BRENDA team
strain K-12 strain DC272
-
-
Manually annotated by BRENDA team
strain XL2-Blue
-
-
Manually annotated by BRENDA team
Escherichia coli XL2-Blue
strain XL2-Blue
-
-
Manually annotated by BRENDA team
Giardia intestinalis WB
srain WB
-
-
Manually annotated by BRENDA team
strain LMC7
SwissProt
Manually annotated by BRENDA team
Leuconostoc mesenteroides LMC7
strain LMC7
SwissProt
Manually annotated by BRENDA team
dmpF
SwissProt
Manually annotated by BRENDA team
strain NCIMB9816
-
-
Manually annotated by BRENDA team
Pseudomonas sp. NCIMB9816
strain NCIMB9816
-
-
Manually annotated by BRENDA team
Thermoanaerobacter ethanolicus 39E
strain 39E
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
Q52060
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
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
Q5RLY6
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
0.1 mM CoA can be replaced by 25 mM pantetheine, 46% of CoA activity, 25 mM 2-mercaptoethanol, 14% of CoA activity, 25 mM dithioerythritol, 10% of CoA activity, 25 mM glutathione, 8.6% of CoA activity, 25 mM cysteamine, 4.6% of CoA activity
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
enzyme carries aldehyde and alcohol dehydrogenase activity
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
ethanol production in aerobic glucose dissimilation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
during glucose fermentation
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
during glucose fermentation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
during ethanol fermentation
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
during ethanol fermentation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
involved in degradation of toxic aromatic compounds via the intermediate catechol
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
Giardia intestinalis WB
-
enzyme carries aldehyde and alcohol dehydrogenase activity
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
Clostridium beijerinckii NRRL B592
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
Leuconostoc mesenteroides LMC7
Q5RLY6
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
involved in degradation of toxic aromatic compounds via the intermediate catechol
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
show the reaction diagram
A5JT11
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
show the reaction diagram
Q79AF6
-
-
-
?, r
acetaldehyde + CoA + NAD+ + H+
acetyl-CoA + NADH
show the reaction diagram
Escherichia coli, Escherichia coli XL2-Blue
-
-
-
-
?
acetyl-CoA + NADH
acetaldehyde + CoA + NAD+
show the reaction diagram
-
-
-
-
r
butyraldehyde + CoA + NAD+
butyryl-CoA + NADH + H+
show the reaction diagram
Q79AF6
-
-
-
r
caprylaldehyde + CoA + NAD+
caprylyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
formaldehyde + CoA + NAD+
formyl-CoA + NADH
show the reaction diagram
-
-
-
-
ir
formaldehyde + CoA + NAD+
formyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
formaldehyde + CoA + NAD+
formyl-CoA + NADH + H+
show the reaction diagram
A5JT11
-
-
-
?
glutaraldehyde + CoA + NAD+
glutaryl-CoA + NADH
show the reaction diagram
-
-
-
-
?
glycolaldehyde + CoA + NAD+
hydroxyacetyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
glyoxal + CoA + NAD+
glyoxyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
heptylaldehyde + CoA + NAD+
heptanoyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
heptylaldehyde + CoA + NAD+
heptanoyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
hexylaldehyde + CoA + NAD+
hexanoyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
hexylaldehyde + CoA + NAD+
hexanoyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
show the reaction diagram
-
-
-
r
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
show the reaction diagram
-
-
-
-
?
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
show the reaction diagram
-
-
-
-
?
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
show the reaction diagram
-
-
-
-
?
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
show the reaction diagram
Giardia intestinalis WB
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
show the reaction diagram
-
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
show the reaction diagram
-
-
-
-
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
show the reaction diagram
-
-
-
-
-
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
show the reaction diagram
-
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
show the reaction diagram
-
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
show the reaction diagram
-
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
show the reaction diagram
-
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
show the reaction diagram
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
show the reaction diagram
Giardia intestinalis WB
-
-
-
-
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
show the reaction diagram
Clostridium beijerinckii NRRL B592
-
-
-
-
r
n-butyraldehyde + CoA + NAD+
n-butyryl-CoA + NADH
show the reaction diagram
-
-
-
-
-
pentaldehyde + CoA + NAD+
pentyl-CoA + NADH + H+
show the reaction diagram
Q79AF6
-
-
-
r
picolinaldehyde + CoA + NAD+
picolinyl-CoA + NADH + H+
show the reaction diagram
Q79AF6
-
-
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
propanal + CoA + NAD+
propionyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
propanal + CoA + NAD+
propionyl-CoA + NADH
show the reaction diagram
-
-
-
-
?
propanal + CoA + NAD+
propionyl-CoA + NADH
show the reaction diagram
-
initial rate of reaction with propanal is 2.7fold slower than that with acetaldehyde
-
-
?
propanal + CoA + NAD+
propionyl-CoA + NADH
show the reaction diagram
-
is used 63% as efficiently as acetaldehyde
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
show the reaction diagram
-
fermentation of 1,2-propanediol
-
?, r
propanal + CoA + NAD+
propionyl-CoA + NADH
show the reaction diagram
Giardia intestinalis WB
-
is used 63% as efficiently as acetaldehyde
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
show the reaction diagram
-
initial rate of reaction with propanal is 2.7fold slower than that with acetaldehyde
-
-
?
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
show the reaction diagram
A5JT11
-
-
-
?
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
show the reaction diagram
Q79AF6
-
-
-
r
valeraldehyde + CoA + NAD+
valeryl-CoA + NADH
show the reaction diagram
-
-
-
-
?
valeraldehyde + CoA + NAD+
valeryl-CoA + NADH
show the reaction diagram
-
-
-
-
?
isobutyraldehyde + CoA + NAD+
isobutyryl-CoA + NADH
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
not: formaldehyde, octylaldehyde, benzaldehyde, D,L-glyceraldehyde, glycolaldehyde
-
-
-
additional information
?
-
-
not benzaldehyde
-
-
-
additional information
?
-
-
not: benzaldehyde
-
-
-
additional information
?
-
-
not: formaldehyde, chloral, benzaldehyde
-
-
-
additional information
?
-
-
not: chloral, formaldehyde, D,L-glyceraldehyde
-
-
-
additional information
?
-
Q79AF6
BphJ forms a heterotetrameric complex with the class II aldolase BphI that channels aldehydes produced in the aldol cleavage reaction to the dehydrogenase via a molecular tunnel
-
-
-
additional information
?
-
Q52060
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
ethanol production in aerobic glucose dissimilation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
during glucose fermentation
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
during glucose fermentation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
during ethanol fermentation
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
during ethanol fermentation
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
involved in degradation of toxic aromatic compounds via the intermediate catechol
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
show the reaction diagram
A5JT11
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH + H+
show the reaction diagram
Q79AF6
-
-
-
?
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
Giardia intestinalis WB
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
Clostridium beijerinckii NRRL B592
-
-
-
r
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
-
-
-
acetaldehyde + CoA + NAD+
acetyl-CoA + NADH
show the reaction diagram
-
involved in degradation of toxic aromatic compounds via the intermediate catechol
-
-
?
propanal + CoA + NAD+
propionyl-CoA + NADH
show the reaction diagram
-
is used 63% as efficiently as acetaldehyde
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
show the reaction diagram
-
fermentation of 1,2-propanediol
-
r
propanal + CoA + NAD+
propionyl-CoA + NADH
show the reaction diagram
Giardia intestinalis WB
-
is used 63% as efficiently as acetaldehyde
-
r
propionaldehyde + CoA + NAD+
propionyl-CoA + NADH + H+
show the reaction diagram
A5JT11
-
-
-
?
formaldehyde + CoA + NAD+
formyl-CoA + NADH + H+
show the reaction diagram
A5JT11
-
-
-
?
additional information
?
-
Q52060
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
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
NADH-dependent
NAD+
-
no reaction with NADP+
NAD+
-
no reaction with NADP+
NAD+
-
NAD+-specific; no reaction with NADP+
NAD+
-
shares a binding site with CoA. Rossmann fold can alternately bind CoA or NAD+ cofactors required for enzymatic catalysis
NADH
-
shows also activity with NADPH, NADH is more effective than NADPH
NADH
-
rate of reaction with NADP+ is only 7% of that with NAD+
CoA
-
shares a binding site with NAD+. Rossmann fold can alternately bind CoA or NAD+ cofactors required for enzymatic catalysis
additional information
-
enzyme is able to acetylate other thiols than CoA, e.g. pantetheine, 2-mercaptoethanol, dithioerythritol, glutathione, cysteamine
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
-
3fold activation with 0.00003 mM, 5fold activation with 0.03 mM, activation only of NADH oxidation, not NAD+ reduction
Mn2+
A5JT11
activity of the enzyme is elevated
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetaldehyde
-
competitive inhibition
acetyl-CoA
-
competitive inhibitor with respect to NAD+; competitive to NAD+
ADP
-
1 mM 42% inhibition, competitive to NAD+
ADP-ribose
-
-
AgNO3
-
1 mM 20% inhibition
AMP
-
1 mM 48% inhibition, competitive to NAD+
ATP
-
1 mM 38% inhibition, competitive to NAD+
benzaldehyde
-
-
Ca2+
-
5 mM causes 51% inhibition
Chloroethanol
-
-
CuSO4
-
1 mM 49% inhibition
Disulfiram
-
0.01 mM causes 70% inhibition
HgCl2
-
1 mM 31% inhibition
iodoacetamide
-
1 mM causes 88-96% inhibition
iodoacetate
-
-
Mg2+
-
5 mM causes 51% inhibition
Na2HAsO4
-
1 mM 100% inhibition, 0.1 mM 32% inhibition
NAD+
-
double competitive, NAD+/CoA ratio is kept at 1:0.24
NADH
-
competitive inhibitor with respect to CoA; competitive to CoA
p-chloromercuribenzoate
-
0.01 mM causes 88-96% inhibition
Tris
-
rate of reaction falls off rapidly in Tris
Valproate
-
50 mM causes 20-46% inhibition
Mn2+
-
5 mM causes 84% inhibition
additional information
-
low ionic strength buffers, 0.2 M boric acid/Na2CO3, 0.2 M glycine/NaOH, 0.2 M NH4Cl/NH4OH, pH 8.0, not inhibitory at 1 mM: K+, Na+, Li+, Mg2+, Mn2+, Zn2 +, Ca2+, Fe2+, Fe3+, EDTA, p-chloromercuribenzoate, iodoacetate, N3-, dipyridyl, lactic acid, acetic acid, ethanol, acetylphosphate, pyruvic acid, adenine, adenosine, guanine, guanosine, GMP, GDP, not inhibitory at 0.1 mM: NADP+, NADPH
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
reduces lag phase before attainment of steady state rate in conjunction with NAD+
3-pyridinecarboxaldehyde adenine dinucleotide
-
NAD+ analogue, activates by binding strongly to activator site, binds weakly to catalytic site
dithiothreitol
-
does require dithiothreitol for optimum activity
GSH
-
7fold activation
NAD+
-
reduces lag phase before attainment of steady state rate in conjunction with 2-mercaptoethanol
sulfhydryl compound
-
requirement for reduced form
sulfhydryl compound
-
requirement for reduced form
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
22
2-mercaptoethanol
-
-
0.01518
acetaldehyde
A5JT11
-
0.362
acetaldehyde
-
-
0.39
acetaldehyde
-
-
0.45
acetaldehyde
-
-
1.3
acetaldehyde
-
-
1.5
acetaldehyde
-
-
1.5
acetaldehyde
-
-
3.7
acetaldehyde
-
-
10
acetaldehyde
-
-
17
acetaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
18.7
acetaldehyde
Q79AF6
mutant enzyme D208A, at 25C in 100 mM HEPES buffer (pH 8.0)
23.6
acetaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
34.9
acetaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
38
acetaldehyde
-
at 25C in 50 mM Tris/HCl buffer, pH 8.0
45.6
acetaldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
133
acetaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
0.007
acetyl-CoA
-
-
0.013
acetyl-CoA
-
-
0.018
acetyl-CoA
-
-
0.0196
acetyl-CoA
-
forward reaction, with NADPH
0.037
acetyl-CoA
-
-
0.154
acetyl-CoA
-
forward reaction, with NADH
11
Butanal
-
-
3.7
Butyraldehyde
-
reverse reaction, with 0.32 mM NAD+ and 0.12 mM CoA
4.6
Butyraldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
12.6
Butyraldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
19.3
Butyraldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
31.7
Butyraldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
0.008
CoA
-
-
0.01
CoA
-
-
0.064
CoA
-
reverse reaction, with 0.32 mM NAD+ and 11 mM butyraldehyde
0.09
CoA
-
at 25C in 50 mM Tris/HCl buffer, pH 8.0
0.00212
formaldehyde
A5JT11
-
20
glycolaldehyde
-
-
0.029
n-Butyryl-CoA
-
-
0.0715
n-Butyryl-CoA
-
forward reaction, with NADPH
0.166
n-Butyryl-CoA
-
forward reaction, with NADH
0.05
NAD+
-
-
0.08
NAD+
-
-
0.25
NAD+
-
reverse reaction, with 0.12 mM CoA and 11 mM butyraldehyde
0.25
NAD+
-
at 25C in 50 mM Tris/HCl buffer, pH 8.0
0.0076
NADH
-
forward reaction, with butyryl-CoA
0.0082
NADH
-
forward reaction, with acetyl-CoA
0.022
NADH
-
-
0.025
NADH
-
-
0.1
NADH
-
-
0.0673
NADPH
-
forward reaction, with butyryl-CoA
0.206
NADPH
-
forward reaction, with acetyl-CoA
11
pantetheine
-
-
8.2
pentaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
3.2
picolinaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
6.9
picolinaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
12
picolinaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
18.2
picolinaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
0.603
propanal
-
-
4.5
propanal
-
-
0.00049
propionaldehyde
A5JT11
-
20.4
propionaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
23.1
propionaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
27.2
propionaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
31.5
propionaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
79.5
propionaldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.9
acetaldehyde
Q79AF6
mutant enzyme I195W, at 25C in 100 mM HEPES buffer (pH 8.0)
7.6
acetaldehyde
Q79AF6
mutant enzyme D208A, at 25C in 100 mM HEPES buffer (pH 8.0)
7.8
acetaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
15.4
acetaldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
15.7
acetaldehyde
-
at 25C in 50 mM Tris/HCl buffer, pH 8.0
17.2
acetaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
19.7
acetaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
37.9
acetaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
7.1
Butyraldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
9.5
Butyraldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
12.6
Butyraldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
16.7
Butyraldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
13
pentaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
1.9
picolinaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
2.4
picolinaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
2.8
picolinaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
3.2
picolinaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
3.4
propionaldehyde
Q79AF6
mutant enzyme I195W, at 25C in 100 mM HEPES buffer (pH 8.0)
6
propionaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
7.6
propionaldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
12.1
propionaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
16.3
propionaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
24.9
propionaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.147
acetaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
90
0.152
acetaldehyde
Q79AF6
mutant enzyme I195W, at 25C in 100 mM HEPES buffer (pH 8.0)
90
0.223
acetaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
90
0.457
acetaldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
90
0.46
acetaldehyde
Q79AF6
mutant enzyme D208A, at 25C in 100 mM HEPES buffer (pH 8.0)
90
0.73
acetaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
90
2.224
acetaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
90
0.0433
Butyraldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
499
0.0458
Butyraldehyde
Q79AF6
mutant enzyme I195W, at 25C in 100 mM HEPES buffer (pH 8.0)
499
0.3
Butyraldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
499
0.37
Butyraldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
499
1.323
Butyraldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
499
2.763
Butyraldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
499
0.0265
pentaldehyde
Q79AF6
mutant enzyme I195W, at 25C in 100 mM HEPES buffer (pH 8.0)
3401
0.0346
pentaldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
3401
0.0728
pentaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
3401
0.076
pentaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
3401
1.584
pentaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
3401
0.00011
picolinaldehyde
Q79AF6
mutant enzyme I195W, at 25C in 100 mM HEPES buffer (pH 8.0)
7490
0.00076
picolinaldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
7490
0.0387
picolinaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
7490
0.154
picolinaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
7490
0.468
picolinaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
7490
0.597
picolinaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
7490
0.0425
propionaldehyde
Q79AF6
mutant enzyme I195W, at 25C in 100 mM HEPES buffer (pH 8.0)
273
0.167
propionaldehyde
Q79AF6
mutant enzyme I195F, at 25C in 100 mM HEPES buffer (pH 8.0)
273
0.221
propionaldehyde
Q79AF6
mutant enzyme I171F, at 25C in 100 mM HEPES buffer (pH 8.0)
273
0.384
propionaldehyde
Q79AF6
mutant enzyme I195A, at 25C in 100 mM HEPES buffer (pH 8.0)
273
0.7
propionaldehyde
Q79AF6
wild type enzyme, at 25C in 100 mM HEPES buffer (pH 8.0)
273
1.219
propionaldehyde
Q79AF6
mutant enzyme I171A, at 25C in 100 mM HEPES buffer (pH 8.0)
273
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
265
acetaldehyde
-
at 25C in 50 mM Tris/HCl buffer, pH 8.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.6
Q5RLY6
crude extracts from expression in Escherichia coli DH5alpha, one unit is defined as the amount of enzyme activity that catalysed the transformation of 1 micromol NADH per min
1.7
Q5RLY6
crude extracts from expression in Escherichia coli BL21, one unit is defined as the amount of enzyme activity that catalysed the transformation of 1 micromol NADH per min
4.88
-
undialyzed, anaerobically purified
8.75
-
bifunctional fusion protein of aldehyde and alcohol dehydrogenase
9.62
-
dialyzed, incubated with dithiothreitol and CoA
60.6
A5JT11
recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
-
NADH oxidation; NADH oxidation, with potassium phosphate buffer
7
-
thioesterase activity
8.5
-
NAD+ reduction
8.5
-
NAD+ reduction
8.8
-
in cyclohexylaminoethanesulfonic acid or Tris-(hydroxymethyl)-methyl-amino-propanesulfonic acid buffer
9
-
NAD+ reduction
9.1
-
NAD+ reduction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
less than 50% of maximal activity above and below
6 - 7
-
NAD+ reduction
6.2 - 7.4
-
67% of maximal activity at pH 6.2, 79% of maximal activity at pH 7.4
6.5 - 8.5
-
activity increases gradually over pH range from 6.5 to 8.5
6.5 - 9.5
-
activity of NADH oxidation increases between 6.5-9.5
7 - 9.5
-
30% of maximal activity at pH 7.0, 100% at pH 9.5
8.5 - 10
-
70% of maximal activity at pH 8.5, 80% of maximal activity at pH 10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
-
55% of maximal activity at 20C, 60% at 60C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Leuconostoc mesenteroides LMC7
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Giardia intestinalis WB
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Clostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35300
-
gel filtration
724721
57000
A5JT11
SDS-PAGE
695594
96600
Q5RLY6
deduced from sequence
672735
100000
-
gel filtration under anaerobic conditions
390174
120000
-
one of four isozymes, gel filtration
390162
140000
-
-
657161
148000
-
gel filtration, molecular mass of enzyme complex, occurs in complex with 4-hydroxy-2-ketovalerate
390175
188000
-
gel filtration
390166
290000
-
gel filtration and sedimentation coefficient
390176
360000
-
gel filtration
286197
370000
-
one of four isozymes, gel filtration
390162
520000
-
one of four isozymes, gel filtration
390162
900000
-
one of four isozymes, gel filtration
390162
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
A5JT11
x * 57000, SDS-PAGE
?
-
x * 95000, SDS-PAGE, amino acid sequence
?
Giardia intestinalis WB
-
x * 95000, SDS-PAGE, amino acid sequence
-
dimer
-
2 * 55000, SDS-PAGE
dimer
Clostridium beijerinckii NRRL B592
-
2 * 55000, SDS-PAGE
-
polymer
-
ca. 40 * 96000, pyruvate-formate-lyase-deactivase with alcohol and aldehyde dehydrogenase activity, nucleotide sequence
tetramer
-
4 * 100000, SDS-PAGE
tetramer
-
4 * 48000, SDS-PAGE
tetramer
-
2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate
tetramer
-
composed of two dimers, one dimer accounts for 4-hydroxy-2-ketovalerate aldolase, subunit size 37500, and one for acylating acetaldehyde dehydrogenase, subunit size 32500
tetramer
Thermoanaerobacter ethanolicus 39E
-
4 * 100000, SDS-PAGE
-
tetramer
-
2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate, composed of two dimers, one dimer accounts for 4-hydroxy-2-ketovalerate aldolase, subunit size 37500, and one for acylating acetaldehyde dehydrogenase, subunit size 32500
-
tetramer
Thermoanaerobacter ethanolicus JW200
-
4 * 100000, SDS-PAGE
-
monomer
-
1 * 33344, electrospray ionization mass spectrometry
additional information
Q52060
DmpFG is a microbial enzyme comprised of two subunits DmpG and DmpF
additional information
-
DmpFG is a microbial enzyme comprised of two subunits DmpG and DmpF
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, in the absence of cofactor or in the presence of either 5 mM NAD+ or CoA using 22% PEG 4000, 0.1 M HEPES/NaOH pH 7.5, 0.1 M sodium acetate
-
hanging drop method, streak-seeding
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
enzyme activity falls to 50% at pH 5 and pH 8
390176
7
-
more stable at pH 7 than at pH 6, 8 or 9 in either Tris acetate or potassium phosphate test buffer, at the same pH more stable in Tris acetate test buffer
390174
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
15 min, 30% activity left
390167
45
-
15 min, inactivation
390167
70
-
3 min, inactivation above
390166
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to O2, can be protected against O2 inactivation by dithiothreitol
-
with Tris acetate buffer at pH 7, less stable at higher buffer concentration between 10 and 150 mM
-
dithioerythritol stabilizes
-
no stabilization by detergents, acetone, ethanol, NAD+, glycerol, CoA, anaerobic conditions
-
extremely unstable in absence of 2-mercaptoethanol
-
labile during purification, stabilization by 2-hydroxyethyldisulfide
-
activity is highest in HEPES buffer and somewhat lower in phosphate buffer, activity in Tris buffer is about half the rate in HEPES buffer
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
5 mM dithiothreitol protects enzyme in crude extracts from O2-inactivation for at least 2 hours
-
addition of 140 mM KCl to 10 mM Tris acetate stabilizes as no activity is lost after 3 days
-
CoA and dithiothreitol restore a higher activity than one of these compounds alone
-
glycerol at 20%, vol/vol, stabilizes in 50 mM Tris acetate buffer at pH 7, as no activity is lost after 3 days at 4C under argon
-
-70C, 10 mM Tris-HCl buffer, pH 8, 3 mM dithioerythritol, 2 weeks, 15% loss of activity
-
-70C, 3 mM dithioerythritol, 85% of enzymatic activity remains after 2 weeks
-
-60C, 20 mM MOPS-KOH pH 7.6, 0.1 mM EDTA, up to one year
-
3C, ammonium sulfate step of purification, several months
-
-80C, 10 mM phosphate buffer, pH 7.5, 1 mM dithiothreitol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography by means of a Ni-Sepharose column
A5JT11
Ni-NTA column chromatography
Q79AF6
under anaerobic conditions
-
from anaerobically grown cells, rod-shaped
-
on DEAE and NAD+-linked affinity columns, combined with an ammonium sulfate fractionation step
-
Q-Sepharose column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in Escherichia coli BL21 cells
A5JT11
Escherichia coli strain W1485
-
expressed in Escherichia coli C41 (DE3) cells
-
gene adhE, pyruvate-formate-lyase-deactivase with alcohol and acetaldehyde dehydrogenase activity
-
pT7.5-dmpFG plasmid expressed in Escherichia coli C41(DE3)
-
expression in Escherichia coli BL21 and DH5alpha
Q5RLY6
overexpression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C131A
Q79AF6
inactive
C131S
Q79AF6
inactive
D208A
Q79AF6
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
I171A
Q79AF6
level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover. The mutation results in a 35% reduction in acetaldehyde channeling efficiency
I171F
Q79AF6
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
I195A
Q79AF6
the variant has a 20fold higher catalytic efficiency for butyraldehyde and pentaldehyde compared to the catalytic efficiency of the wild type toward its natural substrate acetaldehyde. The mutation results in a 35% reduction in acetaldehyde channeling efficiency
I195F
Q79AF6
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
I195W
Q79AF6
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
N170A
Q79AF6
the mutation does not substantially alter aldehyde channeling efficiencies. The level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover
N170D
Q79AF6
level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover
I159A
Q52060
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
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
-