Information on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating):

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EC NUMBERCOMMENTARY
1.2.1.10-

RECOMMENDED NAMEGeneOntology No.
acetaldehyde dehydrogenase (acetylating)GO:0008774

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
show the reaction diagram
----
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
show the reaction diagram
bi-uni-uni-uni-ping-pong mechanismEscherichia coli-390164
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
show the reaction diagram
bi-uni-uni-uni-ping-pong mechanismClostridium beijerinckii-390174
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+
show the reaction diagram
bi-uni-uni-uni-ping-pong mechanismClostridium kluyveri-390176
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 activityPseudomonas sp.-657161

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
oxidation----
oxidationAcinetobacter sp. HBS-2A5JT11-695594
redox reaction----
reduction----

PATHWAYKEGG LinkMetaCyc Link
2-aminoethylphosphonate degradation I-PHOSPHONOTASE-PWY
2-oxopentenoate degradation-PWY-5162
acetylene degradation-P161-PWY
ethanol degradation I-ETOH-ACETYLCOA-ANA-PWY
heterolactic fermentation-P122-PWY
mixed acid fermentation-FERMENTATION-PWY
purine deoxyribonucleosides degradation-PWY0-1297
pyrimidine deoxyribonucleosides degradation-PWY0-1298
pyruvate fermentation to ethanol I-PWY-5480
pyruvate fermentation to ethanol III-PWY-6587
threonine degradation IV-PWY-5436
triethylamine degradation-PWY-7085

SYSTEMATIC NAMEIUBMB Comments
acetaldehyde:NAD+ oxidoreductase (CoA-acetylating)Also acts, more slowly, on glycolaldehyde, propanal and butanal. In Pseudomonas species, this enzyme forms part of a bifunctional enzyme with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. It is the final enzyme in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechol, converting the acetaldehyde produced by EC 4.1.3.39 into acetyl-CoA [3]. NADP+ can replace NAD+ but the rate of reaction is much slower [3].

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenasePseudomonas sp.-bifunctional enzyme657161
ACDH----
acetaldehyde dehydrogenaseLeuconostoc mesenteroidesQ5RLY6acetaldehyde dehydrogenase from Leuconostoc mesenteroides is a bifunctional enzyme possessing alcohol dehydrogenase und acetaldehyde dehydrogenase domains672735
acetaldehyde dehydrogenaseAcinetobacter sp. HBS-2A5JT11-695594
Acetaldehyde dehydrogenase [acetylating]----
acetyl-CoA reductase----
AdhELeuconostoc mesenteroidesQ5RLY6-672735
aldehyde dehydrogenaseAcinetobacter sp. HBS-2A5JT11-695594
aldehyde dehydrogenase (acylating)----
ALDHAcinetobacter sp. HBS-2A5JT11-695594
CoA-dependent aldehyde dehydrogenase----
coenzyme A linked aldehyde dehydrogenase----
DmpFEscherichia coli--690971
NAD+/CoA-dependent aldehyde dehydrogenaseEscherichia coli--690971

CAS REGISTRY NUMBERCOMMENTARY
9028-91-5-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Acinetobacter sp. HBS-2-695594A5JT11UniProtManually annotated by BRENDA team
Clostridium beijerinckiistrain NRRL B592390174--Manually annotated by BRENDA team
Clostridium kluyveri-286052, 390168, 390170, 390176--Manually annotated by BRENDA team
Escherichia coli-390171--Manually annotated by BRENDA team
Escherichia coligrown anaerobically390163--Manually annotated by BRENDA team
Escherichia coliNCIB 8114390162--Manually annotated by BRENDA team
Escherichia colistrain B390164--Manually annotated by BRENDA team
Escherichia colistrain K-12 strain DC272390173--Manually annotated by BRENDA team
Escherichia colistrain XL2-Blue690971--Manually annotated by BRENDA team
Escherichia coli XL2-Bluestrain XL2-Blue690971--Manually annotated by BRENDA team
Giardia intestinalissrain WB390177--Manually annotated by BRENDA team
Leuconostoc mesenteroidesIFO 3426390167--Manually annotated by BRENDA team
Leuconostoc mesenteroidesstrain LMC7672735Q5RLY6SwissProtManually annotated by BRENDA team
Leuconostoc mesenteroides LMC7strain LMC7672735Q5RLY6SwissProtManually annotated by BRENDA team
Propionibacterium freudenreichii-390166--Manually annotated by BRENDA team
Pseudomonas sp.strain CF600390175, 390178, 657161--Manually annotated by BRENDA team
Pseudomonas sp.strain NCIMB9816390179--Manually annotated by BRENDA team
Pseudomonas sp. NCIMB9816strain NCIMB9816390179--Manually annotated by BRENDA team
Thermoanaerobacter ethanolicusstrain 39E286197--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. 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
Escherichia coli--390162-390162-
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Escherichia coli--390163-390163-
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Escherichia coli--390164-390164-
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Escherichia coli--390171-390171-
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Escherichia coli--390163-390163r
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Escherichia coli--390173-390173r
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Giardia intestinalis--390177-390177r
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Pseudomonas sp.--390175-390175-
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Pseudomonas sp.--657161--?
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Leuconostoc mesenteroides--390167-390167r
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri--286052-286052-
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri--390168-390168-
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri--390170-390170-
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri--390168-390168r
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Propionibacterium freudenreichii--390166-390166-
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Clostridium beijerinckii--390174-390174r
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Thermoanaerobacter ethanolicus--286197-286197r
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Leuconostoc mesenteroidesQ5RLY6-672735--?
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri-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 activity390176-390176r
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Giardia intestinalis-enzyme carries aldehyde and alcohol dehydrogenase activity390177-390177r
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Leuconostoc mesenteroides-ethanol production in aerobic glucose dissimilation390167-390167r
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Escherichia coli-during glucose fermentation390162-390162-
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Escherichia coli-during glucose fermentation390164-390164r
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri-during ethanol fermentation390170-390170-
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri-during ethanol fermentation390176-390176r
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Pseudomonas sp.-involved in degradation of toxic aromatic compounds via the intermediate catechol657161--?
acetaldehyde + CoA + NAD+acetyl-CoA + NADH + H+
show the reaction diagram
Acinetobacter sp. HBS-2A5JT11-695594--r
acetaldehyde + CoA + NAD+ + H+acetyl-CoA + NADH
show the reaction diagram
Escherichia coli--690971--?
acetyl-CoA + NADHacetaldehyde + CoA + NAD+
show the reaction diagram
Escherichia coli--390163, 390171--r
caprylaldehyde + CoA + NAD+caprylyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri--286052--?
formaldehyde + CoA + NAD+formyl-CoA + NADH
show the reaction diagram
Giardia intestinalis--390177--ir
formaldehyde + CoA + NAD+formyl-CoA + NADH
show the reaction diagram
Pseudomonas sp.--390175--?
formaldehyde + CoA + NAD+formyl-CoA + NADH + H+
show the reaction diagram
Acinetobacter sp. HBS-2A5JT11-695594--?
glutaraldehyde + CoA + NAD+glutaryl-CoA + NADH
show the reaction diagram
Propionibacterium freudenreichii--390166--?
glycolaldehyde + CoA + NAD+hydroxyacetyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri--390168--?
glycolaldehyde + CoA + NAD+hydroxyacetyl-CoA + NADH
show the reaction diagram
Propionibacterium freudenreichii-not390166---
glyoxal + CoA + NAD+glyoxyl-CoA + NADH
show the reaction diagram
Propionibacterium freudenreichii--390166--?
heptylaldehyde + CoA + NAD+heptanoyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri--286052--?
heptylaldehyde + CoA + NAD+heptanoyl-CoA + NADH
show the reaction diagram
Propionibacterium freudenreichii--390166--?
hexylaldehyde + CoA + NAD+hexanoyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri--286052--?
hexylaldehyde + CoA + NAD+hexanoyl-CoA + NADH
show the reaction diagram
Propionibacterium freudenreichii--390166--?
isobutyraldehyde + CoA + NAD+isobutyryl-CoA + NADH
show the reaction diagram
Giardia intestinalis--390177-390177r
isobutyraldehyde + CoA + NAD+isobutyryl-CoA + NADH
show the reaction diagram
Pseudomonas sp.--390175--?
isobutyraldehyde + CoA + NAD+isobutyryl-CoA + NADH
show the reaction diagram
Leuconostoc mesenteroides--390167--?
n-butyraldehyde + CoA + NAD+n-butyryl-CoA + NADH
show the reaction diagram
Escherichia coli--390171--r
n-butyraldehyde + CoA + NAD+n-butyryl-CoA + NADH
show the reaction diagram
Giardia intestinalis--390177-390177-
n-butyraldehyde + CoA + NAD+n-butyryl-CoA + NADH
show the reaction diagram
Pseudomonas sp.--390175---
n-butyraldehyde + CoA + NAD+n-butyryl-CoA + NADH
show the reaction diagram
Leuconostoc mesenteroides--390167--r
n-butyraldehyde + CoA + NAD+n-butyryl-CoA + NADH
show the reaction diagram
Clostridium kluyveri--286052, 390168--r
n-butyraldehyde + CoA + NAD+n-butyryl-CoA + NADH
show the reaction diagram
Propionibacterium freudenreichii--390166--r
n-butyraldehyde + CoA + NAD+n-butyryl-CoA + NADH
show the reaction diagram
Clostridium beijerinckii--390174--r
n-butyraldehyde + CoA + NAD+n-butyryl-CoA + NADH
show the reaction diagram
Thermoanaerobacter ethanolicus--286197-286197r
propanal + CoA + NAD+propionyl-CoA + NADH
show the reaction diagram
Escherichia coli--390171--?
propanal + CoA + NAD+propionyl-CoA + NADH
show the reaction diagram
Leuconostoc mesenteroides--390167--?
propanal + CoA + NAD+propionyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri--286052, 390168--?
propanal + CoA + NAD+propionyl-CoA + NADH
show the reaction diagram
Pseudomonas sp.-initial rate of reaction with propanal is 2.7fold slower than that with acetaldehyde390175--?
propanal + CoA + NAD+propionyl-CoA + NADH
show the reaction diagram
Giardia intestinalis-is used 63% as efficiently as acetaldehyde390177-390177r
propanal + CoA + NAD+propionyl-CoA + NADH
show the reaction diagram
Propionibacterium freudenreichii-fermentation of 1,2-propanediol390166-390166?, r
propionaldehyde + CoA + NAD+propionyl-CoA + NADH + H+
show the reaction diagram
Acinetobacter sp. HBS-2A5JT11-695594--?
valeraldehyde + CoA + NAD+valeryl-CoA + NADH
show the reaction diagram
Clostridium kluyveri--286052--?
valeraldehyde + CoA + NAD+valeryl-CoA + NADH
show the reaction diagram
Propionibacterium freudenreichii--390166--?
isobutyraldehyde + CoA + NAD+isobutyryl-CoA + NADH
show the reaction diagram
Propionibacterium freudenreichii--390166--?
additional information?-Propionibacterium freudenreichii-not: formaldehyde, octylaldehyde, benzaldehyde, D,L-glyceraldehyde, glycolaldehyde390166---
additional information?-Escherichia coli-not benzaldehyde390164, 390171---
additional information?-Leuconostoc mesenteroides-not: benzaldehyde390167---
additional information?-Clostridium kluyveri-not: formaldehyde, chloral, benzaldehyde390168---
additional information?-Escherichia coli-not: chloral, formaldehyde, D,L-glyceraldehyde390171---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)
COMMENTARY PRODUCTLITERATURE
(Product)
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Escherichia coli--390163-390163
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Escherichia coli--390171-390171
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Escherichia coli--390173-390173
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Giardia intestinalis--390177-390177
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Pseudomonas sp.--390175-390175
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri--286052-286052
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri--390168-390168
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Propionibacterium freudenreichii--390166-390166
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Clostridium beijerinckii--390174-390174
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Thermoanaerobacter ethanolicus--286197-286197
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Leuconostoc mesenteroides-ethanol production in aerobic glucose dissimilation390167-390167
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Escherichia coli-during glucose fermentation390162-390162
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Escherichia coli-during glucose fermentation390164-390164
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri-during ethanol fermentation390170-390170
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Clostridium kluyveri-during ethanol fermentation390176-390176
acetaldehyde + CoA + NAD+acetyl-CoA + NADH
show the reaction diagram
Pseudomonas sp.-involved in degradation of toxic aromatic compounds via the intermediate catechol657161--
acetaldehyde + CoA + NAD+acetyl-CoA + NADH + H+
show the reaction diagram
Acinetobacter sp. HBS-2A5JT11-695594--
formaldehyde + CoA + NAD+formyl-CoA + NADH + H+
show the reaction diagram
Acinetobacter sp. HBS-2A5JT11-695594--
propanal + CoA + NAD+propionyl-CoA + NADH
show the reaction diagram
Giardia intestinalis-is used 63% as efficiently as acetaldehyde390177-390177
propanal + CoA + NAD+propionyl-CoA + NADH
show the reaction diagram
Propionibacterium freudenreichii-fermentation of 1,2-propanediol390166-390166
propionaldehyde + CoA + NAD+propionyl-CoA + NADH + H+
show the reaction diagram
Acinetobacter sp. HBS-2A5JT11-695594--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
CoAClostridium kluyveri--286052, 390168, 390170, 390176 2D-image
CoAThermoanaerobacter ethanolicus--286197 2D-image
CoAEscherichia coli--390162, 390163, 390164, 390171, 390173 2D-image
CoAPropionibacterium freudenreichii--390166 2D-image
CoALeuconostoc mesenteroides--390167 2D-image
CoAClostridium beijerinckii--390174 2D-image
CoAPseudomonas sp.--390175, 390178, 390179 2D-image
CoAGiardia intestinalis--390177 2D-image
NAD+Clostridium kluyveri--286052, 390168, 390170, 390176 2D-image
NAD+Thermoanaerobacter ethanolicus-NADH-dependent286197 2D-image
NAD+Escherichia coli--390162, 390163, 390164, 390171, 390173 2D-image
NAD+Propionibacterium freudenreichii-no reaction with NADP+390166 2D-image
NAD+Leuconostoc mesenteroides-no reaction with NADP+390167 2D-image
NAD+Clostridium beijerinckii--390174 2D-image
NAD+Pseudomonas sp.--390175, 657161 2D-image
NAD+Giardia intestinalis-NAD+-specific; no reaction with NADP+390177 2D-image
NAD+Escherichia coli-shares a binding site with CoA. Rossmann fold can alternately bind CoA or NAD+ cofactors required for enzymatic catalysis690971 2D-image
NAD+Acinetobacter sp. HBS-2A5JT11-695594 2D-image
NADHThermoanaerobacter ethanolicus--286197 2D-image
NADHClostridium beijerinckii-shows also activity with NADPH, NADH is more effective than NADPH390174 2D-image
NADHPseudomonas sp.-rate of reaction with NADP+ is only 7% of that with NAD+390175 2D-image
CoAEscherichia coli-shares a binding site with NAD+. Rossmann fold can alternately bind CoA or NAD+ cofactors required for enzymatic catalysis690971 2D-image
additional informationClostridium kluyveri-enzyme is able to acetylate other thiols than CoA, e.g. pantetheine, 2-mercaptoethanol, dithioerythritol, glutathione, cysteamine390176-

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Fe2+Escherichia coli-3fold activation with 0.00003 mM, 5fold activation with 0.03 mM, activation only of NADH oxidation, not NAD+ reduction390163
Mn2+Acinetobacter sp. HBS-2A5JT11activity of the enzyme is elevated695594

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
acetyl-CoAClostridium kluyveri-competitive inhibitor with respect to NAD+; competitive to NAD+390176 2D-image
ADPLeuconostoc mesenteroides-1 mM 42% inhibition, competitive to NAD+390167 2D-image
ADP-riboseEscherichia coli--390164 2D-image
AgNO3Leuconostoc mesenteroides-1 mM 20% inhibition390167 2D-image
AMPEscherichia coli--390164 2D-image
AMPLeuconostoc mesenteroides-1 mM 48% inhibition, competitive to NAD+390167 2D-image
ATPLeuconostoc mesenteroides-1 mM 38% inhibition, competitive to NAD+390167 2D-image
benzaldehydeEscherichia coli--390164 2D-image
Ca2+Giardia intestinalis-5 mM causes 51% inhibition390177 2D-image
ChloroethanolEscherichia coli--390171 2D-image
CuSO4Leuconostoc mesenteroides-1 mM 49% inhibition390167 2D-image
DisulfiramGiardia intestinalis-0.01 mM causes 70% inhibition390177 2D-image
HgCl2Leuconostoc mesenteroides-1 mM 31% inhibition390167 2D-image
iodoacetamideGiardia intestinalis-1 mM causes 88-96% inhibition390177 2D-image
iodoacetatePseudomonas sp.--657161 2D-image
Mg2+Giardia intestinalis-5 mM causes 51% inhibition390177 2D-image
Na2HAsO4Leuconostoc mesenteroides-1 mM 100% inhibition, 0.1 mM 32% inhibition390167 2D-image
NAD+Clostridium beijerinckii-double competitive, NAD+/CoA ratio is kept at 1:0.24390174 2D-image
NADHClostridium kluyveri-competitive inhibitor with respect to CoA; competitive to CoA390176 2D-image
p-chloromercuribenzoateGiardia intestinalis-0.01 mM causes 88-96% inhibition390177 2D-image
TrisEscherichia coli-rate of reaction falls off rapidly in Tris390173 2D-image
ValproateGiardia intestinalis-50 mM causes 20-46% inhibition390177 2D-image
Mn2+Giardia intestinalis-5 mM causes 84% inhibition390177 2D-image
additional informationLeuconostoc mesenteroides-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+, NADPH390167-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2-mercaptoethanolEscherichia coli-reduces lag phase before attainment of steady state rate in conjunction with NAD+390164 2D-image
2-mercaptoethanolPropionibacterium freudenreichii--390166 2D-image
3-pyridinecarboxaldehyde adenine dinucleotideEscherichia coli-NAD+ analogue, activates by binding strongly to activator site, binds weakly to catalytic site390164 2D-image
dithiothreitolEscherichia coli-does require dithiothreitol for optimum activity390173 2D-image
GSHLeuconostoc mesenteroides-7fold activation390167 2D-image
NAD+Escherichia coli-reduces lag phase before attainment of steady state rate in conjunction with 2-mercaptoethanol390164 2D-image
Sulfhydryl compoundPropionibacterium freudenreichii-requirement for reduced form390166 2D-image
Sulfhydryl compoundEscherichia coli-requirement for reduced form390171 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
22-2-mercaptoethanolClostridium kluyveri--390176 2D-image
0.01518-acetaldehydeAcinetobacter sp. HBS-2A5JT11-695594 2D-image
0.362-acetaldehydeGiardia intestinalis--390177 2D-image
0.39-acetaldehydeClostridium kluyveri--390176 2D-image
0.45-acetaldehydeClostridium kluyveri--286052 2D-image
1.3-acetaldehydeThermoanaerobacter ethanolicus--286197 2D-image
1.5-acetaldehydeClostridium kluyveri--390168 2D-image
1.5-acetaldehydeEscherichia coli--390171 2D-image
3.7-acetaldehydeLeuconostoc mesenteroides--390167 2D-image
10-acetaldehydeEscherichia coli--390164 2D-image
100-acetaldehydePropionibacterium freudenreichii--390166 2D-image
0.007-acetyl-CoAEscherichia coli--390164 2D-image
0.013-acetyl-CoAEscherichia coli--390171 2D-image
0.018-acetyl-CoAGiardia intestinalis--390177 2D-image
0.0196-acetyl-CoAClostridium beijerinckii-forward reaction, with NADPH390174 2D-image
0.037-acetyl-CoAThermoanaerobacter ethanolicus--286197 2D-image
0.154-acetyl-CoAClostridium beijerinckii-forward reaction, with NADH390174 2D-image
2.3-ButanalThermoanaerobacter ethanolicus--286197 2D-image
11-ButanalClostridium kluyveri--390168 2D-image
3.7-ButyraldehydeClostridium beijerinckii-reverse reaction, with 0.32 mM NAD+ and 0.12 mM CoA390174 2D-image
0.008-CoAEscherichia coli--390164 2D-image
0.009-CoALeuconostoc mesenteroides--390167 2D-image
0.01-CoAEscherichia coli--390171 2D-image
0.033-CoAClostridium kluyveri--286052 2D-image
0.035-CoAClostridium kluyveri--390176 2D-image
0.04-CoAPropionibacterium freudenreichii--390166 2D-image
0.064-CoAClostridium beijerinckii-reverse reaction, with 0.32 mM NAD+ and 11 mM butyraldehyde390174 2D-image
0.076-CoAGiardia intestinalis--390177 2D-image
0.16-CoAThermoanaerobacter ethanolicus--286197 2D-image
0.00212-formaldehydeAcinetobacter sp. HBS-2A5JT11-695594 2D-image
20-glycolaldehydeClostridium kluyveri--390168 2D-image
0.029-n-Butyryl-CoAThermoanaerobacter ethanolicus--286197 2D-image
0.0715-n-Butyryl-CoAClostridium beijerinckii-forward reaction, with NADPH390174 2D-image
0.166-n-Butyryl-CoAClostridium beijerinckii-forward reaction, with NADH390174 2D-image
0.05-NAD+Escherichia coli--390171 2D-image
0.08-NAD+Escherichia coli--390164 2D-image
0.17-NAD+Leuconostoc mesenteroides--390167 2D-image
0.25-NAD+Clostridium beijerinckii-reverse reaction, with 0.12 mM CoA and 11 mM butyraldehyde390174 2D-image
0.3-NAD+Clostridium kluyveri--390176 2D-image
0.4-NAD+Clostridium kluyveri--286052 2D-image
0.43-NAD+Propionibacterium freudenreichii--390166 2D-image
0.44-NAD+Thermoanaerobacter ethanolicus--286197 2D-image
0.0076-NADHClostridium beijerinckii-forward reaction, with butyryl-CoA390174 2D-image
0.0082-NADHClostridium beijerinckii-forward reaction, with acetyl-CoA390174 2D-image
0.022-NADHGiardia intestinalis--390177 2D-image
0.025-NADHEscherichia coli--390164 2D-image
0.063-NADHThermoanaerobacter ethanolicus--286197 2D-image
0.1-NADHEscherichia coli--390171 2D-image
0.0673-NADPHClostridium beijerinckii-forward reaction, with butyryl-CoA390174 2D-image
0.206-NADPHClostridium beijerinckii-forward reaction, with acetyl-CoA390174 2D-image
11-pantetheineClostridium kluyveri--390176 2D-image
0.603-propanalGiardia intestinalis--390177 2D-image
4.5-propanalClostridium kluyveri--390168 2D-image
6.9-propanalPropionibacterium freudenreichii--390166 2D-image
0.00049-propionaldehydeAcinetobacter sp. HBS-2A5JT11-695594 2D-image
1.5-ValeraldehydePropionibacterium freudenreichii--390166 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2.5-ADPLeuconostoc mesenteroides--390167 2D-image
0.75-AMPLeuconostoc mesenteroides--390167 2D-image
8.6-ATPLeuconostoc mesenteroides--390167 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.87-Leuconostoc mesenteroides--390167
1.6-Leuconostoc mesenteroidesQ5RLY6crude 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 min672735
1.7-Leuconostoc mesenteroidesQ5RLY6crude 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 min672735
2-Clostridium beijerinckii--390174
3.11-Escherichia coli--390171
4.88-Clostridium beijerinckii-undialyzed, anaerobically purified390174
8.75-Giardia intestinalis-bifunctional fusion protein of aldehyde and alcohol dehydrogenase390177
9.62-Clostridium beijerinckii-dialyzed, incubated with dithiothreitol and CoA390174
14.1-Escherichia coli--390164
16-Thermoanaerobacter ethanolicus--286197
48.6-Clostridium kluyveri--390176
60.6-Acinetobacter sp. HBS-2A5JT11recombinant enzyme695594
83.7-Propionibacterium freudenreichii--390166

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
6.8-Clostridium kluyveri-NADH oxidation; NADH oxidation, with potassium phosphate buffer390176
7-Thermoanaerobacter ethanolicus-thioesterase activity286197
7-Escherichia coli--390171
7-Clostridium beijerinckii--390174
8-Leuconostoc mesenteroides--390167
8.5-Thermoanaerobacter ethanolicus-NAD+ reduction286197
8.5-Giardia intestinalis-NAD+ reduction390177
8.8-Escherichia coli-in cyclohexylaminoethanesulfonic acid or Tris-(hydroxymethyl)-methyl-amino-propanesulfonic acid buffer390173
9-Clostridium kluyveri-NAD+ reduction286052
9.1-Clostridium kluyveri-NAD+ reduction390176

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
58Clostridium kluyveri-less than 50% of maximal activity above and below390176
67Clostridium beijerinckii-NAD+ reduction390174
6.27.4Escherichia coli-67% of maximal activity at pH 6.2, 79% of maximal activity at pH 7.4390171
6.58.5Pseudomonas sp.-activity increases gradually over pH range from 6.5 to 8.5390175
6.59.5Clostridium beijerinckii-activity of NADH oxidation increases between 6.5-9.5390174
79.5Propionibacterium freudenreichii-30% of maximal activity at pH 7.0, 100% at pH 9.5390166
8.29.5Propionibacterium freudenreichii--390166
8.510Clostridium kluyveri-70% of maximal activity at pH 8.5, 80% of maximal activity at pH 10286052

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
30-Leuconostoc mesenteroides--390167
45-Propionibacterium freudenreichii--390166

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
2060Propionibacterium freudenreichii-55% of maximal activity at 20°C, 60% at 60°C390166

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
cell cultureLeuconostoc mesenteroidesQ5RLY6-672735Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
cytosolClostridium kluyveri-soluble fraction5829390176Manually annotated by BRENDA team
cytosolGiardia intestinalis--5829390177Manually annotated by BRENDA team
particle-boundClostridium kluyveri---286052, 390170Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
1nvm, downloadSCOP (1nvm)CATH (1nvm)Pseudomonas sp. (strain CF600)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
57000-Acinetobacter sp. HBS-2A5JT11SDS-PAGE695594
96600-Leuconostoc mesenteroidesQ5RLY6deduced from sequence672735
100000-Clostridium beijerinckii-gel filtration under anaerobic conditions390174
120000-Escherichia coli-one of four isozymes, gel filtration390162
140000-Pseudomonas sp.--657161
148000-Pseudomonas sp.-gel filtration, molecular mass of enzyme complex, occurs in complex with 4-hydroxy-2-ketovalerate390175
188000-Propionibacterium freudenreichii-gel filtration390166
290000-Clostridium kluyveri-gel filtration and sedimentation coefficient390176
360000-Thermoanaerobacter ethanolicus-gel filtration286197
370000-Escherichia coli-one of four isozymes, gel filtration390162
520000-Escherichia coli-one of four isozymes, gel filtration390162
900000-Escherichia coli-one of four isozymes, gel filtration390162

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Giardia intestinalis-x * 95000, SDS-PAGE, amino acid sequence390177
?Acinetobacter sp. HBS-2A5JT11x * 57000, SDS-PAGE695594
dimerClostridium beijerinckii-2 * 55000, SDS-PAGE390174
polymerEscherichia coli-ca. 40 * 96000, pyruvate-formate-lyase-deactivase with alcohol and aldehyde dehydrogenase activity, nucleotide sequence390163
tetramerThermoanaerobacter ethanolicus-4 * 100000, SDS-PAGE286197
tetramerPropionibacterium freudenreichii-4 * 48000, SDS-PAGE390166
tetramerPseudomonas sp.-2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate390175
tetramerPseudomonas sp.-composed of two dimers, one dimer accounts for 4-hydroxy-2-ketovalerate aldolase, subunit size 37500, and one for acylating acetaldehyde dehydrogenase, subunit size 32500657161

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Pseudomonas sp.-657161
hanging drop method, streak-seedingPseudomonas sp.-390178

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
58Clostridium kluyveri-enzyme activity falls to 50% at pH 5 and pH 8390176
7-Clostridium beijerinckii-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 buffer390174

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
40-Leuconostoc mesenteroides-15 min, 30% activity left390167
45-Leuconostoc mesenteroides-15 min, inactivation390167
70-Propionibacterium freudenreichii-3 min, inactivation above390166

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
sensitive to O2, can be protected against O2 inactivation by dithiothreitolClostridium beijerinckii-390174
with Tris acetate buffer at pH 7, less stable at higher buffer concentration between 10 and 150 mMClostridium beijerinckii-390174
dithioerythritol stabilizesClostridium kluyveri-390176
no stabilization by detergents, acetone, ethanol, NAD+, glycerol, CoA, anaerobic conditionsClostridium kluyveri-390176
extremely unstable in absence of 2-mercaptoethanolEscherichia coli-390171
labile during purification, stabilization by 2-hydroxyethyldisulfideEscherichia coli-390164
activity is highest in HEPES buffer and somewhat lower in phosphate buffer, activity in Tris buffer is about half the rate in HEPES bufferPseudomonas sp.-390175

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
5 mM dithiothreitol protects enzyme in crude extracts from O2-inactivation for at least 2 hoursClostridium beijerinckii-390174
addition of 140 mM KCl to 10 mM Tris acetate stabilizes as no activity is lost after 3 daysClostridium beijerinckii-390174
CoA and dithiothreitol restore a higher activity than one of these compounds aloneClostridium beijerinckii-390174
glycerol at 20%, vol/vol, stabilizes in 50 mM Tris acetate buffer at pH 7, as no activity is lost after 3 days at 4°C under argonClostridium beijerinckii-390174
-70°C, 10 mM Tris-HCl buffer, pH 8, 3 mM dithioerythritol, 2 weeks, 15% loss of activityClostridium kluyveri-390176
-70°C, 3 mM dithioerythritol, 85% of enzymatic activity remains after 2 weeksClostridium kluyveri-390176
-60°C, 20 mM MOPS-KOH pH 7.6, 0.1 mM EDTA, up to one yearEscherichia coli-390163
3°C, ammonium sulfate step of purification, several monthsEscherichia coli-390171
-80°C, 10 mM phosphate buffer, pH 7.5, 1 mM dithiothreitolPseudomonas sp.-390175
4°C, anaerobicallyThermoanaerobacter ethanolicus-286197

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
by affinity chromatography by means of a Ni-Sepharose columnAcinetobacter sp. HBS-2A5JT11695594
under anaerobic conditionsClostridium beijerinckii-390174
partialClostridium kluyveri-390168, 390176
from anaerobically grown cells, rod-shapedEscherichia coli-390163
on DEAE and NAD+-linked affinity columns, combined with an ammonium sulfate fractionation stepEscherichia coli-690971
partialEscherichia coli-390164, 390171
-Giardia intestinalis-390177
partialLeuconostoc mesenteroides-390167
-Propionibacterium freudenreichii-390166
-Pseudomonas sp.-390175
-Thermoanaerobacter ethanolicus-286197

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
in Escherichia coli BL21 cellsAcinetobacter sp. HBS-2A5JT11695594
Escherichia coli strain W1485Escherichia coli-390173
gene adhE, pyruvate-formate-lyase-deactivase with alcohol and acetaldehyde dehydrogenase activityEscherichia coli-390163
pT7.5-dmpFG plasmid expressed in Escherichia coli C41(DE3)Escherichia coli-690971
expression in Escherichia coli BL21 and DH5alphaLeuconostoc mesenteroidesQ5RLY6672735
-Pseudomonas sp.-390179
overexpression in Escherichia coliPseudomonas sp.-390175

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
286052Hillmer, P.; Gottschalk, G.Solubilization and partial characterization of particulate dehydrogenases from Clostridium kluyveriBiochim. Biophys. Acta33412-231974Clostridium kluyveri-
286197Burdette, D.; Zeikus, J.G.Purification of acetaldehyde dehydrogenase and alcohol dehydrogenases from Thermoanaerobacter ethanolicus 39E and characterization of the secondary-alcohol dehydrogenase (2 degrees Adh) as a bifunctional alcohol dehydrogenase-acetyl-CoA reductive thioesteraseBiochem. J.302163-1701994Thermoanaerobacter ethanolicus PubMed
390162Jones, P.W.; Turner, J.M.Interrelationships between the enzymes of ethanolamine metabolism in Escherichia coliJ. Gen. Microbiol.130299-3081984Escherichia coli PubMed
390163Kessler, D.; Leibrecht, I.; Knappe, J.Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhEFEBS Lett.28159-631991Escherichia coli PubMed
390164Shone, C.C.; Fromm, H.J.Steady-state and pre-steady-state kinetics of coenzyme A linked aldehyde dehydrogenase from Escherichia coliBiochemistry207494-75011981Escherichia coli PubMed
390166Hosoi, N.; Ozaki, C.; Kitamoto, Y.; Ichikawa, Y.Purification and properties of aldehyde dehydrogenase (acylating) from propionibacterium freudenreichiiJ. Ferment. Technol.57418-4271979Propionibacterium freudenreichii-
390167Kazahaya, T.; Kawai, K.; Yashima, S.; Sasaki, Y.Aerobic dissimilation of glucose by heterolactic bacteria. III. Aldehyde dehydrogenase and alcohol dehydrogenase of Leuconostoc mesenteroidesJ. Gen. Appl. Microbiol.1843-551972Leuconostoc mesenteroides-
390168Burton, R.M.; Stadtman, E.R.The oxidation of acetaldehyde to acetyl coenzyme AJ. Biol. Chem.202873-8901953Clostridium kluyveri-
390170Hillmer, P.; Gottschalk, G.Particulate nature of enzymes involved in the fermentation of ethanol and acetate by Clostridium kluyveriFEBS Lett.21351-3541972Clostridium kluyveri PubMed
390171Rudolph, F.B.; Purich, D.L.; Fromm, H.J.Coenzyme A-linked aldehyde dehydrogenase from Escherichia coli. I. Partial purification, properties, and kinetic studies of the enzymeJ. Biol. Chem.2435539-55451968Escherichia coli PubMed
390173Clark, D.P.; Cronan, J.E., Jr.Acetaldehyde coenzyme A dehydrogenase of Escherichia coliJ. Bacteriol.144179-1841980Escherichia coli PubMed
390174Yan, R.T.; Chen, J.S.Coenzyme A-acylating aldehyde dehydrogenase from Clostridium beijerinckii NRRL B592Appl. Environ. Microbiol.562591-25991990Clostridium beijerinckii PubMed
390175Powlowski, 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 CF600J. Bacteriol.175377-3851993Pseudomonas sp. PubMed
390176Smith, L.T.; Kaplan, N.O.Purification, properties, and kinetic mechanism of coenzyme A-linked aldehyde dehydrogenase from Clostridium kluyveriArch. Biochem. Biophys.203663-6751980Clostridium kluyveri PubMed
390177Sanchez, L.B.Aldehyde dehydrogenase (CoA-acetylating) and the mechanism of ethanol formation in the amitochondriate protist, Giardia lambliaArch. Biochem. Biophys.35457-641998Giardia intestinalis PubMed
390178Manjasetty, 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 CF600Acta Crystallogr. Sect. D57582-5852001Pseudomonas sp. PubMed
390179Platt, 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 sequencesMicrobiology141223-2331995Pseudomonas sp.-
657161Manjasetty, B.A.; Powlowski, J.; Vrielink, A.Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediateProc. Natl. Acad. Sci. USA1006992-69972003Pseudomonas sp. PubMed
672735Koo, O.K.; Jeong, D.W.; Lee, J.M.; Kim, M.J.; Lee, J.H.; Chang, H.C.; Kim, J.H.; Lee, H.J.Cloning and characterization of the bifunctional alcohol/acetaldehyde dehydrogenase gene (adhE) in Leuconostoc mesenteroides isolated from kimchiBiotechnol. Lett.27505-5102005Leuconostoc mesenteroides PubMed
690971Lei, Y.; Pawelek, P.D.; Powlowski, J.A shared binding site for NAD+ and coenzyme A in an acetaldehyde dehydrogenase involved in bacterial degradation of aromatic compoundsBiochemistry476870-68822008Escherichia coli PubMed
695594Zhao, Y.; Lei, M.; Wu, Y.; Wang, C.; Zhang, Z.; Deng, F.; Wang, H.Molecular cloning and expression of the complete DNA sequence encoding NAD+-dependent acetaldehyde dehydrogenase from Acinetobacter sp. strain HBS-2Ann. Microbiol.5997-1042009Acinetobacter sp. HBS-2-

LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.10)
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IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
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Protein Mutant Database
InterPro (database of protein families, domains and functional sites)