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Information on EC 1.1.1.75 - (R)-aminopropanol dehydrogenase
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1.1.1.75 (R)-aminopropanol dehydrogenaseIUBMB Comments
Requires K+.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
1-aminopropan-2-ol-dehydrogenase, 1-aminopropan-2-ol-NAD+ dehydrogenase, AADH, DL-1-aminopropan-2-ol: NAD+ dehydrogenase, L(+)-1-aminopropan-2-ol-NAD/NADP oxidoreductase, L(+)-1-aminopropan-2-ol:NAD+ oxidoreductase, L-1-amino-2-propanol dehydrogenase, L-aminopropanol dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-aminopropan-2-ol-dehydrogenase
-
-
-
-
1-aminopropan-2-ol-NAD+ dehydrogenase
-
-
-
-
AADH
DL-1-aminopropan-2-ol: NAD+ dehydrogenase
-
-
-
-
L(+)-1-aminopropan-2-ol-NAD/NADP oxidoreductase
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-
-
-
L(+)-1-aminopropan-2-ol:NAD+ oxidoreductase
-
-
-
-
L-1-amino-2-propanol dehydrogenase
L-aminopropanol dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-1-aminopropan-2-ol + NAD+ = aminoacetone + NADH + H+
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(R)-1-aminopropan-2-ol:NAD+ oxidoreductase
Requires K+.
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CAS REGISTRY NUMBER
COMMENTARY
37250-13-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-amino-3-diethylaminopropan-2-ol + NAD+
2-amino-N,N-diethylacetamide + NADH
-
-
-
-
?
2-aminocyclohexanol + NADP+
2-aminocyclohexanone + NADPH + H+
-
-
-
?
D,L-2-hydroxy-2-phenylethylamine + NAD+
2-amino-1-phenylethanone + NADH
-
-
-
-
?
D,L-4-amino-3-hydroxybutyrate + NAD+
4-amino-3-oxobutyrate + NADH
-
-
-
-
?
hydroxyacetone + NAD+
2-oxopropanal + NADH
-
no activity with acetone
-
-
?
D,L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
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D-enantiomer 50% of activity with L-enantiomer
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ir
D,L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
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more active with L-enantiomer, activity with D-enantiomer might be due to D-aminopropanol specific enzyme
-
?
D,L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
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more active with L-enantiomer, activity with D-enantiomer might be due to D-aminopropanol specific enzyme
-
?
D,L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
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at high substrate concentrations both enantiomers utilized at the same rate, at low substrate concentration L-enantiomer preferred over D-enantiomer
-
?
L-1-amino-2-butanol + NADP+
1-amino-2-butanone + NADPH + H+
-
-
-
?
L-1-amino-2-butanol + NADP+
1-amino-2-butanone + NADPH + H+
-
-
-
?
L-1-amino-2-propanol + NADP+
aminoacetone + NADPH + H+
-
-
-
?
L-1-amino-2-propanol + NADP+
aminoacetone + NADPH + H+
-
-
-
?
L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
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involved in L-threonine and vitamin B12 pathway
-
?
L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
-
involved in L-threonine and vitamin B12 pathway
-
?
L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
-
no activity with D-enantiomer
-
r
L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
-
no activity with D-enantiomer
-
r
L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
-
no activity with D-enantiomer
-
r
L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
-
involved in L-threonine and vitamin B12 pathway
-
r
L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
-
possible role in carnitine metabolism
-
?
L-1-aminopropan-2-ol + NADP+
aminoacetone + NADPH
-
about the same activity as with NAD+ as cofactor
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r
L-1-aminopropan-2-ol + NADP+
aminoacetone + NADPH
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half maximum activity
-
?
additional information
?
-
the enzyme catalyzes the stereospecific dehydrogenation of several aminoalcohols and also catalyzes the NADPH-dependent asymmetric reduction of (S)-1-phenyl-2-methylaminopropan-1-one to d-psi-EP
-
-
?
additional information
?
-
substrate specificity of AADH and optimization of the catalytic reaction assay method, overview
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-
?
additional information
?
-
the enzyme catalyzes the stereospecific dehydrogenation of several aminoalcohols and also catalyzes the NADPH-dependent asymmetric reduction of (S)-1-phenyl-2-methylaminopropan-1-one to d-psi-EP
-
-
?
additional information
?
-
substrate specificity of AADH and optimization of the catalytic reaction assay method, overview
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-1-amino-2-propanol + NADP+
aminoacetone + NADPH + H+
-
-
-
?
L-1-amino-2-propanol + NADP+
aminoacetone + NADPH + H+
-
-
-
?
L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
-
involved in L-threonine and vitamin B12 pathway
-
?
L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
-
involved in L-threonine and vitamin B12 pathway
-
?
L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
-
involved in L-threonine and vitamin B12 pathway
-
r
L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
-
possible role in carnitine metabolism
-
?
additional information
?
-
the enzyme catalyzes the stereospecific dehydrogenation of several aminoalcohols and also catalyzes the NADPH-dependent asymmetric reduction of (S)-1-phenyl-2-methylaminopropan-1-one to d-psi-EP
-
-
?
additional information
?
-
the enzyme catalyzes the stereospecific dehydrogenation of several aminoalcohols and also catalyzes the NADPH-dependent asymmetric reduction of (S)-1-phenyl-2-methylaminopropan-1-one to d-psi-EP
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
weak inhibition at high concentration, little effect in soluble extract of disintegrated mitochondria
D,L-3-hydroxybutyrate
-
non-competitive, Ki: 200 mM in liver homogenates, little effect in soluble fraction from disintegrated mitochondria
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.001
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
9.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8
-
washed cell suspension, very low activity at 4.5, 50% activity at pH 8
6 - 10
-
two peaks at pH 7 and 10 with very low activity at pH 8.5, at pH 7 50% of maximum activity
7.5 - 11
-
very low activity at pH 7.5, 60% of activity at pH 11 in liver homogenates
8.5 - 10.5
-
40% of activity in soluble extract of disintegrated mitochondria
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (102 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C phosphate buffer, pH 7.2, 1 mg protein/ml, stable for more than 1 year
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aadh, DNA and amino acid sequence determination and analysis, expression in Escherichia coli JM109 leading to a 10.4fold increase in specific activity as to catalysis of the reduction of (S)-1-phenyl-2-methylaminopropan-1-one, as compared with that of Rhodococcus erythropolis strain MAK154 induced by 1-amino-2-propanol. Coexpression of aadh with glucose dehydrogenase gene gdh as cofactor regeneration enzyme, and installation of a system for sufficient production of d-psi-pseudoephedrine from racemic (S)-1-phenyl-2-methylaminopropan-1-one
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Turner, J.M.
Microbial metabolism of amino ketones. Aminoacetone formation from 1-aminopropan-2-ol by a dehydrgenase in Escerichia coli
Biochem. J.
99
427-433
1966
Escherichia coli
brenda
Turner, J.M.
Microbial metabolism of amino ketones. L-1-aminopropan-2-ol dehydrogenase and L-threonine dehydrgenase in Escerichia coli
Biochem. J.
104
112-121
1967
Escherichia coli
brenda
Cox, N.; Turner, J.M.; Willetts, A.J.
Aminopropanol dehydrogenase activity in rat-liver preparations
Biochim. Biophys. Acta
170
438-439
1968
Rattus norvegicus
brenda
Turner, J.M.; Willetts, A.J.
Amino ketone formation and aminopropanol-dehydrogenase activity in rat-liver preparations
Biochem. J.
102
511-519
1967
Rattus norvegicus
brenda
Willetts, A.J.; Turner, J.M.
Threonine metabolism in a strain of Bacillus subtilis enzymic oxidation of 1-aminopropan-2-ol and aminoacetone
Biochim. Biophys. Acta
252
98-104
1971
Bacillus subtilis
brenda
Faulkner, A.; Turner, J.M.
Microbial metabolism of amino alcohols. Aminoacetone metabolism via 1-aminopropan-2-ol in Pseudomonas sp. N.C.I.B. 8858
Biochem. J.
138
263-276
1974
Pseudomonas sp.
brenda
Pickard, M.A.; Higgins, I.J.; Turner, J.M.
Purification and properties of l-1-aminopropan-2-ol. NAD oxidoreductase from a pseudomonad grown on DL-1-aminopropan-2-ol
J. Gen. Microbiol.
54
115-126
1968
Pseudomonas sp.
brenda
Pickard, M.A.; Higgins, I.J.; Turner, J.M.
Microbial metabolism of 1-aminopropan-2-ol
J. Gen. Microbiol.
45
i-ii
1966
Pseudomonas sp.
-
brenda
Higgins, I.J.; Turner, J.M.
Microbial metabolism of aminoacetone
Biochem. J.
99
26P-27P
1966
Pseudomonas sp.
-
brenda
Higgins, I.J.; Pickard, M.A.; Turner, J.M.; Willets, A.J.
1-Aminopropan-2-ol-NAD oxidoreductases
Biochem. J.
99
27P
1966
Escherichia coli, Rattus norvegicus
-
brenda
Kataoka, M.; Ishige, T.; Urano, N.; Nakamura, Y.; Sakuradani, E.; Fukui, S.; Kita, S.; Sakamoto, K.; Shimizu, S.
Cloning and expression of the L-1-amino-2-propanol dehydrogenase gene from Rhodococcus erythropolis, and its application to double chiral compound production
Appl. Microbiol. Biotechnol.
80
597-604
2008
Rhodococcus erythropolis (A1IG83), Rhodococcus erythropolis MAK154 (A1IG83)
brenda
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