Information on EC 1.1.1.75 - (R)-aminopropanol dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.1.1.75
-
RECOMMENDED NAME
GeneOntology No.
(R)-aminopropanol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-1-aminopropan-2-ol + NAD+ = aminoacetone + NADH + H+
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
aminopropanol phosphate biosynthesis II
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Glycine, serine and threonine metabolism
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aminopropanol phosphate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(R)-1-aminopropan-2-ol:NAD+ oxidoreductase
Requires K+.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-13-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
strain MAK154, gene aadh
UniProt
Manually annotated by BRENDA team
strain MAK154, gene aadh
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-diaminopropan-2-ol + NAD+
2-aminoacetamide + NADH
show the reaction diagram
1-amino-3-diethylaminopropan-2-ol + NAD+
2-amino-N,N-diethylacetamide + NADH
show the reaction diagram
-
-
-
-
?
1-aminopropan-2,3-diol + NAD+
?
show the reaction diagram
-
-
-
-
?
2-aminocyclohexanol + NADP+
2-aminocyclohexanone + NADPH + H+
show the reaction diagram
-
-
-
?
butan-2,3-diol + NAD+
?
show the reaction diagram
-
-
-
-
?
D,L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
show the reaction diagram
D,L-2-hydroxy-2-phenylethylamine + NAD+
2-amino-1-phenylethanone + NADH
show the reaction diagram
-
-
-
-
?
D,L-3-hydroxybutyrate + NAD+
?
show the reaction diagram
-
-
-
-
?
D,L-4-amino-3-hydroxybutyrate + NAD+
4-amino-3-oxobutyrate + NADH
show the reaction diagram
-
-
-
-
?
D,L-aminobutan-2-ol + NAD+
1-amino-2-oxobutane + NADH
show the reaction diagram
D,L-phenylserine + NAD+
?
show the reaction diagram
D-glucose + NADP+
? + NADPH + H+
show the reaction diagram
hydroxyacetone + NAD+
2-oxopropanal + NADH
show the reaction diagram
-
no activity with acetone
-
-
?
L-1-amino-2-butanol + NADP+
1-amino-2-butanone + NADPH + H+
show the reaction diagram
L-1-amino-2-propanol + NADP+
aminoacetone + NADPH + H+
show the reaction diagram
L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
show the reaction diagram
L-1-aminopropan-2-ol + NADP+
aminoacetone + NADPH
show the reaction diagram
propan-1,2-diol + NAD+
?
show the reaction diagram
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-
-
-
?
propan-1,3-diol + NAD+
?
show the reaction diagram
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-
-
-
?
additional information
?
-
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
L-1-amino-2-propanol + NADP+
aminoacetone + NADPH + H+
show the reaction diagram
L-1-aminopropan-2-ol + NAD+
aminoacetone + NADH
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
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required
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
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slight inhibition
Fe2+
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slightly activating
Mg2+
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slightly activating at 1.3 mM, inhibitory above 3 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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3-chloromercuribenzoate
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complete inhibition at 0.05 mM
8-hydroxyquinoline
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nearly complete inhibition at 2.5 mM
D,L-1,3-diaminopropan-2-ol
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D,L-1-bromopropan-2-ol
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D,L-1-chloropropan-2-ol
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D,L-2hydroxy-2-phenylethylamine
D,L-3-hydroxybutyrate
D,L-propan-1,2-diol
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-
D,L-serine
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D-1-amininopropan-2-ol
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EDTA
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weak inhibition at high concentration, little effect in soluble extract of disintegrated mitochondria
iodoacetate
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more inhibitory in intact cells than in cell free extracts
L-1-(3,4-dihydroxyphenyl)-2-aminoethanol
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noradrenalin
L-cysteine
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sodium carbonate/dicarbonate buffers
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at alkaline pH
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 200
1-aminopropan-2-ol
0.12 - 10
D,L-1-aminopropan-2-ol
200
D,L-4-amino-3-hydroxybutyrate
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liver homogenates
54 - 110
D-1-Aminopropan-2-ol
1.5 - 48
L-1-Aminopropan-2-ol
0.05 - 4
NAD+
0.2
NADP+
-
with D,L-1-aminopropan-2-ol as substrate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0006
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for both enantiomers of 1-aminopropan-2-ol
0.003
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under optimum conditions
0.008
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cell free extract
0.4
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crude extract
8.5
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4
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washed cell suspension
8.5
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sharp optimum
9.1
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soluble extract of disintegrated mitochondria
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8
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washed cell suspension, very low activity at 4.5, 50% activity at pH 8
6 - 10
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two peaks at pH 7 and 10 with very low activity at pH 8.5, at pH 7 50% of maximum activity
6 - 10.5
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low activity at pH 6, 80% of activity at pH 10.5
6.5 - 9
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cell free extracts, 50% activity at both pH
7.5 - 11
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very low activity at pH 7.5, 60% of activity at pH 11 in liver homogenates
8.5 - 10.5
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40% of activity in soluble extract of disintegrated mitochondria
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000 - 80000
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gel filtration
250000
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gel filtration
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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50% loss of activity after 24 h
52
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78% loss of activity within 15 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis overnight at 4°C, no loss of activity
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stable on freezing and thawing an ultrasonication
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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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-15°C stable for several days
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-15°C, 0.1 M Tris/HCl buffer, pH 7.2, 50% loss of activity
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-20°C, 0.1 M phosphate buffer, pH 7, 6 days, no loss of activity
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0-5°C significant loss in activity
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0°C, 0.1 M Tris/HCl buffer, pH 7.2, 90% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
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