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Literature summary for 1.1.1.75 extracted from

  • Turner, J.M.
    Microbial metabolism of amino ketones. L-1-aminopropan-2-ol dehydrogenase and L-threonine dehydrgenase in Escerichia coli (1967), Biochem. J., 104, 112-121.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
(R)-1-aminopropan-2-ol competitive Escherichia coli
3-chloromercuribenzoate complete inhibition at 0.05 mM Escherichia coli
8-hydroxyquinoline nearly complete inhibition at 2.5 mM Escherichia coli
D,L-1,3-diaminopropan-2-ol
-
Escherichia coli
D,L-2hydroxy-2-phenylethylamine
-
Escherichia coli
D,L-serine
-
Escherichia coli
iodoacetate more inhibitory in intact cells than in cell free extracts Escherichia coli
L-1-(3,4-dihydroxyphenyl)-2-aminoethanol noradrenalin Escherichia coli
sodium carbonate/dicarbonate buffers at alkaline pH Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
NAD+ at pH 7 with aminopropanol as substrate Escherichia coli
0.4
-
NAD+ at pH 9.6 with aminopropanol as substrate Escherichia coli
1.5
-
L-1-Aminopropan-2-ol cell free extracts Escherichia coli
10
-
D,L-1-aminopropan-2-ol cell free extracts Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-1-aminopropan-2-ol + NAD+ Escherichia coli involved in L-threonine and vitamin B12 pathway aminoacetone + NADH
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.008
-
cell free extract Escherichia coli

Storage Stability

Storage Stability Organism
-15°C stable for several days Escherichia coli
0-5°C significant loss in activity Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D,L-1-aminopropan-2-ol + NAD+ more active with L-enantiomer, activity with D-enantiomer might be due to D-aminopropanol specific enzyme Escherichia coli aminoacetone + NADH
-
?
D,L-aminobutan-2-ol + NAD+
-
Escherichia coli 1-amino-2-oxobutane + NADH
-
?
D,L-phenylserine + NAD+
-
Escherichia coli ?
-
?
L-1-aminopropan-2-ol + NAD+
-
Escherichia coli aminoacetone + NADH
-
?
L-1-aminopropan-2-ol + NAD+ involved in L-threonine and vitamin B12 pathway Escherichia coli aminoacetone + NADH
-
?
L-1-aminopropan-2-ol + NADP+
-
Escherichia coli aminoacetone + NADPH
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
cell free extract, second peak at pH 7.0-7.2 Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
6 10 two peaks at pH 7 and 10 with very low activity at pH 8.5, at pH 7 50% of maximum activity Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+ required Escherichia coli
NADP+ poor substitute for NAD+ Escherichia coli