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Literature summary 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

EC Number Inhibitors Comment Organism Structure
1.1.1.75 (R)-1-aminopropan-2-ol competitive Escherichia coli
1.1.1.75 3-chloromercuribenzoate complete inhibition at 0.05 mM Escherichia coli
1.1.1.75 8-hydroxyquinoline nearly complete inhibition at 2.5 mM Escherichia coli
1.1.1.75 D,L-1,3-diaminopropan-2-ol
-
 Escherichia coli
1.1.1.75 D,L-2hydroxy-2-phenylethylamine
-
 Escherichia coli
1.1.1.75 D,L-serine
-
 Escherichia coli
1.1.1.75 iodoacetate more inhibitory in intact cells than in cell free extracts Escherichia coli
1.1.1.75 L-1-(3,4-dihydroxyphenyl)-2-aminoethanol noradrenalin Escherichia coli
1.1.1.75 sodium carbonate/dicarbonate buffers at alkaline pH Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.75 0.05
-
 NAD+ at pH 7 with aminopropanol as substrate Escherichia coli
1.1.1.75 0.4
-
 NAD+ at pH 9.6 with aminopropanol as substrate Escherichia coli
1.1.1.75 1.5
-
 L-1-Aminopropan-2-ol cell free extracts Escherichia coli
1.1.1.75 10
-
 D,L-1-aminopropan-2-ol cell free extracts Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.75 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.75 partial Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.75 0.008
-
 cell free extract Escherichia coli

Storage Stability

EC Number Storage Stability Organism
1.1.1.75 -15°C stable for several days Escherichia coli
1.1.1.75 0-5°C significant loss in activity Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.75 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
-
 ?
1.1.1.75 D,L-aminobutan-2-ol + NAD+
-
 Escherichia coli 1-amino-2-oxobutane + NADH
-
 ?
1.1.1.75 D,L-phenylserine + NAD+
-
 Escherichia coli ?
-
 ?
1.1.1.75 L-1-aminopropan-2-ol + NAD+
-
 Escherichia coli aminoacetone + NADH
-
 ?
1.1.1.75 L-1-aminopropan-2-ol + NAD+ involved in L-threonine and vitamin B12 pathway Escherichia coli aminoacetone + NADH
-
 ?
1.1.1.75 L-1-aminopropan-2-ol + NADP+
-
 Escherichia coli aminoacetone + NADPH
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.75 10
-
 cell free extract, second peak at pH 7.0-7.2 Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.75 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

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