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Literature summary for 1.1.1.1 extracted from

  • Huang, L.; Sayoga, G.; Hollmann, F.; Kara, S.
    Horse liver alcohol dehydrogenase-catalyzed oxidative lactamization of amino alcohols (2018), ACS Catal., 8, 8680-8684 .
No PubMed abstract available
Search for more literature for 1.1.1.1

Application

Application Comment Organism
synthesis horse liver alcohol dehydrogenase (HLADH) together with the NADH oxidase from Streptococcus mutans (SmNOX) are applied for the oxidative lactamization of various amino alcohols, direct synthesis of lactams (5-, 6-, and 7-membered) starting from amino-alcohols in a bienzymatic cascade. A direct approach for biocatalytic oxidative lactamization reaction. In situ regeneration of NAD+ with SmNOX in the HLADH-catalyzed oxidative lactamization of 4-amino-1-butanol to gamma-butyrolactam. The bienzymatic reaction cascade exhibits an optimum between pH 8 and pH 10, which can be attributed to the rather narrow pH range of SmNOX compared to that of HLADH. The fast reoxidation of NADH eliminated inhibitory effects of NADH on the HLADH-catalyzed oxidation Equus caballus

Inhibitors

Inhibitors Comment Organism Structure
5-amino-1-pentanol
-
 Equus caballus
6-amino-1-hexanol
-
 Equus caballus
NADH inhibitory effects of NADH on the HLADH-catalyzed oxidation Equus caballus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.8
-
 4-amino-1-butanol pH 11.0, 25°C, recombinant enzyme Equus caballus
6.71
-
 6-amino-1-hexanol pH 9.0, 25°C, recombinant enzyme Equus caballus
17.8
-
 4-amino-1-butanol pH 9.0, 25°C, recombinant enzyme Equus caballus
26.9
-
 5-amino-1-pentanol pH 9.0, 25°C, recombinant enzyme Equus caballus
34.9
-
 4-amino-1-butanol pH 7.0, 25°C, recombinant enzyme Equus caballus

Organism

Organism UniProt Comment Textmining
Equus caballus P00327
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Equus caballus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-amino-1-butanol + NAD+ 95% conversion Equus caballus to gamma-butyrolactam + NADH + H+
-
 ?
5-amino-1-pentanol + NAD+ 38% conversion Equus caballus delta-valerolactam + NADH + H+
-
 ?
6-amino-1-hexanol + NAD+ 14% conversion Equus caballus epsilon-caprolactam + NADH + H+
-
 ?
additional information horse liver alcohol dehydrogenase together with the NADH oxidase from Streptococcus mutans are applied for the oxidative lactamization of various amino alcohols, direct synthesis of lactams (5-, 6-, and 7-membered) starting from amino-alcohols in a bienzymatic cascade. Poor activity with aromatic amino alcohols (2-(2-aminoethyl)phenyl)-methanol and (2-(aminomethyl)phenyl) methanol Equus caballus ?
-
-

Synonyms

Synonyms Comment Organism
ADH
-
 Equus caballus
hLADH
-
 Equus caballus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Equus caballus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
380
-
 4-amino-1-butanol pH 9.0, 25°C, recombinant enzyme Equus caballus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
 Equus caballus

pH Range

pH Minimum pH Maximum Comment Organism
7 11 under the analyzed conditions, the activity of HLADH steadily increases with increasing pH up to pH 9.0 and then decreases at more alkaline conditions, but highest oxidative lactimization activity at pH 11.00 in the coupled assay with NADH oxidase Equus caballus

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
9.33
-
 pH 9.0, 25°C, recombinant enzyme Equus caballus 5-amino-1-pentanol
11
-
 pH 9.0, 25°C, recombinant enzyme Equus caballus 6-amino-1-hexanol

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
21.35
-
 4-amino-1-butanol pH 9.0, 25°C, recombinant enzyme Equus caballus