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Literature summary for 1.4.1.28 extracted from

  • Lee, S.; Jeon, H.; Giri, P.; Lee, U.; Jung, H.; Lim, S.; Sarak, S.; Khobragade, T.; Kim, B.; Yun, H.
    The reductive amination of carbonyl compounds using native amine dehydrogenase from Laribacter hongkongensis (2021), Biotechnol. Bioprocess Eng., 26, 384-391 .
No PubMed abstract available
Search for more literature for 1.4.1.28

Application

Application Comment Organism
synthesis reductive amination of cyclohexanone (up to 100 mM) into cyclohexylamine is performed with an AmDH and formate dehydrogenase system with more than 99% conversion using Escherichia coli whole cell as well as purified enzymes. Chiral amine are produced from the corresponding ketone using inexpensive ammonium formate as sole sacrificial agent and enzymes omega-transaminase, AmDH, and formate dehydrogenase Laribacter hongkongensis
synthesis reductive amination of cyclohexanone (up to 100 mM) into cyclohexylamine using transgenic Escherichia coli as whole-cell reactors as well as purified enzymes Laribacter hongkongensis

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Laribacter hongkongensis

Crystallization (Commentary)

Crystallization (Comment) Organism
homology modeling of structure. The coordination of the amine group to E108 holds the tetrahedral carbon of the substrate bearing the amine Laribacter hongkongensis

Organism

Organism UniProt Comment Textmining
Laribacter hongkongensis
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
170
-
 substrate cyclohexanone, pH not specified in the publication, temperature not specified in the publication Laribacter hongkongensis
364
-
 substrate isovaleraldehyde, pH not specified in the publication, temperature not specified in the publication Laribacter hongkongensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-methylbutanal + NH3 + NADH + H+ 214% of the activity with cyclohexanone Laribacter hongkongensis 3-methylbutan-1-amine + H2O + NAD+
-
 ?
acetophenone + NH3 + NADH + H+
-
 Laribacter hongkongensis (S)-alpha-methylbenzylamine + H2O + NAD+
-
 ?
benzaldehyde + NH3 + NAD(P)H + H+
-
 Laribacter hongkongensis benzylamine + H2O + NAD(P)+
-
 ?
benzaldehyde + NH3 + NADH + H+ 10.4% of the activity with cyclohexanone Laribacter hongkongensis benzylamine + H2O + NAD+
-
 ?
butan-2-one + NH3 + NADH + H+ 5.5% of the activity with cyclohexanone Laribacter hongkongensis 2-butylamine + H2O + NAD+
-
 ?
cyclohexanone + NH3 + NAD(P)H + H+
-
 Laribacter hongkongensis cyclohexylamine + H2O + NAD(P)+
-
 ?
cyclohexanone + NH3 + NADH + H+
-
 Laribacter hongkongensis cyclohexylamine + H2O + NAD+
-
 ?
cyclopentanone + NH3 + NADH + H+ 3.4% of the activity with cyclohexanone Laribacter hongkongensis cyclopentylamine + H2O + NAD+
-
 ?
isovaleraldehyde + NH3 + NAD(P)H + H+
-
 Laribacter hongkongensis 3-methylbutan-1-amine + H2O + NAD(P)+
-
 ?
additional information poor substrates: linear aliphatic carbonyl compounds such as 3-heptanone, 2-pentanone as well as cyclopentanone Laribacter hongkongensis ?
-
-

Subunits

Subunits Comment Organism
? x * 36800, SDS-PAGE, recombinant protein Laribacter hongkongensis

Synonyms

Synonyms Comment Organism
AMDH
-
 Laribacter hongkongensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
 Laribacter hongkongensis

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Laribacter hongkongensis

General Information

General Information Comment Organism
metabolism in the docking analysis, cyclohexanone is well-orientated with -5.4 kcal/mol of binding energy and 3.16 A distance from the side chain of E104, key residue for interacting ammonia and substrate Laribacter hongkongensis