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Literature summary for 1.1.1.75 extracted from

  • Kataoka, M.; Ishige, T.; Urano, N.; Nakamura, Y.; Sakuradani, E.; Fukui, S.; Kita, S.; Sakamoto, K.; Shimizu, S.
    Cloning and expression of the L-1-amino-2-propanol dehydrogenase gene from Rhodococcus erythropolis, and its application to double chiral compound production (2008), Appl. Microbiol. Biotechnol., 80, 597-604.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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 Rhodococcus erythropolis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-1-amino-2-propanol + NADP+ Rhodococcus erythropolis
-
aminoacetone + NADPH + H+
-
?
L-1-amino-2-propanol + NADP+ Rhodococcus erythropolis MAK154
-
aminoacetone + NADPH + H+
-
?
additional information Rhodococcus erythropolis the enzyme catalyzes the stereospecific dehydrogenation of several aminoalcohols and also catalyzes the NADPH-dependent asymmetric reduction of (S)-1-phenyl-2-methylaminopropan-1-one to d-psi-EP ?
-
?
additional information Rhodococcus erythropolis MAK154 the enzyme catalyzes the stereospecific dehydrogenation of several aminoalcohols and also catalyzes the NADPH-dependent asymmetric reduction of (S)-1-phenyl-2-methylaminopropan-1-one to d-psi-EP ?
-
?

Organism

Organism UniProt Comment Textmining
Rhodococcus erythropolis A1IG83 gene aadh
-
Rhodococcus erythropolis MAK154 A1IG83 gene aadh
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-aminocyclohexanol + NADP+
-
Rhodococcus erythropolis 2-aminocyclohexanone + NADPH + H+
-
?
D-glucose + NADP+
-
Rhodococcus erythropolis ? + NADPH + H+
-
?
D-glucose + NADP+
-
Rhodococcus erythropolis MAK154 ? + NADPH + H+
-
?
L-1-amino-2-butanol + NADP+
-
Rhodococcus erythropolis 1-amino-2-butanone + NADPH + H+
-
?
L-1-amino-2-butanol + NADP+
-
Rhodococcus erythropolis MAK154 1-amino-2-butanone + NADPH + H+
-
?
L-1-amino-2-propanol + NADP+
-
Rhodococcus erythropolis aminoacetone + NADPH + H+
-
?
L-1-amino-2-propanol + NADP+
-
Rhodococcus erythropolis MAK154 aminoacetone + NADPH + H+
-
?
additional information the enzyme catalyzes the stereospecific dehydrogenation of several aminoalcohols and also catalyzes the NADPH-dependent asymmetric reduction of (S)-1-phenyl-2-methylaminopropan-1-one to d-psi-EP Rhodococcus erythropolis ?
-
?
additional information substrate specificity of AADH and optimization of the catalytic reaction assay method, overview Rhodococcus erythropolis ?
-
?
additional information the enzyme catalyzes the stereospecific dehydrogenation of several aminoalcohols and also catalyzes the NADPH-dependent asymmetric reduction of (S)-1-phenyl-2-methylaminopropan-1-one to d-psi-EP Rhodococcus erythropolis MAK154 ?
-
?
additional information substrate specificity of AADH and optimization of the catalytic reaction assay method, overview Rhodococcus erythropolis MAK154 ?
-
?

Synonyms

Synonyms Comment Organism
AADH
-
Rhodococcus erythropolis
L-1-amino-2-propanol dehydrogenase
-
Rhodococcus erythropolis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Rhodococcus erythropolis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Rhodococcus erythropolis

Cofactor

Cofactor Comment Organism Structure
NADP+ dependent on Rhodococcus erythropolis