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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus erythropolis | A1IG83 | gene aadh | - |
Rhodococcus erythropolis MAK154 | A1IG83 | gene aadh | - |
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 | Comment | Organism |
---|---|---|
AADH | - |
Rhodococcus erythropolis |
L-1-amino-2-propanol dehydrogenase | - |
Rhodococcus erythropolis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Rhodococcus erythropolis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Rhodococcus erythropolis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | dependent on | Rhodococcus erythropolis |