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Literature summary for 1.4.3.12 extracted from

  • Li, G.; Yao, P.; Cong, P.; Ren, J.; Wang, L.; Feng, J.; Lau, P.C.; Wu, Q.; Zhu, D.
    New recombinant cyclohexylamine oxidase variants for deracemization of secondary amines by orthogonally assaying designed mutants with structurally diverse substrates (2016), Sci. Rep., 6, 24973 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.4.3.12

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Top10 cells Microbacterium oxydans

Protein Variants

Protein Variants Comment Organism
L199F the mutant is more active than the wild type enzyme toward the primary amines Microbacterium oxydans
L199I the mutant is more active than the wild type enzyme toward the primary amines Microbacterium oxydans
L199T the mutation enhances the enzyme activity toward the secondary amines Microbacterium oxydans
M226A the mutant exhibits enhanced activity relative to the wild type enzyme for most (S)-enantiomers of primary amines and some secondary amines Microbacterium oxydans
M226I the mutant is more active than the wild type enzyme toward the primary amines Microbacterium oxydans
M226T the mutant is more active than the wild type enzyme toward the primary amines Microbacterium oxydans
T198A the mutant exhibits enhanced activity relative to the wild type enzyme for most (S)-enantiomers of primary amines and some secondary amines Microbacterium oxydans
T198F the mutation enhances the enzyme activity toward the secondary amines Microbacterium oxydans
T198F/L199S/M226F the substrate 2-methyl-1, 2, 3, 4-tetrahydroquinoline is deracemized by the triple mutant Microbacterium oxydans
T198I the mutant is more active than the wild type enzyme toward the primary amines Microbacterium oxydans
Y321A the mutation enhances the enzyme activity toward the secondary amines Microbacterium oxydans
Y321F the mutation enhances the enzyme activity toward the secondary amines Microbacterium oxydans
Y321I the mutation enhances the enzyme activity toward the secondary amines and displays an enhanced catalytic efficiency toward 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline Microbacterium oxydans
Y321I/M226T the double mutant acts on (S)-N-(prop-2-yn-1-yl)-2,3-dihydro-1H-inden-1-amine Microbacterium oxydans
Y321T the mutation enhances the enzyme activity toward the secondary amines Microbacterium oxydans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cyclohexylamine + O2 + H2O Microbacterium oxydans
-
 cyclohexanone + NH3 + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Microbacterium oxydans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(1R)-1-(4-chlorophenyl)ethan-1-amine + H2O + O2
-
 Microbacterium oxydans 1-(4-chlorophenyl)ethanone + NH3 + H2O2
-
 ?
(1R)-1-phenylethan-1-amine + H2O + O2
-
 Microbacterium oxydans 1-phenylacetaldehyde + NH3 + H2O2
-
 ?
(1S)-1-(4-chlorophenyl)ethan-1-amine + H2O + O2
-
 Microbacterium oxydans 1-(4-chlorophenyl)ethanone + NH3 + H2O2
-
 ?
(1S)-1-phenylethan-1-amine + H2O + O2
-
 Microbacterium oxydans 1-phenylacetaldehyde + NH3 + H2O2
-
 ?
(1S)-1-phenylpropan-1-amine + H2O + O2
-
 Microbacterium oxydans 1-phenylpropan-1-one + NH3 + H2O2
-
 ?
(2R)-heptan-2-amine + H2O + O2
-
 Microbacterium oxydans heptan-2-one + NH3 + H2O2
-
 ?
(2S)-heptan-2-amine + H2O + O2
-
 Microbacterium oxydans heptan-2-one + NH3 + H2O2
-
 ?
(S)-N-benzyl-1-phenylethylamine + O2 + H2O
-
 Microbacterium oxydans ?
-
 ?
cyclohexylamine + O2 + H2O
-
 Microbacterium oxydans cyclohexanone + NH3 + H2O2
-
 ?
additional information no activitiy towards (R)-N-(prop-2-yn-1-yl)-2, 3-dihydro-1H-inden-1-amine, 1-(4-methoxybenzyl)-1,2,3,4,5,6,7,8-octahydroisoquinoline, (S)-N-methyl-1-phenylethanamine, and 1-methyl-1,2,3,4-tetrahydroisoquinoline Microbacterium oxydans ?
-
 ?

Synonyms

Synonyms Comment Organism
CHAO
-
 Microbacterium oxydans