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Literature summary for 2.2.1.6 extracted from

  • Loschonsky, S.; Waltzer, S.; Fraas, S.; Wacker, T.; Andrade, S.L.; Kroneck, P.M.; Mueller, M.
    Catalytic scope of the thiamine-dependent multifunctional enzyme cyclohexane-1,2-dione hydrolase (2014), ChemBioChem, 15, 389-392.
    View publication on PubMed
Search for more literature for 2.2.1.6

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) Azoarcus sp.

Organism

Organism UniProt Comment Textmining
Azoarcus sp.
-
-
-
Azoarcus sp. 22Lin
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Azoarcus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-naphthaldehyde + pyruvate
-
 Azoarcus sp. (1R)-1-hydroxy-1-(naphthalen-1-yl)propan-2-one + CO2
-
 ?
1-naphthaldehyde + pyruvate
-
 Azoarcus sp. 22Lin (1R)-1-hydroxy-1-(naphthalen-1-yl)propan-2-one + CO2
-
 ?
2-bromobenzaldehyde + pyruvate
-
 Azoarcus sp. (R)-1-hydroxy-1-(2-bromophenyl)propan-2-one + CO2
-
 ?
2-bromobenzaldehyde + pyruvate
-
 Azoarcus sp. 22Lin (R)-1-hydroxy-1-(2-bromophenyl)propan-2-one + CO2
-
 ?
2-chlorobenzaldehyde + pyruvate
-
 Azoarcus sp. (R)-1-hydroxy-1-(2-chlorophenyl)propan-2-one + CO2
-
 ?
2-chlorobenzaldehyde + pyruvate
-
 Azoarcus sp. 22Lin (R)-1-hydroxy-1-(2-chlorophenyl)propan-2-one + CO2
-
 ?
2-fluorobenzaldehyde + pyruvate
-
 Azoarcus sp. (R)-1-hydroxy-1-(2-fluorophenyl)propan-2-one + CO2
-
 ?
2-hydroxybenzaldehyde + pyruvate
-
 Azoarcus sp. (R)-1-hydroxy-1-(2-hydroxyphenyl)propan-2-one + CO2
-
 ?
2-iodobenzaldehyde + pyruvate
-
 Azoarcus sp. (R)-1-hydroxy-1-(2-iodophenyl)propan-2-one + CO2
-
 ?
2-methoxybenzaldehyde + pyruvate
-
 Azoarcus sp. (R)-1-hydroxy-1-(2-methoxyphenyl)propan-2-one + CO2
-
 ?
2-methylbenzaldehyde + pyruvate
-
 Azoarcus sp. (R)-1-hydroxy-1-(2-methylphenyl)propan-2-one + CO2
-
 ?
2-naphthaldehyde + pyruvate
-
 Azoarcus sp. (1R)-1-hydroxy-1-(naphthalen-2-yl)propan-2-one + CO2
-
 ?
2-nitrobenzaldehyde + pyruvate
-
 Azoarcus sp. (R)-1-hydroxy-1-(2-nitrophenyl)propan-2-one + CO2
-
 ?
4-(tert-butyl)benzaldehyde + pyruvate
-
 Azoarcus sp. (R)-1-hydroxy-1-(4-(tert-butyl)phenyl)propan-2-one + CO2
-
 ?
4-ethoxybenzaldehyde + pyruvate
-
 Azoarcus sp. (R)-1-hydroxy-1-(4-ethoxyphenyl)propan-2-one + CO2
-
 ?
4-ethylbenzaldehyde + pyruvate
-
 Azoarcus sp. (R)-1-hydroxy-1-(4-ethylphenyl)propan-2-one + CO2
-
 ?
4-isopropylbenzaldehyde + pyruvate
-
 Azoarcus sp. (R)-1-hydroxy-1-(4-isopropylphenyl)propan-2-one + CO2
-
 ?
4-phenylbenzaldehyde + pyruvate
-
 Azoarcus sp. (R)-1-hydroxy-1-(4-ethylphenyl)propan-2-one + CO2
-
 ?
additional information in addition to its physiological C-C bond-cleavage activity, CDH catalyzes the asymmetric cross-benzoin reaction of a broad variety of aromatic aldehydes and pyruvate. In the case of the sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde, the respective 2-hydroxyketone products are obtained in high yield. The recombinant CDH shows the same C-C bond-cleavage and C-C bond-formation activity as the enzyme purified from its native source, Azoarcus sp. strain 22Lin. Enzyme CDH catalyzes the asymmetric cross-benzoin reaction of aromatic aldehydes and (decarboxylated) pyruvate (up to quantitative conversion, 92-99% ee). The enzyme accepts also hydroxybenzaldehydes and nitrobenzaldehydes. On a semipreparative scale, sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde are transformed into the corresponding 2-hydroxy ketone products in high yields, enzyme substrate specificity and enantioselectivity, overview Azoarcus sp. ?
-
 ?
additional information in addition to its physiological C-C bond-cleavage activity, CDH catalyzes the asymmetric cross-benzoin reaction of a broad variety of aromatic aldehydes and pyruvate. In the case of the sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde, the respective 2-hydroxyketone products are obtained in high yield. The recombinant CDH shows the same C-C bond-cleavage and C-C bond-formation activity as the enzyme purified from its native source, Azoarcus sp. strain 22Lin. Enzyme CDH catalyzes the asymmetric cross-benzoin reaction of aromatic aldehydes and (decarboxylated) pyruvate (up to quantitative conversion, 92-99% ee). The enzyme accepts also hydroxybenzaldehydes and nitrobenzaldehydes. On a semipreparative scale, sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde are transformed into the corresponding 2-hydroxy ketone products in high yields, enzyme substrate specificity and enantioselectivity, overview Azoarcus sp. 22Lin ?
-
 ?
pyruvate + benzaldehyde The enzyme is able to catalyze nonphysiological asymmetric C-C bond formation, the cross-benzoin reaction of benzaldehyde and pyruvate (after decarboxylation) to result in the R-configured 1-hydroxy-1-phenylpropan-2-one (98% ee) Azoarcus sp. (R)-phenylacetylcarbinol + CO2 i.e. (R)-1-hydroxy-1-phenylpropan-2-one ?
pyruvate + benzaldehyde The enzyme is able to catalyze nonphysiological asymmetric C-C bond formation, the cross-benzoin reaction of benzaldehyde and pyruvate (after decarboxylation) to result in the R-configured 1-hydroxy-1-phenylpropan-2-one (98% ee) Azoarcus sp. 22Lin (R)-phenylacetylcarbinol + CO2 i.e. (R)-1-hydroxy-1-phenylpropan-2-one ?

Subunits

Subunits Comment Organism
homodimer the enzyme is a homodimer in solution, the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer Azoarcus sp.
homotetramer in the crystallized form Azoarcus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Azoarcus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 assay at Azoarcus sp.

Cofactor

Cofactor Comment Organism Structure
FAD noncovalently bound, one FAD per monomer Azoarcus sp.
additional information the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer Azoarcus sp.
thiamine diphosphate dependent on, one thiamine diphosphate per monomer Azoarcus sp.