Cloned (Comment) | Organism |
---|---|
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Azoarcus sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Azoarcus sp. | - |
- |
- |
Azoarcus sp. 22Lin | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Azoarcus sp. |
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 | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Azoarcus sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
assay at | Azoarcus sp. |
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. |