Cloned (Comment) | Organism |
---|---|
gene xylC, recombinant expression in Escherichia coli strain BL21(DE3) in inclusion bodies. Using higher concentration of lysozyme in lysis buffer, high speed, and long-term centrifugation reduces the protein aggregation | Rhodococcus ruber |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
4.2 | - |
benzaldehyde | pH 8.5, 25°C, recombinant enzyme | Rhodococcus ruber |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
benzaldehyde + H2O + NAD+ | Rhodococcus ruber | - |
benzoate + NADH + 2 H+ | - |
? | |
benzaldehyde + H2O + NAD+ | Rhodococcus ruber UKMP-5M | - |
benzoate + NADH + 2 H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus ruber | - |
isolated from oilcontaminated soils in Malaysia | - |
Rhodococcus ruber UKMP-5M | - |
isolated from oilcontaminated soils in Malaysia | - |
Purification (Comment) | Organism |
---|---|
recombinant enzyme 14fold from Escherichia coli strain BL21(DE3) by anion exchange chromatography | Rhodococcus ruber |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
purified recombinant enzyme shows highest activity of 9.4 U/ml | Rhodococcus ruber |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
benzaldehyde + H2O + NAD+ | - |
Rhodococcus ruber | benzoate + NADH + 2 H+ | - |
? | |
benzaldehyde + H2O + NAD+ | - |
Rhodococcus ruber UKMP-5M | benzoate + NADH + 2 H+ | - |
? | |
additional information | metabolite identification by gas chromatography mass spectrometry (GC-MS) | Rhodococcus ruber | ? | - |
- |
|
additional information | metabolite identification by gas chromatography mass spectrometry (GC-MS) | Rhodococcus ruber UKMP-5M | ? | - |
- |
Subunits | Comment | Organism |
---|---|---|
? | x * 27000, recombinant enzyme, SDS-PAGE | Rhodococcus ruber |
Synonyms | Comment | Organism |
---|---|---|
BZDH | - |
Rhodococcus ruber |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
recombinant enzyme | Rhodococcus ruber |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
purified recombinant enzyme, loss of 50% activity | Rhodococcus ruber |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
recombinant enzyme | Rhodococcus ruber |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | NAD+-dependent enzyme | Rhodococcus ruber |
General Information | Comment | Organism |
---|---|---|
physiological function | enzyme BZDH has the ability to degrade benzaldehyde to less toxic compounds. The BZDH is a critical enzyme for the degradation of aromatic hydrocarbons in Rhodococcus sp. The BZDH from Rhodococcus ruber strain UKMP-5M shows similar function with other aldehyde dehydrogenases | Rhodococcus ruber |