EC Number   |
General Information |
Reference |
|---|
   1.2.1.28 | evolution |
benzaldehyde dehydrogenase from Pseudomonas putida (PpBADH) belongs to the Class 3 aldehyde dehydrogenase (ALDH) family. The Class 3 ALDHs are unusual in that they are generally dimeric (rather than tetrameric), relatively non-specific and utilize both NAD+ and NADP+. The pattern of cofactor binding for the rat Class 3 ALDH differs from that of PpBADH and other ALDHs |
-, 763664 |
| 1.2.1.28 | metabolism |
benzaldehyde dehydrogenase (PpBADH) is the terminal enzyme in the mandelamide/mandelate pathway of Pseudomonas putida strain ATCC 12633, it catalyzes the conversion of benzaldehyde to benzoic acid with the concomitant reduction of NAD+ (EC 1.2.1.28) or NADP+ (EC 1.2.1.7) to NADH or NADPH, respectively. Benzoic acid subsequently enters the beta-oxoadipate pathway and the citric acid cycle |
-, 763664 |
| 1.2.1.28 | metabolism |
the enzyme is involved in biphenyl phytoalexin biosynthesis. Pyrus pyrifolia cell cultures respond to yeast extract treatment by accumulating benzoate-derived biphenyl phytoalexins, namely, noraucuparin and aucuparin |
757496 |
| 1.2.1.28 | metabolism |
the wide substrate specificity of the enzyme enables the strain to detoxify methylnaphthalenes to naphthoic acids efficiently |
-, 724140 |
| 1.2.1.28 | more |
two conserved glutamates, at positions 215 and 337, might act as the general base necessary to hydrolyze the thioacyl intermediate, structure-activity relationship, mechanism, overview. Glu215 is the likely candidate for PpBADH, a result more typical of the Class 1 and 2 ALDH families. Hydride transfer is not rate limiting, lending further credence to the suggestion that PpBADH is more similar to the Class 1 and 2 ALDHs than it is to other Class 3 ALDHs. Structure comparisons |
763664 |
| 1.2.1.28 | 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 |
-, 763165 |
