1.2.1.28: benzaldehyde dehydrogenase (NAD+)
This is an abbreviated version!
For detailed information about benzaldehyde dehydrogenase (NAD+), go to the full flat file.
Reaction
Synonyms
BALDH, benzaldehyde dehydrogenase, benzaldehyde dehydrogenase (NAD), BZDH, mdlD, More, NAD(P)-dependent benzaldehyde dehydrogenase, PpBADH, XylC
ECTree
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General Information
General Information on EC 1.2.1.28 - benzaldehyde dehydrogenase (NAD+)
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evolution
metabolism
physiological function
additional information
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
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
evolution
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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
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the wide substrate specificity of the enzyme enables the strain to detoxify methylnaphthalenes to naphthoic acids efficiently
metabolism
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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
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
metabolism
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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
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metabolism
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the wide substrate specificity of the enzyme enables the strain to detoxify methylnaphthalenes to naphthoic acids efficiently
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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
physiological function
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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
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