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Literature summary for 1.2.1.7 extracted from

  • Zahniser, M.P.D.; Prasad, S.; Kneen, M.M.; Kreinbring, C.A.; Petsko, G.A.; Ringe, D.; McLeish, M.J.
    Structure and mechanism of benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633, a member of the Class 3 aldehyde dehydrogenase superfamily (2017), Protein Eng. Des. Sel., 30, 271-278 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene mdlD, recombinant epression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Pseudomonas putida

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme in complex with NADP+ and NADP+/benzoate, sitting drop vapour diffusion method, mixing of 10 mg/ml protein in 100 mM HEPES, 100 mM KCl, 2 mM DTT, 2 mM NADP+, pH 7.5, and 1 mM benzoate (for the complex cyrstals), with crystallization solution containing 2.0 M ammonium sulfate and 5% v/v isopropanol, 5-7 days, X-ray diffraction structure determination and analysis at 2.28 A resolution Pseudomonas putida

Protein Variants

Protein Variants Comment Organism
E215D site-directed mutagenesis, the mutant shows reduced activity compared to wild-type Pseudomonas putida
E215L site-directed mutagenesis, inactive mutant Pseudomonas putida
E215Q site-directed mutagenesis, inactive mutant Pseudomonas putida
E337D site-directed mutagenesis, the mutant shows reduced activity compared to wild-type Pseudomonas putida
E337L site-directed mutagenesis, the mutant shows reduced activity compared to wild-type Pseudomonas putida
E337Q site-directed mutagenesis, the mutant shows reduced activity compared to wild-type Pseudomonas putida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
benzaldehyde + H2O + NADP+ Pseudomonas putida
-
benzoate + NADPH + 2 H+
-
?
benzaldehyde + H2O + NADP+ Pseudomonas putida ATCC 12633
-
benzoate + NADPH + 2 H+
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas putida Q84DC3
-
-
Pseudomonas putida ATCC 12633 Q84DC3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-chlorobenzaldehyde + H2O + NADP+
-
Pseudomonas putida 4-chlorobenzoate + NADPH + 2 H+
-
?
4-chlorobenzaldehyde + H2O + NADP+
-
Pseudomonas putida ATCC 12633 4-chlorobenzoate + NADPH + 2 H+
-
?
4-methoxybenzaldehyde + H2O + NADP+
-
Pseudomonas putida 4-methoxybenzoate + NADPH + 2 H+
-
?
4-methoxybenzaldehyde + H2O + NADP+
-
Pseudomonas putida ATCC 12633 4-methoxybenzoate + NADPH + 2 H+
-
?
4-nitrobenzaldehyde + H2O + NADP+
-
Pseudomonas putida 4-nitrobenzoate + NADPH + 2 H+
-
?
4-nitrobenzaldehyde + H2O + NADP+
-
Pseudomonas putida ATCC 12633 4-nitrobenzoate + NADPH + 2 H+
-
?
benzaldehyde + H2O + NADP+
-
Pseudomonas putida benzoate + NADPH + 2 H+
-
?
benzaldehyde + H2O + NADP+
-
Pseudomonas putida ATCC 12633 benzoate + NADPH + 2 H+
-
?
additional information specificity data for PpBADH shows that long chain aliphatics containing 5-8 carbons have about twice the relative rate of reactivity than benzaldehyde. As the chain length decreases, the activity declines quickly, with less than 0.1% activity being observed with acetaldehyde. Structure-function analysis Pseudomonas putida ?
-
-
additional information specificity data for PpBADH shows that long chain aliphatics containing 5-8 carbons have about twice the relative rate of reactivity than benzaldehyde. As the chain length decreases, the activity declines quickly, with less than 0.1% activity being observed with acetaldehyde. Structure-function analysis Pseudomonas putida ATCC 12633 ?
-
-

Synonyms

Synonyms Comment Organism
mdlD
-
Pseudomonas putida
More see also EC 1.2.1.28 Pseudomonas putida
NAD(P)-dependent benzaldehyde dehydrogenase
-
Pseudomonas putida
PpBADH
-
Pseudomonas putida

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
30
-
assay at Pseudomonas putida

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
additional information PpBADH is able to utilize both NAD+ and NADP+, selective mechanism, overview Pseudomonas putida
NADP+
-
Pseudomonas putida

General Information

General Information Comment Organism
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 Pseudomonas putida
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 Pseudomonas putida
additional information two conserved glutamates, at positions 215 and 337, 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 Pseudomonas putida