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Literature summary extracted from

  • Bains, J.; Leon, R.; Temke, K.G.; Boulanger, M.J.
    Elucidating the reaction mechanism of the benzoate oxidation pathway encoded aldehyde dehydrogenase from Burkholderia xenovorans LB400 (2011), Protein Sci., 20, 1048-1059.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.77 mutations confirmed by sequence analysis Paraburkholderia xenovorans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.77 E257Q-NADP+ mutant at 1.4 A resolution, C296A-NADP+ at 1.4 A resolution, E167A mutant at 1.6 A resolution, E496A mutant at 1.65 A resolution Paraburkholderia xenovorans

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.77 C296A same purification behavior as the native enzyme indicating that the mutation does not alter basic enzyme structure, but no catalytic activity detected consistent with a critical nucleophilic role for C296 Paraburkholderia xenovorans
1.2.1.77 E167A significant reduction in enzyme activity but not perturbing the overall structure, significant reduction in activity of 77%, likely candidate to present the catalytic water to the general base E257 that leads to deacylation and product release Paraburkholderia xenovorans
1.2.1.77 E257Q tolerated with respect to overall protein stability, but dramatic reduction in kcat value and no activity detectable, E257 serves probably as the primary general base to deprotonate the nucleophilic C296 Paraburkholderia xenovorans
1.2.1.77 E400A 91% reduction in kcat value, E400 plays an essential role in facilitating the acquisition of the hydride conformation Paraburkholderia xenovorans
1.2.1.77 E496A significant reduction in enzyme activity but not perturbing the overall structure, significant reduction in activity of 90% Paraburkholderia xenovorans
1.2.1.77 H485A dramatic reduction in enzyme solubility Paraburkholderia xenovorans
1.2.1.77 H485Q completely recalcitrant to purification, H485 may be important in stabilizing the nicotinamide amide moiety of NADP+ Paraburkholderia xenovorans
1.2.1.77 K168A significant reduction in enzyme activity but not perturbing the overall structure, significant reduction in activity of 92.5%, K168 likely serves to stabilize charges and tune pKa of the active site glutamate side-chains Paraburkholderia xenovorans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.77 cis-3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O Paraburkholderia xenovorans catalytic mechanism proposed in detail cis-3,4-dehydroadipyl-CoA + NADPH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.77 Paraburkholderia xenovorans Q13WK4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.77 by nickel affinity column and gel filtration Paraburkholderia xenovorans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.77 cis-3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O catalytic mechanism proposed in detail Paraburkholderia xenovorans cis-3,4-dehydroadipyl-CoA + NADPH + H+
-
 ?
1.2.1.77 propionaldehyde + NADP+ + H2O propionaldehyde is used as the aldehydic substrate in enzyme assay because of commercial unavailability of the native substrate Paraburkholderia xenovorans propionate + NADPH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.77 ALDH
-
 Paraburkholderia xenovorans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.77 additional information
-
 additional information no activities detectable for C296A and E257Q mutant enzymes Paraburkholderia xenovorans
1.2.1.77 5.75
-
 propionaldehyde H485A mutant enzyme, pH 7.5, temperature not specified in the publication Paraburkholderia xenovorans
1.2.1.77 12.1
-
 propionaldehyde K168A mutant enzyme, pH 7.5, temperature not specified in the publication Paraburkholderia xenovorans
1.2.1.77 14.6
-
 propionaldehyde E400A mutant enzyme, pH 7.5, temperature not specified in the publication Paraburkholderia xenovorans
1.2.1.77 16.2
-
 propionaldehyde E496A mutant enzyme, pH 7.5, temperature not specified in the publication Paraburkholderia xenovorans
1.2.1.77 36.8
-
 propionaldehyde E167A mutant enzyme, pH 7.5, temperature not specified in the publication Paraburkholderia xenovorans
1.2.1.77 162
-
 propionaldehyde wild type enzyme, pH 7.5, temperature not specified in the publication Paraburkholderia xenovorans

General Information

EC Number General Information Comment Organism
1.2.1.77 metabolism enzyme catalyzes an essential step in the metabolism of benzoate in Burkholderia xenovorans LB400 Paraburkholderia xenovorans