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Literature summary extracted from

  • Bajns J., Boulanger MJ.
    Structural and biochemical characterization of a novel aldehyde dehydrogenase encoded by the benzoate oxidation pathway in Burkholderia xenovorans LB400 (2008), J. Mol. Biol., 379, 597-608.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.5 expressed as a hexa-histidine-tagged fusion in Escherichia coli BL21 Star (DE3) Paraburkholderia xenovorans LB400
1.2.1.77 expressed in Escherichia coli BL21 Star (DE3) cells Paraburkholderia xenovorans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.5 ALDHC in complex with NADPH bound in the cofactor binding pocket and an ordered fragment of a polyethylene glycol molecule bound in the substrate tunnel, to 1.6 A resolution. Belongs to space group P1. The ALDHC monomer comprises three distinct domains, an N-terminal cofactor (NAD/P+)-binding domain, a catalytic domain, and an oligomerization domain Paraburkholderia xenovorans LB400
1.2.1.77 sitting drop vapour diffusion method, at 18°C in 29% PEG 3350K and 100 mM bis-Tris (pH 6.0), 1.6 A crystal structure of ALDHC in complex with NADPH bound in the cofactor-binding pocket and an ordered fragment of a polyethylene glycol molecule bound in the substrate tunnel Paraburkholderia xenovorans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.5 0.04
-
 NADP+
-
 Paraburkholderia xenovorans LB400
1.2.1.5 0.042
-
 Heptanal
-
 Paraburkholderia xenovorans LB400
1.2.1.5 0.3
-
 Valeraldehyde
-
 Paraburkholderia xenovorans LB400
1.2.1.5 0.501
-
 NAD+
-
 Paraburkholderia xenovorans LB400
1.2.1.5 1.21
-
 propionaldehyde
-
 Paraburkholderia xenovorans LB400
1.2.1.5 1.66
-
 Isovaleraldehyde
-
 Paraburkholderia xenovorans LB400
1.2.1.5 1.9
-
 formaldehyde
-
 Paraburkholderia xenovorans LB400
1.2.1.5 4.15
-
 benzaldehyde
-
 Paraburkholderia xenovorans LB400
1.2.1.77 0.04
-
 NADP+ in 50 mM Tris-HCl (pH 7.5), at 25°C Paraburkholderia xenovorans
1.2.1.77 0.042
-
 heptaldehyde in 50 mM Tris-HCl (pH 7.5), at 25°C Paraburkholderia xenovorans
1.2.1.77 0.3
-
 Valeraldehyde in 50 mM Tris-HCl (pH 7.5), at 25°C Paraburkholderia xenovorans
1.2.1.77 0.501
-
 NAD+ in 50 mM Tris-HCl (pH 7.5), at 25°C Paraburkholderia xenovorans
1.2.1.77 1.21
-
 propionaldehyde in 50 mM Tris-HCl (pH 7.5), at 25°C Paraburkholderia xenovorans
1.2.1.77 1.66
-
 Isovaleraldehyde in 50 mM Tris-HCl (pH 7.5), at 25°C Paraburkholderia xenovorans
1.2.1.77 1.9
-
 formaldehyde in 50 mM Tris-HCl (pH 7.5), at 25°C Paraburkholderia xenovorans
1.2.1.77 4.15
-
 benzaldehyde in 50 mM Tris-HCl (pH 7.5), at 25°C Paraburkholderia xenovorans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.5 110000
-
 gel filtration Paraburkholderia xenovorans LB400

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.77 3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O Paraburkholderia xenovorans the enzyme is involved in the benzoate oxidation (box) pathway 3,4-dehydroadipyl-CoA + NADPH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.5 Paraburkholderia xenovorans Q13WK4
-
-
1.2.1.5 Paraburkholderia xenovorans LB400 Q13WK4
-
-
1.2.1.77 Paraburkholderia xenovorans Q13WK4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.5 to homogeneity by nickel affinity chromatography and gel filtration Paraburkholderia xenovorans LB400
1.2.1.77
-
 Paraburkholderia xenovorans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.5 benzaldehyde + NADP+ + H2O
-
 Paraburkholderia xenovorans LB400 benzoate + NADPH + H+
-
 ?
1.2.1.5 formaldehyde + NADP+ + H2O
-
 Paraburkholderia xenovorans LB400 formate + NADPH + H+
-
 ?
1.2.1.5 heptanal + NADP+ + H2O
-
 Paraburkholderia xenovorans LB400 heptanoate + NADPH + H+
-
 ?
1.2.1.5 isovaleraldehyde + NADP+ + H2O
-
 Paraburkholderia xenovorans LB400 isovalerate + NADPH + H+
-
 ?
1.2.1.5 additional information ALDHC is preferentially active towards linear medium-chain to long-chain aldehydes as compared to branched-chain, short-chain or aromatic aldehydes. Reorientation of an extended loop (Asn478-Pro490) is responsible for the constricted structure of the substrate tunnel, with the side chain of Asn478 imposing steric restrictions on branched-chain and aromatic aldehydes. A key glycine (Gly104) positioned at the mouth of the tunnel allows for maximum tunnel depth required to bind the linear medium to long aliphatic chain of the native substrate Paraburkholderia xenovorans LB400 ?
-
 ?
1.2.1.5 propionaldehyde + NAD+ + H2O
-
 Paraburkholderia xenovorans LB400 propionate + NADH + H+
-
 r
1.2.1.5 propionaldehyde + NAD+ + H2O
-
 Paraburkholderia xenovorans propionate + NADH + H+
-
 ?
1.2.1.5 propionaldehyde + NADP+ + H2O
-
 Paraburkholderia xenovorans LB400 propionate + NADPH + H+
-
 ?
1.2.1.5 valeraldehyde + NADP+ + H2O
-
 Paraburkholderia xenovorans LB400 valerate + NADPH + H+
-
 ?
1.2.1.77 3,4-dehydroadipyl-CoA semialdehyde + NADP+ + H2O the enzyme is involved in the benzoate oxidation (box) pathway Paraburkholderia xenovorans 3,4-dehydroadipyl-CoA + NADPH + H+
-
 ?
1.2.1.77 3,4-didehydroadipyl-CoA semialdehyde + NAD+ + H2O
-
 Paraburkholderia xenovorans 3,4-didehydroadipyl-CoA + NADH + H+
-
 r
1.2.1.77 benzaldehyde + NADP+ + H2O
-
 Paraburkholderia xenovorans benzoate + NADPH + H+
-
 ?
1.2.1.77 formaldehyde + NADP+ + H2O
-
 Paraburkholderia xenovorans formate + NADPH + H+
-
 ?
1.2.1.77 heptaldehyde + NADP+ + H2O
-
 Paraburkholderia xenovorans heptanoate + NADPH + H+
-
 ?
1.2.1.77 isovaleraldehyde + NADP+ + H2O
-
 Paraburkholderia xenovorans isovalerate + NADPH + H+
-
 ?
1.2.1.77 additional information the native substrate (3,4-dehydroadipyl-CoA semialdehyde) is not tested as it is commercially unavailable. The enzyme is preferentially active towards linear medium-chain to long-chain aldehydes as compared to branched-chain, short-chain or aromatic aldehydes Paraburkholderia xenovorans ?
-
 ?
1.2.1.77 propionaldehyde + NADP+ + H2O
-
 Paraburkholderia xenovorans propionate + NADPH + H+
-
 ?
1.2.1.77 valeraldehyde + NADP+ + H2O
-
 Paraburkholderia xenovorans valerate + NADPH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.5 dimer gel filtration Paraburkholderia xenovorans LB400
1.2.1.77 ? forms a dimer in solution with a molecular mass of 110000, SDS-PAGE Paraburkholderia xenovorans

Synonyms

EC Number Synonyms Comment Organism
1.2.1.5 aldehyde dehydrogenase
-
 Paraburkholderia xenovorans LB400
1.2.1.5 ALDHC
-
 Paraburkholderia xenovorans LB400
1.2.1.5 chromosomally encoded box pathway ALDH
-
 Paraburkholderia xenovorans LB400
1.2.1.77 ALDHC
-
 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 0.019
-
 benzaldehyde in 50 mM Tris-HCl (pH 7.5), at 25°C Paraburkholderia xenovorans
1.2.1.77 0.04
-
 NADP+ in 50 mM Tris-HCl (pH 7.5), at 25°C, cosubstrate: propionaldehyde Paraburkholderia xenovorans
1.2.1.77 0.046
-
 formaldehyde in 50 mM Tris-HCl (pH 7.5), at 25°C Paraburkholderia xenovorans
1.2.1.77 0.074
-
 Isovaleraldehyde in 50 mM Tris-HCl (pH 7.5), at 25°C Paraburkholderia xenovorans
1.2.1.77 0.501
-
 NAD+ in 50 mM Tris-HCl (pH 7.5), at 25°C, cosubstrate: propionaldehyde Paraburkholderia xenovorans
1.2.1.77 2.32
-
 propionaldehyde in 50 mM Tris-HCl (pH 7.5), at 25°C Paraburkholderia xenovorans
1.2.1.77 5.16
-
 Valeraldehyde in 50 mM Tris-HCl (pH 7.5), at 25°C Paraburkholderia xenovorans
1.2.1.77 29.9
-
 heptaldehyde in 50 mM Tris-HCl (pH 7.5), at 25°C Paraburkholderia xenovorans

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.5 NAD+
-
 Paraburkholderia xenovorans LB400
1.2.1.5 NADP+ significant preference for NADP+. Cofactor selectivity is governed by a complex network of hydrogen bonds between the oxygen atoms of the 2'-phosphoryl moiety of NADP+ and a threonine/lysine pair on ALDHC Paraburkholderia xenovorans LB400
1.2.1.77 NAD+ the enzyme is more active in the presence of NADP+ relative to NAD+. Crystallographic data show that cofactor selectivity is governed by a complex network of hydrogen bonds between the oxygen atoms of the 2'-phosphoryl moiety of NADP+ and a threonine/lysine pair on the enzyme Paraburkholderia xenovorans
1.2.1.77 NADP+ the enzyme is more active in the presence of NADP+ relative to NAD+. Crystallographic data show that cofactor selectivity is governed by a complex network of hydrogen bonds between the oxygen atoms of the 2'-phosphoryl moiety of NADP+ and a threonine/lysine pair on the enzyme Paraburkholderia xenovorans