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Literature summary for 1.2.1.5 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
NADP+
-
Paraburkholderia xenovorans LB400
0.042
-
Heptanal
-
Paraburkholderia xenovorans LB400
0.3
-
Valeraldehyde
-
Paraburkholderia xenovorans LB400
0.501
-
NAD+
-
Paraburkholderia xenovorans LB400
1.21
-
propionaldehyde
-
Paraburkholderia xenovorans LB400
1.66
-
Isovaleraldehyde
-
Paraburkholderia xenovorans LB400
1.9
-
formaldehyde
-
Paraburkholderia xenovorans LB400
4.15
-
benzaldehyde
-
Paraburkholderia xenovorans LB400

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Paraburkholderia xenovorans Q13WK4
-
-
Paraburkholderia xenovorans LB400 Q13WK4
-
-

Purification (Commentary)

Purification (Comment) Organism
to homogeneity by nickel affinity chromatography and gel filtration Paraburkholderia xenovorans LB400

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzaldehyde + NADP+ + H2O
-
Paraburkholderia xenovorans LB400 benzoate + NADPH + H+
-
?
formaldehyde + NADP+ + H2O
-
Paraburkholderia xenovorans LB400 formate + NADPH + H+
-
?
heptanal + NADP+ + H2O
-
Paraburkholderia xenovorans LB400 heptanoate + NADPH + H+
-
?
isovaleraldehyde + NADP+ + H2O
-
Paraburkholderia xenovorans LB400 isovalerate + NADPH + H+
-
?
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 ?
-
?
propionaldehyde + NAD+ + H2O
-
Paraburkholderia xenovorans LB400 propionate + NADH + H+
-
r
propionaldehyde + NAD+ + H2O
-
Paraburkholderia xenovorans propionate + NADH + H+
-
?
propionaldehyde + NADP+ + H2O
-
Paraburkholderia xenovorans LB400 propionate + NADPH + H+
-
?
valeraldehyde + NADP+ + H2O
-
Paraburkholderia xenovorans LB400 valerate + NADPH + H+
-
?

Subunits

Subunits Comment Organism
dimer gel filtration Paraburkholderia xenovorans LB400

Synonyms

Synonyms Comment Organism
aldehyde dehydrogenase
-
Paraburkholderia xenovorans LB400
ALDHC
-
Paraburkholderia xenovorans LB400
chromosomally encoded box pathway ALDH
-
Paraburkholderia xenovorans LB400

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Paraburkholderia xenovorans LB400
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