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Literature summary extracted from

  • Baker, P.; Carere, J.; Seah, S.Y.
    Substrate specificity, substrate channeling, and allostery in BphJ: an acylating aldehyde dehydrogenase associated with the pyruvate aldolase BphI (2012), Biochemistry, 51, 4558-4567.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.3.39 BphJ the aldehyde dehydrogenase BphJ coordinates the catalytic activity of BphI through allostery rather than through aldehyde channeling Paraburkholderia xenovorans

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.10
-
 Paraburkholderia xenovorans
4.1.3.39 expressed in Escherichia coli Paraburkholderia xenovorans

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.10 C131A inactive Paraburkholderia xenovorans
1.2.1.10 C131S inactive Paraburkholderia xenovorans
1.2.1.10 D208A the mutant shows reduced catalytic efficiency compared to the wild type enzyme Paraburkholderia xenovorans
1.2.1.10 I171A level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover. The mutation results in a 35% reduction in acetaldehyde channeling efficiency Paraburkholderia xenovorans
1.2.1.10 I171F the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Paraburkholderia xenovorans
1.2.1.10 I195A the variant has a 20fold higher catalytic efficiency for butyraldehyde and pentaldehyde compared to the catalytic efficiency of the wild type toward its natural substrate acetaldehyde. The mutation results in a 35% reduction in acetaldehyde channeling efficiency Paraburkholderia xenovorans
1.2.1.10 I195F the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme Paraburkholderia xenovorans
1.2.1.10 I195W the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Paraburkholderia xenovorans
1.2.1.10 N170A the mutation does not substantially alter aldehyde channeling efficiencies. The level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover Paraburkholderia xenovorans
1.2.1.10 N170D level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover Paraburkholderia xenovorans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.10 3.2
-
 picolinaldehyde mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 4.6
-
 Butyraldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 6.9
-
 picolinaldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 8.2
-
 pentaldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 12
-
 picolinaldehyde mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 12.6
-
 Butyraldehyde mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 17
-
 acetaldehyde mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 18.2
-
 picolinaldehyde wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 18.7
-
 acetaldehyde mutant enzyme D208A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 19.3
-
 Butyraldehyde mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 20.4
-
 propionaldehyde mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 23.1
-
 propionaldehyde wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 23.6
-
 acetaldehyde wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 27.2
-
 propionaldehyde mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 31.5
-
 propionaldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 31.7
-
 Butyraldehyde wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 34.9
-
 acetaldehyde mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 45.6
-
 acetaldehyde mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 79.5
-
 propionaldehyde mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 133
-
 acetaldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
4.1.3.39 0.089
-
 (S)-4-hydroxy-2-oxopentanoate in the presence of NADH, in 100 mM HEPES pH 8.0, at 25°C Paraburkholderia xenovorans
4.1.3.39 0.158
-
 (S)-4-hydroxy-2-oxopentanoate in the absence of NADH, in 100 mM HEPES pH 8.0, at 25°C Paraburkholderia xenovorans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.10 acetaldehyde + CoA + NAD+ Paraburkholderia xenovorans
-
 acetyl-CoA + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.10 Paraburkholderia xenovorans Q79AF6
-
-
4.1.3.39 Paraburkholderia xenovorans
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.10 Ni-NTA column chromatography Paraburkholderia xenovorans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.10 acetaldehyde + CoA + NAD+
-
 Paraburkholderia xenovorans acetyl-CoA + NADH + H+
-
 ?
1.2.1.10 acetaldehyde + CoA + NAD+
-
 Paraburkholderia xenovorans acetyl-CoA + NADH + H+
-
 r
1.2.1.10 butyraldehyde + CoA + NAD+
-
 Paraburkholderia xenovorans butyryl-CoA + NADH + H+
-
 r
1.2.1.10 additional information BphJ forms a heterotetrameric complex with the class II aldolase BphI that channels aldehydes produced in the aldol cleavage reaction to the dehydrogenase via a molecular tunnel Paraburkholderia xenovorans ?
-
 ?
1.2.1.10 pentaldehyde + CoA + NAD+
-
 Paraburkholderia xenovorans pentyl-CoA + NADH + H+
-
 r
1.2.1.10 picolinaldehyde + CoA + NAD+
-
 Paraburkholderia xenovorans picolinyl-CoA + NADH + H+
-
 r
1.2.1.10 propionaldehyde + CoA + NAD+
-
 Paraburkholderia xenovorans propionyl-CoA + NADH + H+
-
 r
4.1.3.39 (S)-4-hydroxy-2-oxopentanoate
-
 Paraburkholderia xenovorans ethanal + pyruvate
-
 ?
4.1.3.39 additional information BphJ forms a heterotetrameric complex with BphI that channels aldehydes produced in the aldol cleavage reaction to the dehydrogenase via a molecular tunnel Paraburkholderia xenovorans ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.1.10 ACDH
-
 Paraburkholderia xenovorans
1.2.1.10 BphJ
-
 Paraburkholderia xenovorans
1.2.1.10 nonphosphorylating acylating aldehyde dehydrogenase
-
 Paraburkholderia xenovorans
4.1.3.39 BphI
-
 Paraburkholderia xenovorans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.10 1.9
-
 picolinaldehyde mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 2.4
-
 picolinaldehyde mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 2.8
-
 picolinaldehyde wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 3.2
-
 picolinaldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 3.4
-
 propionaldehyde mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 6
-
 propionaldehyde mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 6.9
-
 acetaldehyde mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 7.1
-
 Butyraldehyde mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 7.6
-
 acetaldehyde mutant enzyme D208A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 7.6
-
 propionaldehyde mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 7.8
-
 acetaldehyde mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 9.5
-
 Butyraldehyde wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 12.1
-
 propionaldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 12.6
-
 Butyraldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 13
-
 pentaldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 15.4
-
 acetaldehyde mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 16.3
-
 propionaldehyde wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 16.7
-
 Butyraldehyde mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 17.2
-
 acetaldehyde wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 19.7
-
 acetaldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 24.9
-
 propionaldehyde mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 37.9
-
 acetaldehyde mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
4.1.3.39 0.79
-
 (S)-4-hydroxy-2-oxopentanoate in the absence of NADH, in 100 mM HEPES pH 8.0, at 25°C Paraburkholderia xenovorans
4.1.3.39 4.07
-
 (S)-4-hydroxy-2-oxopentanoate in the presence of NADH, in 100 mM HEPES pH 8.0, at 25°C Paraburkholderia xenovorans

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.10 NAD+
-
 Paraburkholderia xenovorans
4.1.3.39 NADH BphI is activated in the presence of the BphJ cofactor, NADH, by about 5fold Paraburkholderia xenovorans

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.2.1.10 0.00011
-
 picolinaldehyde mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.00076
-
 picolinaldehyde mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.0265
-
 pentaldehyde mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.0346
-
 pentaldehyde mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.0387
-
 picolinaldehyde mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.0425
-
 propionaldehyde mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.0433
-
 Butyraldehyde mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.0458
-
 Butyraldehyde mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.0728
-
 pentaldehyde mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.076
-
 pentaldehyde wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.147
-
 acetaldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.152
-
 acetaldehyde mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.154
-
 picolinaldehyde wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.167
-
 propionaldehyde mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.221
-
 propionaldehyde mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.223
-
 acetaldehyde mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.3
-
 Butyraldehyde wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.37
-
 Butyraldehyde mutant enzyme I171F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.384
-
 propionaldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.457
-
 acetaldehyde mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.46
-
 acetaldehyde mutant enzyme D208A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.468
-
 picolinaldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.597
-
 picolinaldehyde mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.7
-
 propionaldehyde wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 0.73
-
 acetaldehyde wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 1.219
-
 propionaldehyde mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 1.323
-
 Butyraldehyde mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 1.584
-
 pentaldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 2.224
-
 acetaldehyde mutant enzyme I171A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans
1.2.1.10 2.763
-
 Butyraldehyde mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0) Paraburkholderia xenovorans