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Literature summary extracted from

  • Wang, W.; Baker, P.; Seah, S.Y.
    Comparison of two metal-dependent pyruvate aldolases related by convergent evolution: substrate specificity, kinetic mechanism, and substrate channeling (2010), Biochemistry, 49, 3774-3782.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.3.39 overexpressed Paraburkholderia xenovorans LB400

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.2.52 the active site of HpaI is formed by approx. 30 residues from adjacent dimers and consists of an approx. 15 A deep bell-shaped cleft with an approx. 12 A wide mouth. This broad entrance to the active site is predominantly lined with noncharged residues and a few positively charged residues Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.2.52 2-oxobutanoate competitive inhibition Escherichia coli
4.1.2.52 2-oxopentanoate competitive inhibition Escherichia coli
4.1.2.52 4-methyl-2-oxopentanoate competitive inhibition Escherichia coli
4.1.2.52 glyoxylate competitive inhibition Escherichia coli
4.1.2.52 pyruvate competitive inhibition Escherichia coli
4.1.3.39 2-ketobutanoate
-
 Escherichia coli
4.1.3.39 2-ketobutanoate
-
 Paraburkholderia xenovorans
4.1.3.39 2-ketobutanoate
-
 Paraburkholderia xenovorans LB400
4.1.3.39 2-ketopentanoate
-
 Escherichia coli
4.1.3.39 2-ketopentanoate
-
 Paraburkholderia xenovorans
4.1.3.39 2-ketopentanoate
-
 Paraburkholderia xenovorans LB400
4.1.3.39 4-methyl-2-oxopentanoate
-
 Escherichia coli
4.1.3.39 4-methyl-2-oxopentanoate
-
 Paraburkholderia xenovorans
4.1.3.39 4-methyl-2-oxopentanoate
-
 Paraburkholderia xenovorans LB400
4.1.3.39 glyoxylate
-
 Escherichia coli
4.1.3.39 glyoxylate
-
 Paraburkholderia xenovorans
4.1.3.39 glyoxylate
-
 Paraburkholderia xenovorans LB400
4.1.3.39 pyruvate
-
 Escherichia coli
4.1.3.39 pyruvate
-
 Paraburkholderia xenovorans
4.1.3.39 pyruvate
-
 Paraburkholderia xenovorans LB400
4.1.3.43 2-oxobutanoate competitive inhibition Paraburkholderia xenovorans
4.1.3.43 2-oxopentanoate competitive inhibition Paraburkholderia xenovorans
4.1.3.43 4-methyl-2-oxopentanoate competitive inhibition Paraburkholderia xenovorans
4.1.3.43 glyoxylate competitive inhibition Paraburkholderia xenovorans
4.1.3.43 pyruvate competitive inhibition Paraburkholderia xenovorans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.2.52 5.6
-
 pyruvate steady-state kinetic parameter, pH 8.0 and 25°C Escherichia coli
4.1.2.52 9.1
-
 Succinic semialdehyde Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 13.4
-
 Butyraldehyde Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 32.9
-
 propionaldehyde Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 33.3
-
 glycolaldehyde Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 50.1
-
 acetaldehyde Km(app) with 2-oxobutanoate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 62.1
-
 acetaldehyde steady-state kinetic parameter, pH 8.0 and 25°C Escherichia coli
4.1.2.52 62.9
-
 acetaldehyde Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 73.8
-
 Isobutyraldehyde Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 88.6
-
 DL-glyceraldehyde Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.3.39 13.4
-
 Butyraldehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 32.9
-
 propionaldehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 33.3
-
 glycolaldehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 62.9
-
 acetaldehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 64.28
-
 acetaldehyde at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate Paraburkholderia xenovorans LB400
4.1.3.39 64.8
-
 acetaldehyde pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 73.8
-
 Succinic semialdehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 88.6
-
 (R,S)-glyceraldehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 124.6
-
 glycolaldehyde pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 124.6
-
 glycolaldehyde at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate Paraburkholderia xenovorans LB400
4.1.3.39 135.9
-
 propionaldehyde pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 135.9
-
 propionaldehyde at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate Paraburkholderia xenovorans LB400
4.1.3.43 14.8
-
 pyruvate steady-state kinetic parameter, pH 8.0 and 25°C Paraburkholderia xenovorans
4.1.3.43 64.3
-
 acetaldehyde app. Km-value with pyruvate as carbonyl donor, pH 8.0 and 25°C Paraburkholderia xenovorans
4.1.3.43 67
-
 acetaldehyde steady-state kinetic parameter, pH 8.0 and 25°C Paraburkholderia xenovorans
4.1.3.43 124.6
-
 glycolaldehyde app. Km-value with pyruvate as carbonyl donor, pH 8.0 and 25°C Paraburkholderia xenovorans
4.1.3.43 135.9
-
 propionaldehyde app. Km-value with pyruvate as carbonyl donor, pH 8.0 and 25°C Paraburkholderia xenovorans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.2.52 Co2+
-
 Escherichia coli
4.1.3.39 Mn2+
-
 Paraburkholderia xenovorans LB400
4.1.3.43 Mn2+ cofactor Paraburkholderia xenovorans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.2.52 pyruvate + succinic semialdehyde Escherichia coli
-
 4-hydroxy-2-oxo-1,7-heptanedioate enzyme lacks stereospecific control producing racemic mixtures of its physiological substrate, 4-hydroxy-2-oxo-1,7-heptanedioate ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.52 Escherichia coli
-
-
-
4.1.3.39 Escherichia coli Q47098
-
-
4.1.3.39 Paraburkholderia xenovorans
-
-
-
4.1.3.39 Paraburkholderia xenovorans LB400 P51015
-
-
4.1.3.43 Paraburkholderia xenovorans
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.3.39
-
 Paraburkholderia xenovorans LB400

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.2.52 4-hydroxy-2-oxoheptanedioate = pyruvate + succinate semialdehyde rapid equilibrium random order mechanism Escherichia coli
a
4.1.3.39 (S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate rapid equilibrium random order mechanism Escherichia coli
a
4.1.3.39 (S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate compulsory order mechanism, with pyruvate binding first Paraburkholderia xenovorans
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.52 2-oxobutanoate + acetaldehyde
-
 Escherichia coli ?
-
 ?
4.1.2.52 pyruvate + acetaldehyde
-
 Escherichia coli 4-hydroxy-2-oxopentanoate enzyme lacks stereospecific control producing racemic mixtures of 4-hydroxy-2-oxopentanoate i.e. HOPA ?
4.1.2.52 pyruvate + butyraldehyde
-
 Escherichia coli ?
-
 ?
4.1.2.52 pyruvate + DL-glyceraldehyde
-
 Escherichia coli ?
-
 ?
4.1.2.52 pyruvate + glycolaldehyde
-
 Escherichia coli ?
-
 ?
4.1.2.52 pyruvate + isobutyraldehyde
-
 Escherichia coli ?
-
 ?
4.1.2.52 pyruvate + pentaldehyde
-
 Escherichia coli ?
-
 ?
4.1.2.52 pyruvate + propionaldehyde
-
 Escherichia coli ?
-
 ?
4.1.2.52 pyruvate + succinic semialdehyde
-
 Escherichia coli 4-hydroxy-2-oxo-1,7-heptanedioate enzyme lacks stereospecific control producing racemic mixtures of its physiological substrate, 4-hydroxy-2-oxo-1,7-heptanedioate ?
4.1.3.39 additional information BphI exhibits a compulsory order mechanism, with pyruvate binding first. BphI is able to utilize acetaldehyde produced by the reduction of acetyl-CoA catalyzed by the associated aldehyde dehydrogenase, BphJ. This aldehyde is directly channeled from the dehydrogenase to the aldolase active sites, with an efficiency of 84%. The BphJ reductive deacylation reaction increases 4fold when BphI is catalyzing the aldol addition reaction. The BphI-BphJ enzyme complex exhibits unique bidirectionality in substrate channeling and allosteric activation Paraburkholderia xenovorans LB400 ?
-
 ?
4.1.3.39 additional information BphI is able to utilize aldehyde acceptors two to five carbons in length. BphI is able to bind 2-keto acids larger than pyruvate. BphI synthesizes only (4S)-4-hydroxy-2-oxopentanoate from pyruvate and acetaldehyde. BphI is also able to utilize acetaldehyde produced by the reduction of acetyl-CoA catalyzed by the associated aldehyde dehydrogenase, BphJ. This aldehyde is directly channeled from the dehydrogenase to the aldolase active sites, with an efficiency of 84%. The BphJ reductive deacylation reaction increases 4-fold when BphI is catalyzing the aldol addition reaction. The BphI-BphJ enzyme complex exhibits unique bidirectionality in substrate channeling and allosteric activation Paraburkholderia xenovorans ?
-
 ?
4.1.3.39 additional information HpaI is able to utilize aldehyde acceptors two to five carbons in length, shows broad specificity and has a preference for aldehydes containing longer linear alkyl chains or C2-OH substitutions. HpaI is able to bind 2-keto acids larger than pyruvate, and to utilize both pyruvate and 2-ketobutanoate as carbonyl donors in the aldol addition reaction. HpaI lacks stereospecific control producing racemic mixtures of 4-hydroxy-2-oxopentanoate from pyruvate and acetaldehyde Escherichia coli ?
-
 ?
4.1.3.39 pyruvate + (R,S)-glyceraldehyde
-
 Escherichia coli ?
-
 ?
4.1.3.39 pyruvate + acetaldehyde
-
 Paraburkholderia xenovorans LB400 (4S)-hydroxy-2-oxopentanoate
-
 ?
4.1.3.39 pyruvate + acetaldehyde
-
 Paraburkholderia xenovorans (4S)-4-hydroxy-2-oxovalerate
-
 ?
4.1.3.39 pyruvate + acetaldehyde
-
 Escherichia coli 4-hydroxy-2-oxopentanoate
-
 ?
4.1.3.39 pyruvate + butyraldehyde
-
 Paraburkholderia xenovorans ?
-
 ?
4.1.3.39 pyruvate + butyraldehyde
-
 Paraburkholderia xenovorans LB400 ?
-
 ?
4.1.3.39 pyruvate + butyraldehyde
-
 Escherichia coli ?
-
 ?
4.1.3.39 pyruvate + glycolaldehyde
-
 Paraburkholderia xenovorans LB400 ?
-
 ?
4.1.3.39 pyruvate + glycolaldehyde
-
 Paraburkholderia xenovorans 4,5-dihydroxy-2-oxo-pentanoic acid
-
 ?
4.1.3.39 pyruvate + glycolaldehyde
-
 Escherichia coli 4,5-dihydroxy-2-oxo-pentanoic acid
-
 ?
4.1.3.39 pyruvate + isobutyraldehyde
-
 Paraburkholderia xenovorans ?
-
 ?
4.1.3.39 pyruvate + isobutyraldehyde
-
 Paraburkholderia xenovorans LB400 ?
-
 ?
4.1.3.39 pyruvate + isobutyraldehyde
-
 Escherichia coli ?
-
 ?
4.1.3.39 pyruvate + pentaldehyde
-
 Paraburkholderia xenovorans LB400 ?
-
 ?
4.1.3.39 pyruvate + propionaldehyde
-
 Paraburkholderia xenovorans ?
-
 ?
4.1.3.39 pyruvate + propionaldehyde
-
 Paraburkholderia xenovorans LB400 ?
-
 ?
4.1.3.39 pyruvate + propionaldehyde
-
 Escherichia coli ?
-
 ?
4.1.3.39 pyruvate + succinic semialdehyde
-
 Escherichia coli (4RS)-4-hydroxy-2-oxoheptane-1,7-dioate racemic product ?
4.1.3.39 pyruvate + succinic semialdehyde
-
 Paraburkholderia xenovorans ?
-
 ?
4.1.3.43 pyruvate + acetaldehyde
-
 Paraburkholderia xenovorans (4S)-4-hydroxy-2-oxopentanoate
-
 ?
4.1.3.43 pyruvate + butyraldehyde
-
 Paraburkholderia xenovorans ?
-
 ?
4.1.3.43 pyruvate + glycolaldehyde
-
 Paraburkholderia xenovorans ?
-
 ?
4.1.3.43 pyruvate + isobutyraldehyde
-
 Paraburkholderia xenovorans ?
-
 ?
4.1.3.43 pyruvate + pentaldehyde
-
 Paraburkholderia xenovorans ?
-
 ?
4.1.3.43 pyruvate + propionaldehyde
-
 Paraburkholderia xenovorans ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.2.52 HpaI
-
 Escherichia coli
4.1.3.39 BphI
-
 Paraburkholderia xenovorans
4.1.3.39 BphI
-
 Paraburkholderia xenovorans LB400
4.1.3.39 pyruvate aldolase
-
 Paraburkholderia xenovorans LB400
4.1.3.43 BphI
-
 Paraburkholderia xenovorans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.2.52 5.6
-
 DL-glyceraldehyde Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 21.9
-
 acetaldehyde Kcat(app) with 2-oxobutanoate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 64.9
-
 Isobutyraldehyde Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 132.5
-
 Butyraldehyde Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 175.5
-
 glycolaldehyde Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 203.8
-
 Succinic semialdehyde Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 205.4
-
 acetaldehyde Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 219.5
-
 pyruvate steady-state kinetic parameter, with acetaldehyde as aldehyde donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 358.4
-
 propionaldehyde Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.3.39 0.4
-
 glycolaldehyde pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 0.4
-
 glycolaldehyde at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate Paraburkholderia xenovorans LB400
4.1.3.39 0.86
-
 acetaldehyde pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 0.86
-
 acetaldehyde at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate Paraburkholderia xenovorans LB400
4.1.3.39 1.79
-
 propionaldehyde pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 1.79
-
 propionaldehyde at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate Paraburkholderia xenovorans LB400
4.1.3.39 5.6
-
 (R,S)-glyceraldehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 64.9
-
 Succinic semialdehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 132.5
-
 Butyraldehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 175.5
-
 glycolaldehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 205.4
-
 acetaldehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 358.4
-
 propionaldehyde pH 8.0, 25°C Escherichia coli
4.1.3.43 0.4
-
 glycolaldehyde app. kcat-value with pyruvate as carbonyl donor, pH 8.0 and 25°C Paraburkholderia xenovorans
4.1.3.43 0.86
-
 acetaldehyde app. kcat-value with pyruvate as carbonyl donor, pH 8.0 and 25°C Paraburkholderia xenovorans
4.1.3.43 1.04
-
 pyruvate steady-state kinetic parameter, with acetaldehyde as aldehyde donor, pH 8.0 and 25°C Paraburkholderia xenovorans
4.1.3.43 1.79
-
 propionaldehyde app. kcat-value with pyruvate as carbonyl donor, pH 8.0 and 25°C Paraburkholderia xenovorans

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.1.2.52 0.4
-
 glyoxylate pH 8.0, 25°C Escherichia coli
4.1.2.52 0.5
-
 2-oxobutanoate pH 8.0, 25°C Escherichia coli
4.1.2.52 0.51
-
 pyruvate pH 8.0, 25°C Escherichia coli
4.1.2.52 2.01
-
 pyruvate pH 8.0, 25°C Escherichia coli
4.1.2.52 3.6
-
 2-oxopentanoate pH 8.0, 25°C Escherichia coli
4.1.2.52 6.98
-
 4-methyl-2-oxopentanoate pH 8.0, 25°C Escherichia coli
4.1.3.39 0.21
-
 glyoxylate pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 0.21
-
 glyoxylate in the presence of 0.4 mM NADH, 2 mM Mn2+, 20 units of ADH in 100 mM HEPES buffer, pH 8.0 at 25°C, in a total volume of 1 ml Paraburkholderia xenovorans LB400
4.1.3.39 0.34
-
 2-ketobutanoate pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 0.34
-
 2-ketobutanoate in the presence of 0.4 mM NADH, 2 mM Mn2+, 20 units of ADH in 100 mM HEPES buffer, pH 8.0 at 25°C, in a total volume of 1 ml Paraburkholderia xenovorans LB400
4.1.3.39 0.4
-
 glyoxylate pH 8.0, 25°C Escherichia coli
4.1.3.39 0.5
-
 2-ketobutanoate pH 8.0, 25°C Escherichia coli
4.1.3.39 0.51
-
 pyruvate pH 8.0, 25°C Escherichia coli
4.1.3.39 0.55
-
 pyruvate pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 0.55
-
 pyruvate in the presence of 0.4 mM NADH, 2 mM Mn2+, 20 units of ADH in 100 mM HEPES buffer, pH 8.0 at 25°C, in a total volume of 1 ml Paraburkholderia xenovorans LB400
4.1.3.39 1.09
-
 2-ketopentanoate pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 1.09
-
 2-ketopentanoate in the presence of 0.4 mM NADH, 2 mM Mn2+, 20 units of ADH in 100 mM HEPES buffer, pH 8.0 at 25°C, in a total volume of 1 ml Paraburkholderia xenovorans LB400
4.1.3.39 2.71
-
 4-methyl-2-oxopentanoate pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 2.71
-
 4-methyl-2-oxopentanoate in the presence of 0.4 mM NADH, 2 mM Mn2+, 20 units of ADH in 100 mM HEPES buffer, pH 8.0 at 25°C, in a total volume of 1 ml Paraburkholderia xenovorans LB400
4.1.3.39 3.6
-
 2-ketopentanoate pH 8.0, 25°C Escherichia coli
4.1.3.39 6.98
-
 4-methyl-2-oxopentanoate pH 8.0, 25°C Escherichia coli
4.1.3.43 0.21
-
 glyoxylate pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.43 0.34
-
 2-oxobutanoate pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.43 0.55
-
 pyruvate pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.43 1.09
-
 2-oxopentanoate pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.43 2.71
-
 4-methyl-2-oxopentanoate pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.43 10.3
-
 pyruvate pH 8.0, 25°C 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
4.1.2.52 0.063
-
 DL-glyceraldehyde Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 0.4
-
 acetaldehyde Kcat/Km(app) with 2-oxobutanoate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 0.9
-
 Isobutyraldehyde Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 3.3
-
 acetaldehyde Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 5.27
-
 glycolaldehyde Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 9.9
-
 Butyraldehyde Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 10.9
-
 propionaldehyde Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 20
-
 pentaldehyde Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.2.52 22.2
-
 Succinic semialdehyde Kcat/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Escherichia coli
4.1.3.39 0.00047
-
 pentaldehyde at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate Paraburkholderia xenovorans LB400
4.1.3.39 0.0005
-
 Isobutyraldehyde at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate Paraburkholderia xenovorans LB400
4.1.3.39 0.00219
-
 Butyraldehyde at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate Paraburkholderia xenovorans LB400
4.1.3.39 0.0037
-
 glycolaldehyde at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate Paraburkholderia xenovorans LB400
4.1.3.39 0.0132
-
 propionaldehyde at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate Paraburkholderia xenovorans LB400
4.1.3.39 0.0134
-
 acetaldehyde at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate Paraburkholderia xenovorans LB400
4.1.3.39 0.063
-
 (R,S)-glyceraldehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 0.5
-
 Succinic semialdehyde pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 2.19
-
 Butyraldehyde pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 3.3
-
 acetaldehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 3.7
-
 glycolaldehyde pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 5.27
-
 glycolaldehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 9.9
-
 Butyraldehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 10.9
-
 propionaldehyde pH 8.0, 25°C Escherichia coli
4.1.3.39 13.2
-
 propionaldehyde pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 13.4
-
 acetaldehyde pH 8.0, 25°C Paraburkholderia xenovorans
4.1.3.39 22.5
-
 Succinic semialdehyde pH 8.0, 25°C Escherichia coli
4.1.3.43 0.00047
-
 pentaldehyde kcat(app)/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Paraburkholderia xenovorans
4.1.3.43 0.0005
-
 Isobutyraldehyde kcat(app)/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Paraburkholderia xenovorans
4.1.3.43 0.0022
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 Butyraldehyde kcat(app)/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Paraburkholderia xenovorans
4.1.3.43 0.0037
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 glycolaldehyde kcat(app)/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Paraburkholderia xenovorans
4.1.3.43 0.0132
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 propionaldehyde kcat(app)/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Paraburkholderia xenovorans
4.1.3.43 0.0134
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 acetaldehyde kcat(app)/Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C Paraburkholderia xenovorans