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Literature summary extracted from

  • Powlowski, J.; Sahlman, L.; Shingler, V.
    Purification and properties of the physically associated meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600 (1993), J. Bacteriol., 175, 377-385.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.3.39 NAD+ stimulates slightly Pseudomonas sp.
4.1.3.39 NADH stimulates Pseudomonas sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.10 overexpression in Escherichia coli Pseudomonas sp.
4.1.3.39 gene dmpG encodes the enzyme in the dmp operon together with aldehyde dehydrogenase, EC 1.2.1.10, with which it forms an enzyme complex Pseudomonas sp.

General Stability

EC Number General Stability Organism
1.2.1.10 activity is highest in HEPES buffer and somewhat lower in phosphate buffer, activity in Tris buffer is about half the rate in HEPES buffer Pseudomonas sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.3.39 Zn2+ strong inhibition Pseudomonas sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.3.39 Mn2+ stimulates 6-8fold at 1 mM Pseudomonas sp.
4.1.3.39 additional information no effect by Mg2+ and Ca2+ Pseudomonas sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.10 32500
-
 2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate Pseudomonas sp.
1.2.1.10 39000
-
 2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate Pseudomonas sp.
1.2.1.10 148000
-
 gel filtration, molecular mass of enzyme complex, occurs in complex with 4-hydroxy-2-ketovalerate Pseudomonas sp.
4.1.3.39 35000
-
 2 * 35000 + 2 * 40000, enzyme complex of aldehyde dehydrogenase and 4-hydroxy-2-ketovalerate aldolase, SDS-PAGE Pseudomonas sp.
4.1.3.39 40000
-
 2 * 35000 + 2 * 40000, enzyme complex of aldehyde dehydrogenase and 4-hydroxy-2-ketovalerate aldolase, SDS-PAGE Pseudomonas sp.
4.1.3.39 148000
-
 enzyme in complex with aldehyde dehydrogenase, EC 1.2.1.10, gel filtration Pseudomonas sp.

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+ Pseudomonas sp.
-
 acetyl-CoA + NADH
-
 ?
1.2.1.10 acetaldehyde + CoA + NAD+ Pseudomonas sp. CF 600
-
 acetyl-CoA + NADH
-
 ?
4.1.3.39 4-hydroxy-2-oxovalerate Pseudomonas sp.
-
 pyruvate + acetaldehyde
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.10 Pseudomonas sp.
-
-
-
1.2.1.10 Pseudomonas sp. CF 600
-
-
-
4.1.3.39 Pseudomonas sp.
-
 gene dmpG
-
4.1.3.39 Pseudomonas sp. CF 600
-
 gene dmpG
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.10
-
 Pseudomonas sp.
4.1.3.39 co-purification with aldehyde dehydrogenase, EC 1.2.1.10, to homogeneity in a 5-step chromatographic procedure Pseudomonas sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.3.39 4.2
-
 purified enzyme Pseudomonas sp.

Storage Stability

EC Number Storage Stability Organism
1.2.1.10 -80°C, 10 mM phosphate buffer, pH 7.5, 1 mM dithiothreitol Pseudomonas sp.
4.1.3.39 -80°C, purified native enzyme, stable for at least 6 months Pseudomonas sp.
4.1.3.39 4-6°C, purified native enzyme, stable for at least 6 days Pseudomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.10 acetaldehyde + CoA + NAD+
-
 Pseudomonas sp. acetyl-CoA + NADH
-
 ?
1.2.1.10 acetaldehyde + CoA + NAD+
-
 Pseudomonas sp. CF 600 acetyl-CoA + NADH
-
 ?
1.2.1.10 formaldehyde + CoA + NAD+
-
 Pseudomonas sp. formyl-CoA + NADH
-
 ?
1.2.1.10 formaldehyde + CoA + NAD+
-
 Pseudomonas sp. CF 600 formyl-CoA + NADH
-
 ?
1.2.1.10 isobutyraldehyde + CoA + NAD+
-
 Pseudomonas sp. isobutyryl-CoA + NADH
-
 ?
1.2.1.10 isobutyraldehyde + CoA + NAD+
-
 Pseudomonas sp. CF 600 isobutyryl-CoA + NADH
-
 ?
1.2.1.10 n-butyraldehyde + CoA + NAD+
-
 Pseudomonas sp. n-butyryl-CoA + NADH
-
 ?
1.2.1.10 n-butyraldehyde + CoA + NAD+
-
 Pseudomonas sp. CF 600 n-butyryl-CoA + NADH
-
 ?
1.2.1.10 propanal + CoA + NAD+ initial rate of reaction with propanal is 2.7fold slower than that with acetaldehyde Pseudomonas sp. propionyl-CoA + NADH
-
 ?
1.2.1.10 propanal + CoA + NAD+ initial rate of reaction with propanal is 2.7fold slower than that with acetaldehyde Pseudomonas sp. CF 600 propionyl-CoA + NADH
-
 ?
4.1.3.39 4-hydroxy-2-oxovalerate
-
 Pseudomonas sp. pyruvate + acetaldehyde
-
 ?
4.1.3.39 4-hydroxy-2-oxovalerate the enzyme utilizes the L-(S)-isomer or the racemate Pseudomonas sp. pyruvate + acetaldehyde
-
 ?
4.1.3.39 additional information the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, which acts on acetaldehyde to form acetyl-CoA Pseudomonas sp. ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.10 tetramer 2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate Pseudomonas sp.
4.1.3.39 More the enzyme is encoded in the dmp operon with aldehyde dehydrogenase, EC 1.2.1.10, with which it forms an enzyme complex Pseudomonas sp.
4.1.3.39 tetramer 2 * 35000 + 2 * 40000, enzyme complex of aldehyde dehydrogenase and 4-hydroxy-2-ketovalerate aldolase, SDS-PAGE Pseudomonas sp.

Synonyms

EC Number Synonyms Comment Organism
4.1.3.39 4-hydroxy-2-ketovalerate aldolase
-
 Pseudomonas sp.
4.1.3.39 HOA
-
 Pseudomonas sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.3.39 25
-
 assay at Pseudomonas sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.3.39 8.5 9
-
 Pseudomonas sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.2.1.10 6.5 8.5 activity increases gradually over pH range from 6.5 to 8.5 Pseudomonas sp.
4.1.3.39 6.5 9
-
 Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.10 CoA
-
 Pseudomonas sp.
1.2.1.10 NAD+
-
 Pseudomonas sp.
1.2.1.10 NADH rate of reaction with NADP+ is only 7% of that with NAD+ Pseudomonas sp.