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Literature summary extracted from

  • Manjasetty, B.A.; Powlowski, J.; Vrielink, A.
    Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate (2003), Proc. Natl. Acad. Sci. USA, 100, 6992-6997.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.10
-
 Pseudomonas sp.
4.1.3.39 purified selenomethionine-labeled enzyme complex of 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating), protein solution contains 9 mg/ml protein in 50 mM Tris-HCl, pH 7.4, 1 mM DTT, and 2 mM NAD+, mixing of equal volumes of 0.001 ml of protein and reservoir solutions, the latter contains 18% PEG 8000, 100 mM ammonium sulfate, and 100 mM PIPES, pH 7.5, 3 days, crystals are used for microseeding, cryoprotection by soaking in mother liquor with 20% v/v 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 1.7 A resolution Pseudomonas sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.10 iodoacetate
-
 Pseudomonas sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.10 140000
-
-
 Pseudomonas sp.
4.1.3.39 32500
-
 1 * 32500 + 1 * 37500, active unit is an enzyme complex of aldehyde dehydrogenase and 4-hydroxy-2-ketovalerate aldolase, SDS-PAGE and crystal structure Pseudomonas sp.
4.1.3.39 37500
-
 1 * 32500 + 1 * 37500, active unit is an enzyme complex of aldehyde dehydrogenase and 4-hydroxy-2-ketovalerate aldolase, SDS-PAGE and crystal structure 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. involved in degradation of toxic aromatic compounds via the intermediate catechol acetyl-CoA + NADH
-
 r
1.2.1.10 acetaldehyde + CoA + NAD+ Pseudomonas sp. CF 600 involved in degradation of toxic aromatic compounds via the intermediate catechol acetyl-CoA + NADH
-
 r
4.1.3.39 4-hydroxy-2-oxovalerate Pseudomonas sp. last but one step in meta-cleavage pathway for catechol degradation pyruvate + acetaldehyde
-
 ?
4.1.3.39 additional information Pseudomonas sp. the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, performs the final step in meta-cleavage pathway for catechol degradation ?
-
 ?
4.1.3.39 additional information Pseudomonas sp. CF 600 the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, performs the final step in meta-cleavage pathway for catechol degradation ?
-
 ?

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.
-
 dmpFG-encoded 4-hydroxy-2-ketovalerate aldolase/aldehyde dehydrogenase (acylating), EC 1.2.1.10
-
4.1.3.39 Pseudomonas sp. CF 600
-
 dmpFG-encoded 4-hydroxy-2-ketovalerate aldolase/aldehyde dehydrogenase (acylating), EC 1.2.1.10
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.2.1.10 acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+ part of a bifunctional enzyme complex that also displays 4-hydroxy-2-ketovalerate aldolase activity Pseudomonas sp.
a
4.1.3.39 (S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate active site structure, molecular channeling of substrate and intermediate Pseudomonas sp.
a

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
-
 r
1.2.1.10 acetaldehyde + CoA + NAD+ involved in degradation of toxic aromatic compounds via the intermediate catechol Pseudomonas sp. acetyl-CoA + NADH
-
 r
1.2.1.10 acetaldehyde + CoA + NAD+
-
 Pseudomonas sp. CF 600 acetyl-CoA + NADH
-
 r
1.2.1.10 acetaldehyde + CoA + NAD+ involved in degradation of toxic aromatic compounds via the intermediate catechol Pseudomonas sp. CF 600 acetyl-CoA + NADH
-
 r
4.1.3.39 4-hydroxy-2-oxovalerate
-
 Pseudomonas sp. pyruvate + acetaldehyde
-
 ?
4.1.3.39 4-hydroxy-2-oxovalerate last but one step in meta-cleavage pathway for catechol degradation Pseudomonas sp. pyruvate + acetaldehyde
-
 ?
4.1.3.39 4-hydroxy-2-oxovalerate
-
 Pseudomonas sp. CF 600 pyruvate + acetaldehyde
-
 ?
4.1.3.39 additional information the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, performs the final step in meta-cleavage pathway for catechol degradation Pseudomonas sp. ?
-
 ?
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, molecular channeling of substrate and intermediate Pseudomonas sp. ?
-
 ?
4.1.3.39 additional information the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, performs the final step in meta-cleavage pathway for catechol degradation Pseudomonas sp. CF 600 ?
-
 ?
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, molecular channeling of substrate and intermediate Pseudomonas sp. CF 600 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.10 tetramer composed of two dimers, one dimer accounts for 4-hydroxy-2-ketovalerate aldolase, subunit size 37500, and one for acylating acetaldehyde dehydrogenase, subunit size 32500 Pseudomonas sp.
4.1.3.39 dimer 1 * 32500 + 1 * 37500, active unit is an enzyme complex of aldehyde dehydrogenase and 4-hydroxy-2-ketovalerate aldolase, SDS-PAGE and crystal structure Pseudomonas sp.
4.1.3.39 More enzyme complex structure analysis Pseudomonas sp.

Synonyms

EC Number Synonyms Comment Organism
1.2.1.10 4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase bifunctional enzyme Pseudomonas sp.
4.1.3.39 DmpFG
-
 Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.10 NAD+
-
 Pseudomonas sp.