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Literature summary extracted from

  • de Araujo, S.; Neves, C.M.L.; Guimaraes, S.L.; Whitman, C.P.; Johnson Jr., W.H.; Aparicio, R.; Nagem, R.A.P.
    Structural and kinetic characterization of recombinant 2-hydroxymuconate semialdehyde dehydrogenase from Pseudomonas putida G7 (2015), Arch. Biochem. Biophys., 579, 8-17 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.85 gene nahI, the naphthalene catabolic genes (nah) of NAH7 are organized into two operons on a 83 kilobase plasmid, recombinant expression of soluble N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha Pseudomonas putida

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.85 enzyme structure analysis by dynamic light scattering, small-angle X-ray scattering experiments and circular dichroism spectroscopy Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.85 additional information
-
 additional information Michaelis-Menten kinetics Pseudomonas putida
1.2.1.85 0.0013
-
 2-hydroxymuconate-6-semialdehyde pH 8.5, 25°C, recombinant enzyme Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.85 184000
-
 recombinant enzyme, gel filtration Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.85 2-hydroxymuconate-6-semialdehyde + NAD+ + H2O Pseudomonas putida
-
 (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
-
 ?
1.2.1.85 2-hydroxymuconate-6-semialdehyde + NAD+ + H2O Pseudomonas putida G7
-
 (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.85 Pseudomonas putida Q1XGK8
-
-
1.2.1.85 Pseudomonas putida G7 Q1XGK8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.85 recombinant soluble N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, tag cleavage by TEV protease, and another nickel affinity chromatography step, followed by gel filtration and ultrafiltration Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.85 2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
-
 Pseudomonas putida (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
-
 ?
1.2.1.85 2-hydroxymuconate-6-semialdehyde + NAD+ + H2O
-
 Pseudomonas putida G7 (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + NADH + 2 H+
-
 ?
1.2.1.85 additional information enzyme NahI is highly specific for its biological substrate, 2-hydroxymuconate semialdehyde, no activity with salicylaldehyde, another intermediate in the naphthalene-degradation pathway Pseudomonas putida ?
-
 ?
1.2.1.85 additional information enzyme NahI is highly specific for its biological substrate, 2-hydroxymuconate semialdehyde, no activity with salicylaldehyde, another intermediate in the naphthalene-degradation pathway Pseudomonas putida G7 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.85 More enzyme protein structure analysis by circular dichroism spectroscopy, and three-dimensional structure model, overview Pseudomonas putida
1.2.1.85 tetramer x * 51712, recombinant detagged enzyme, mass spectrometry, x * 55000, recombinant N-terminally His-tagged enzyme, SDS-PAGE Pseudomonas putida

Synonyms

EC Number Synonyms Comment Organism
1.2.1.85 2-hydroxymuconate semialdehyde dehydrogenase
-
 Pseudomonas putida
1.2.1.85 NahI
-
 Pseudomonas putida

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.85 25
-
 assay at Pseudomonas putida

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.85 0.9
-
 2-hydroxymuconate-6-semialdehyde pH 8.5, 25°C, recombinant enzyme Pseudomonas putida

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.85 8.5
-
 assay at Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.85 NAD+
-
 Pseudomonas putida

General Information

EC Number General Information Comment Organism
1.2.1.85 evolution the naphthalene catabolic genes (nah) of NAH7 are organized into two operons. The nah operon (nahAaAbAcAdBFCED) encodes the upper pathway enzymes involved in the conversion of naphthalene to salicylate. On the other hand, the sal operon (nahGTHINLOMKJ) codes for the lower pathway enzymes involved in the conversion of salicylate to pyruvate and acetaldehyde. The lower pathway starts with the oxidation of salicylate to catechol by salicylate hydroxylase (NahG), which is extradiol-cleaved by catechol-2,3-dioxygenase (NahH) and further transformed to pyruvate and acetyl-CoA by the remaining meta-cleavage pathway gene products, NahI, NahJ, NahK, NahN, NahL, NahM, and NahO. Enzyme NahI is further classified into the ALDH8 family together with different 2-hydroxymuconate semialdehyde dehydrogenases Pseudomonas putida
1.2.1.85 physiological function the enzyme is involved in the degradation of intermediate 2-hydroxymuconate 6-semialdehyde in the naphthalene-degradation pathway Pseudomonas putida