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Literature summary for 1.2.1.32 extracted from

  • Huo, L.; Davis, I.; Liu, F.; Andi, B.; Esaki, S.; Iwaki, H.; Hasegawa, Y.; Orville, A.M.; Liu, A.
    Crystallographic and spectroscopic snapshots reveal a dehydrogenase in action (2015), Nat. Commun., 6, 5935 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.1.32

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expressin of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli Pseudomonas fluorescens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged E268A mutant enzyme in complex with NAD+ or NAD+ and 2-aminomuconate or 2-hydroxymuconate, hanging drop diffusion, mixing of 0.0015 ml of 40 mg/ml protein solution with 0.0015 ml of reservoir solution containing 20% PEG 3350 and 0.2 M sodium phosphate dibasic monohydrate, pH 9.1, at 18°C, 2-3 days, crystals are soaked in ligand solution for the formation of complex crystals, X-ray diffraction structure determination and analysis at 1.95-2.20 A resolution, molecular replacement using 5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase, PDB: 2D4E, as a search model, and molecular modelling Pseudomonas fluorescens

Protein Variants

Protein Variants Comment Organism
E268A site-directed mutagenesis, catalytically inactive mutant, formation of an enzyme-substrate adduct in the E268A mutant investigated by mass spectrometry Pseudomonas fluorescens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten steady-state kinetics and kinetic analysis, overview Pseudomonas fluorescens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-aminomuconate 6-semialdehyde + NAD+ + H2O Pseudomonas fluorescens
-
 2-aminomuconate + NADH + 2 H+
-
 ?
2-aminomuconate 6-semialdehyde + NAD+ + H2O Pseudomonas fluorescens KU-7
-
 2-aminomuconate + NADH + 2 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens Q83V33
-
-
Pseudomonas fluorescens KU-7 Q83V33
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His-tagged wild-type and mutant enzymes from Escherichia coli Pseudomonas fluorescens

Reaction

Reaction Comment Organism Reaction ID
2-aminomuconate 6-semialdehyde + NAD+ + H2O = 2-aminomuconate + NADH + H+ the catalytic cycle, overview Pseudomonas fluorescens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-aminomuconate 6-semialdehyde + NAD+ + H2O
-
 Pseudomonas fluorescens 2-aminomuconate + NADH + 2 H+
-
 ?
2-aminomuconate 6-semialdehyde + NAD+ + H2O enzyme-substrate binding structure and catalytic mechanism, overview. Due to the unstable nature of its substrate 2-aminomuconate 6-semialdehyde, 2-AMS, the activity of AMSDH is detected using a coupled-enzyme assay that employs its upstream partner, alpha-amino beta-carboxymuconate epsilon-semialdehyde decarboxylase (ACMSD), to generate 2-AMS in situ Pseudomonas fluorescens 2-aminomuconate + NADH + 2 H+
-
 ?
2-aminomuconate 6-semialdehyde + NAD+ + H2O
-
 Pseudomonas fluorescens KU-7 2-aminomuconate + NADH + 2 H+
-
 ?
2-aminomuconate 6-semialdehyde + NAD+ + H2O enzyme-substrate binding structure and catalytic mechanism, overview. Due to the unstable nature of its substrate 2-aminomuconate 6-semialdehyde, 2-AMS, the activity of AMSDH is detected using a coupled-enzyme assay that employs its upstream partner, alpha-amino beta-carboxymuconate epsilon-semialdehyde decarboxylase (ACMSD), to generate 2-AMS in situ Pseudomonas fluorescens KU-7 2-aminomuconate + NADH + 2 H+
-
 ?

Subunits

Subunits Comment Organism
? x * 56252, recombinant N-terminally His-tagged enzyme mutant E268A, mass spectrometry Pseudomonas fluorescens
More analysis of crystal structures of a tetrahedral, thiohemiacetal intermediate, a thioacyl intermediate and an NAD+-bound complex from the active site mutant E268A. These covalent intermediates are characterized by single-crystal and solution-state electronic absorption spectroscopy. The crystal structures reveal that the substrate undergoes an E/Z isomerization at the enzyme active site before an sp3-to-sp2 transition during enzyme-mediated oxidation Pseudomonas fluorescens

Synonyms

Synonyms Comment Organism
2-aminomuconate-6-semialdehyde dehydrogenase
-
 Pseudomonas fluorescens
AMSDH
-
 Pseudomonas fluorescens
nbaE gene name, UniProt Pseudomonas fluorescens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
10
-
 assay at Pseudomonas fluorescens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Pseudomonas fluorescens

Cofactor

Cofactor Comment Organism Structure
NAD+ enzyme-cofactor binding structure and catalytic mechanism, overview Pseudomonas fluorescens

General Information

General Information Comment Organism
metabolism the enzyme is involved in the metabolic pathway for tryptophan degradation Pseudomonas fluorescens
additional information analysis of catalytic mechanism, formation of catalytic intermediates, ligand binding, and active site structure, molecular modelling, overview Pseudomonas fluorescens
physiological function several aldehydic intermediates in the metabolic pathway for tryptophan degradation can decay into neuroactive compounds that are associated with numerous neurological diseases. 2-Aminomuconate-6-semialdehyde dehydrogenase is involved in the pathway and is responsible for disarming the final aldehydic intermediate. The enzymeis responsible for oxidizing the unstable metabolic intermediate 2-aminomuconate-6-semialdehyde to 2-aminomuconate Pseudomonas fluorescens