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Literature summary extracted from

  • Krahulec, S.; Armao, G.C.; Bubner, P.; Klimacek, M.; Nidetzky, B.
    Polyol-specific long-chain dehydrogenases/reductases of mannitol metabolism in Aspergillus fumigatus: biochemical characterization and pH studies of mannitol 2-dehydrogenase and mannitol-1-phosphate 5-dehydrogenase (2009), Chem. Biol. Interact., 178, 274-282.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.17 heterologous expression in Escherichia coli JM109 Aspergillus fumigatus
1.1.1.67 expressed in Escherichia coli JM109 cells Aspergillus fumigatus

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.17 K213A residual activity Aspergillus fumigatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.67 0.019
-
NADH at 25°C, in 100 mM Tris/HCl buffer, pH 7.1 Aspergillus fumigatus
1.1.1.67 0.15
-
NAD+ at 25°C, in 100 mM glycine/NaOH buffer pH 10.0 Aspergillus fumigatus
1.1.1.67 13
-
D-mannitol at 25°C, in 100 mM glycine/NaOH buffer pH 10.0 Aspergillus fumigatus
1.1.1.67 60
-
D-fructose at 25°C, in 100 mM Tris/HCl buffer, pH 7.1 Aspergillus fumigatus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.67 additional information does not require metals for activity Aspergillus fumigatus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.67 58000
-
recombinant enzyme, SDS-PAGE Aspergillus fumigatus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.17 Aspergillus fumigatus
-
-
-
1.1.1.67 Aspergillus fumigatus Q4WQY4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.17 wild-type and mutant Aspergillus fumigatus
1.1.1.67 Co2+ chelating Sepharose column chromatography and Superdex 200 gel filtration Aspergillus fumigatus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.67 14
-
crude extract, at 25°C, using 100 mM Tris-HCl buffer, pH 7.1 Aspergillus fumigatus
1.1.1.67 33
-
after 6.7fold purification, at 25°C, using 100 mM Tris-HCl buffer, pH 7.1 Aspergillus fumigatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.17 D-fructose 6-phosphate + NADH + H+
-
Aspergillus fumigatus D-mannitol 1-phosphate + NAD+
-
r
1.1.1.17 D-mannitol 1-phosphate + NAD+
-
Aspergillus fumigatus D-fructose 6-phosphate + NADH + H+
-
r
1.1.1.17 additional information important role for Lys213 in the catalytic mechanism of M1PDH Aspergillus fumigatus ?
-
?
1.1.1.67 D-mannitol + NAD+
-
Aspergillus fumigatus D-fructose + NADH + H+
-
r
1.1.1.67 D-mannitol + NADP+ M2DH is a much poorer enzyme when it employes NADP+ and NADPH as compared to NAD+ and NADH Aspergillus fumigatus D-fructose + NADPH + H+
-
r

Subunits

EC Number Subunits Comment Organism
1.1.1.67 monomer 1 * 58000, recombinant enzyme, SDS-PAGE Aspergillus fumigatus

Synonyms

EC Number Synonyms Comment Organism
1.1.1.17 M1PDH
-
Aspergillus fumigatus
1.1.1.67 M2DH
-
Aspergillus fumigatus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.17 0.0019
-
D-mannitol 1-phosphate purified mutant K213A Aspergillus fumigatus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.17 6 10 for the oxidative and reductive direction of the reactions under conditions where substrate is limiting (kcat/K) or saturating (kcat) Aspergillus fumigatus
1.1.1.67 6 10
-
Aspergillus fumigatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.17 NAD+
-
Aspergillus fumigatus
1.1.1.17 NADH
-
Aspergillus fumigatus
1.1.1.67 NAD+ dependent on, M2DH is a much poorer enzyme when it employes NADP+ and NADPH as compared to NAD+ and NADH Aspergillus fumigatus
1.1.1.67 NADP+ M2DH is a much poorer enzyme when it employes NADP+ and NADPH as compared to NAD+ and NADH Aspergillus fumigatus