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Literature summary extracted from

  • Sakuma, M.; Kametani, S.; Akanuma, H.
    Purification and some properties of a hepatic NADPH-dependent reductase that specifically acts on 1,5-anhydro-D-fructose (1998), J. Biochem., 123, 189-193.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.263 1,5-anhydro-D-glucitol 2.3% inhibition at 100 mM Sus scrofa
1.1.1.263 2-mercaptoethanol 2.3% inhibition at 1 mM Sus scrofa
1.1.1.263 ascorbic acid 30% inhibition at 1 mM Sus scrofa
1.1.1.263 Barbital 15% inhibition at 1 mM Sus scrofa
1.1.1.263 D-glucose 2.6% inhibition at 100 mM Sus scrofa
1.1.1.263 D-glucose-1-phosphate 25.5% inhibition at 50 mM Sus scrofa
1.1.1.263 D-Glucose-6-phosphate 2% inhibition at 50 mM Sus scrofa
1.1.1.263 EDTA 59% inhibition at 10 mM Sus scrofa
1.1.1.263 iodoacetamide 41% inhibition at 1 mM Sus scrofa
1.1.1.263 iodoacetic acid 27% inhibition at 1 mM Sus scrofa
1.1.1.263 p-chloromercuribenzoic acid 79% inhibition at 0.1 mM, partially reversed by 0.1 mM 2-mercaptoethanol Sus scrofa
1.1.1.263 Phenobarbital 22% inhibition at 1 mM Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.263 0.44
-
1,5-Anhydro-D-fructose
-
Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.263 35000
-
gel filtration Sus scrofa
1.1.1.263 38000
-
1 * 38000, SDS-PAGE Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.263 1,5-anhydro-D-fructose + NADPH Sus scrofa best substrate, only poorly active with NADH 1,5-anhydro-D-glucitol + NADP+
-
ir

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.263 Rattus sp.
-
-
-
1.1.1.263 Sus scrofa
-
porcine
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.263 to homogeneity, chromatography techniques Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.263 liver
-
Sus scrofa
-
1.1.1.263 liver higher activity compared to the porcine liver enzyme Rattus sp.
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.263 1.16
-
-
Sus scrofa

Storage Stability

EC Number Storage Stability Organism
1.1.1.263 4°C, 20 mM sodium phosphate, pH 7.0, one month Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.263 1,5-anhydro-D-fructose + NADPH best substrate, only poorly active with NADH Sus scrofa 1,5-anhydro-D-glucitol + NADP+
-
ir
1.1.1.263 2,3-butanedione + NADPH 50% of the activity compared to the natural substrate Sus scrofa hydroxybutanone + NADP+
-
?
1.1.1.263 acetaldehyde + NADPH + H+ very low activity Sus scrofa ethanol + NADP+
-
?
1.1.1.263 formaldehyde + NADPH low activity Sus scrofa methanol + NADP+
-
?
1.1.1.263 glucosone + NADPH very low activity Sus scrofa ? + NADP+
-
?
1.1.1.263 glucuronic acid + NADPH low activity Sus scrofa ? + NADP+
-
?
1.1.1.263 pyridine-3-aldehyde + NADPH good substrate Sus scrofa pyridine-3-ol + NADP+
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.263 monomer 1 * 38000, SDS-PAGE Sus scrofa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.263 37
-
-
Sus scrofa

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.263 45
-
decreasing activity above Sus scrofa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.263 8.7
-
1,5-Anhydro-D-fructose
-
Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.263 7
-
-
Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.263 NADPH
-
Rattus sp.
1.1.1.263 NADPH can not replaced by NADH Sus scrofa