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Literature summary extracted from

  • Ljungcrantz, P.; Bulow, L.; Mosbach, K.
    Construction and characterization of a recombinant tripartite enzyme, galactose dehydrogenase/beta-galactosidase/galactokinase (1990), FEBS Lett., 275, 91-94.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.23 additional information in-frame gene fusion between galactose dehydrogenase, beta-galactosidase and galactokinase, the two major enzyme forms of hybrid protein consist of 4 and 8 subunits, each subunit is made up of one monomer each of galactose dehydrogenase, EC 1.1.1.48, beta-galactosidase, EC 3.2.1.23, and galactokinase, EC 2.7.1.6 Pseudomonas fluorescens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.48 D-galactose + NAD+ Pseudomonas fluorescens
-
D-galactono-1,5-lactone + NADH
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.48 Pseudomonas fluorescens
-
-
-
3.2.1.23 Pseudomonas fluorescens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.23 gene fusion between galactose dehydrogenase, beta-galactosidase and galactokinase Pseudomonas fluorescens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.48 D-galactose + NAD+
-
Pseudomonas fluorescens D-galactono-1,5-lactone + NADH
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.48 50
-
50% activity after 60 min, 100 mM, pH 8.0, 1 mM MgCl2, 1 mM dithiothreitol Pseudomonas fluorescens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.48 10
-
-
Pseudomonas fluorescens