Roche Diagnostics Operations, Inc.

Roche Diabetes Care, Inc.

Roche Diagnostics Gmbh

F. Hoffmann-la Roche Ag

Daniela Beck

Peter Kratzsch

Mara Boenitz-Dulat

Rainer Schmuck

Wolfgang-Reinhold Knappe

Zhixin Shao

Detlef Thym

Thomas Streidl

Herbert Von Der Eltz

Carina Horn

Stacy Hunt DuVall

Stacy Hunt Duvall

The present invention relates to a mutant 3-hydroxybutyrate dehydrogenase (3-HBDH) with improved performance relative to the wild-type 3-HBDH, a nucleic acid encoding the mutant 3-HBDH, a cell comprising the mutant 3-HBDH or the nucleic acid, a method of determining the amount or concentration of 3-hydroxybutyrate in a sample, and a device for determining the amount or concentration of 3-hydroxybutyrate in a sample.

Mutant 3-hydroxybutyrate dehydrogenase fromas well as methods and uses involving the same

The present disclosure relates to a mutant 3-hydroxybutyrate dehydrogenase (3-HBDH) with improved performance relative to the wild-type 3-HBDH, a nucleic acid encoding the mutant 3-HBDH, a cell having the mutant 3-HBDH or the nucleic acid, and/or a method of determining the amount or concentration of 3-hydroxybutyrate in a sample. Also disclosed is the use of the mutant 3-HBDH for determining the amount or concentration of 3-hydroxybutyrate in a sample, and a device for determining the amount or concentration of 3-hydroxybutyrate in a sample.

Mutant 3-hydroxybutyrate dehydrogenase from alcaligenes faecalis as well as methods and uses involving the same

A mutant of PQQ-dependent soluble glucose dehydrogenase (s-GDH; EC 1.1.5.2) is provided with improved specificity for glucose as compared to maltose, having a substitution of threonine at position 348 by either glycine, alamine or serine, wherein said mutant additionally comprises, at least one mutation for improving the stability of the mutant and one or more mutation(s) for improving the affinity of the mutant to glucose, and/or one or more mutation(s) for further improving the specificity of the mutant for glucose as compared to maltose, and wherein position 348 correspond to the amino acid positions known from thes-GDH wild-type sequence. Also disclosed are genes encoding such mutant s-GDH, and different applications of these s-GDH mutants, particularly for determining the concentration of glucose in a sample.

Mutants of pyrroloquinoline quinone dependent soluble glucose dehydrogenase

The present invention relates to improved variants of soluble pyrroloquinoline quinone (PQQ)-dependent glucose dehydrogenases (s-GDH), to genes encoding mutated s-GDH, to mutant proteins of s-GDH with improved substrate specificity for glucose, and to different applications of these s-GDH variants, particularly for determining concentrations of sugar, especially of glucose in a sample.

Forms of soluble pyrroloquinoline quinone-dependent glucose dehydrogenase

Growing community of inventors

Penzberg, Germany

Daniela Beck