Arkray, Inc.

Ultizyme International Ltd.

Roche Diagnostics Operations, Inc.

Roche Diabetes Care, Inc.

I-Sens, Inc.

Ultizymer International, Ltd.

Roche Diagnostics Gmbh

F. Hoffmann-La Roche Ag

Bioengineering Laboratories, LLC

Katsuhiro Kojima

Kazushige Mori

Koji Sode

Junko Shimazaki

Sode Koji

Youngjea Kang

The purpose of the present invention is to provide a fungus-derived FADGDH that has a direct electron transfer ability. Provided is a fusion protein comprising a fungus-derived FADGDH or a mutant thereof and a cytochrome molecule connected to the N-terminus of the FADGDH or variant thereof.

Fusion protein of flavin adenine dinucleotide-glucose dehydrogenase and cytochrome molecule

By using a mutant glucose oxidase comprising an amino acid sequence in which a residue corresponding to isoleucine at position 489 or arginine at position 335 in the amino acid sequence of SEQ ID NO:1 is substituted with an amino acid residue having a reactive functional group in a side chain, and binding an electron acceptor to the mutant glucose oxidase through the amino acid residue having a reactive functional group, an electron acceptor-modified glucose oxidase is obtained.

Mutant glucose oxidase and use thereof

A mutant cytochrome protein originated from a cytochrome protein having three heme-binding domains, which mutant cytochrome protein lacks the first heme-binding domain and the second heme-binding domain as counted from the N-terminus, is provided. The mutant cytochrome protein may lack a region(s) containing the first and second heme-binding domains.

Mutant cytochrome protein lacking certain heme domains and use thereof

Mutant cytochrome protein and use thereof

The present invention provides a mutant-type glucose dehydrogenase having glucose dehydrogenase activity and having decreased reactivity with xylose, wherein said mutant-type glucose dehydrogenase comprises a mutant-type &#x3b1;-subunit comprising an amino acid sequence of 520 to 550 amino acids comprising an amino acid sequence of 520 to 550 amino acids comprising SEQ ID NO: 21, SEQ ID NO: 22, SEQ ID NO: 23, SEQ ID NO: 24 and SEQ ID NO: 25 in this order from N-terminus to C-terminus, except that one or more amino acid residue(s) selected from the group consisting of the glycine at position 10 in SEQ ID NO: 23, the histidine at position 4 in SEQ ID NO: 24, and the asparagine at position 4 in SEQ ID NO: 25 is/are substituted with another/other amino acid(s).

Mutant-type glucose dehydrogenase and use thereof

Compositions, devices, kits and methods are disclosed for assaying cholesterol with a cholesterol oxidase mutant that has been modified at an amino acid residue involved in the active site. The cholesterol oxidase mutant has reduced oxidase activity while substantially maintaining its dehydrogenase activity.

Cholesterol oxidase mutants, compositions, devices, kits and uses thereof

Compositions, devices, kits and methods are disclosed for assaying glucose with a glucose oxidase mutant that has been modified at an amino acid residue involved in the active site. The glucose oxidase mutant has reduced oxidase activity while substantially maintaining its dehydrogenase activity.

Growing community of inventors

Tokyo, Japan

Katsuhiro Kojima