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Featured researches published by Osao Adachi.


Analytical Biochemistry | 1985

Method of enzymatic determination of pyrroloquinoline quinone

Minoru Ameyama; Masatsugu Nonobe; Emiko Shinagawa; Kazunobu Matsushita; Osao Adachi

An improved enzymatic method for the determination of pyrroloquinoline quinone, a novel prosthetic group of some important oxidoreductases, has been developed with cytoplasmic membrane of Escherichia coli K-12, in which D-glucose dehydrogenase (EC 1.1.99.17) was completely resolved to apo-enzyme by EDTA treatment. Incubation of the EDTA-treated membrane with exogenous pyrroloquinoline quinone in the presence of magnesium ions gave a quantitative determination of pyrroloquinoline quinone by assaying the restored D-glucose dehydrogenase activity. This novel enzymatic method was confirmed to be highly reproducible up to 10 ng of pyrroloquinoline quinone and could be applied to a routine assay of pyrroloquinoline quinone.


Clinica Chimica Acta | 1985

Determination of seminal fructose using d-fructose dehydrogenase

Koji Nakashima; Hitoshi Takei; Osao Adachi; Emiko Shinagawa; Minoru Ameyama

Seminal plasma, the liquid component of semen, is mainly secreted from the seminal vesicles and is characterized by relatively high concentrations of fructose and extremely low concentrations of glucose [l]. Fructolysis is a main energy source for sperm. Thus, assay of seminal fructose can provide information concerning the activity of the seminal vesicles and the condition of the ejaculatory ducts [2]. Various disorders of these organs may be responsible for cases of infertility [a]. Determination of seminal fructose has been done by paper chromatography 131, gas chromatography [4], calorimetry [S] and enzymic methods 1671. We describe an enzymic method for seminal fructose using bacterial membranebound D-fructose dehydrogenase (E.C. 1.1.99.11) [8.9].


Biochemical and Biophysical Research Communications | 1986

The 9-carboxyl group of pyrroloquinoline quinone, a novel prosthetic group, is essential in the formation of holoenzyme of D-glucose dehydrogenase

E Shinagawa; Kazunobu Matsushita; Masatsugu Nonobe; Osao Adachi; Minoru Ameyama; Yoshiki Ohshiro; Sinobu Itoh; Yutaka Kitamura

Availability of different analogues of pyrroloquinoline quinone as the prosthetic group for apo-D-glucose dehydrogenase was examined. The 9-carboxyl group of pyrroloquinoline quinone was shown to be essential for the reconstitution of the enzyme activity. Although the carboxyl group may not be involved in catalytic function, it is quite probable to contribute the binding of the prosthetic group to apoenzyme.


Archive | 2016

Membrane-Bound Dehydrogenases of Acetic Acid Bacteria

Osao Adachi; Toshiharu Yakushi

One of the major key features of acetic acid bacteria is their strong oxidation ability of alcohols and sugars, resulting in quantitative production of oxidized compounds. Respiratory chains consisting of ubiquinone, terminal ubiquinol oxidase, and several primary membrane-bound dehydrogenases are responsible for this unique ability. Here, we describe recent progress in the understanding of enzymatic and molecular properties and biogenesis of the membrane-bound dehydrogenases, such as pyrroloquinoline quinone-dependent alcohol dehydrogenase–cytochrome complex, and recent findings on new membrane-bound dehydrogenases. Quinate oxidation by quinate dehydrogenase (QDH) of acetic acid bacteria is a key agent in the vitro shikimate production process composed of the membranes containing QDH and 3-dehydroquinate dehydratase and NADP+-dependent shikimate dehydrogenase. The addition of a catalytic amount of NADP+ and an NADPH-regeneration system drive the process forward to produce shikimate with almost 100 % yield. The pentose oxidation respiratory chain produces 4-keto-d-arabonate or 4-keto-d-ribonate, depending on the substrate. Novel three different membrane-bound enzymes are indicated: d-aldopentose 4-dehydrogenase, 4-keto-d-aldopentose 1-dehydrogenase, and d-pentonate 4-dehydrogenase.


Agricultural and biological chemistry | 1985

Solubilization, Purification and Properties of Membrane-bound Glycerol Dehydrogenase from Gluconobacter industrius

Minoru Ameyama; Emiko Shinagawa; Kazunobu Matsushita; Osao Adachi


Journal of Bacteriology | 1987

Reconstitution of pyrroloquinoline quinone-dependent D-glucose oxidase respiratory chain of Escherichia coli with cytochrome o oxidase.

Kazunobu Matsushita; Masatsugu Nonobe; E Shinagawa; Osao Adachi; M Ameyama


Agricultural and biological chemistry | 1986

Purification and Characterization of the Quinoprotein d-Glucose Dehydrogenase Apoenzyme from Escherichia coli

Minoru Ameyama; Masatsugu Nonobe; Emiko Shinagawa; Kazunobu Matsushita; Koichi Takimoto; Osao Adachi


Agricultural and biological chemistry | 1985

Mode of Binding of Pyrroloquinoline Quinone to Apo-glucose Dehydrogenase

Minoru Ameyama; Masatsugu Nonobe; Masaharu Hayashi; Emiko Shinagawa; Kazunobu Matsushita; Osao Adachi


Agricultural and biological chemistry | 1985

Growth Stimulating Activity for Microorganisms in Naturally Occurring Substances and Partial Characterization of the Substance for the Activity as Pyrroloquinoline Quinone

Minoru Ameyama; Emiko Shinagawa; Kazunobu Matsushita; Osao Adachi


Fems Microbiology Letters | 1986

Immunological evidence for two types of PQQ‐dependent d‐glucose dehydrogenase in bacterial membranes and the location of the enzyme in Escherichia coli

Kazunobu Matsushita; Emiko Shinagawa; Taketo Inoue; Osao Adachi; M Ameyama

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Koji Nakashima

St. Luke's College of Nursing

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