| Co-Investigator(Kenkyū-buntansha) |
MORIGUCHI Mituaki Ohita Univ., Dept. Eng., Prof., 工学部, 教授 (70026574)
KATO Nobuo Tottori Univ., Dept. Eng., Prof., 工学部, 教授 (50026556)
KODAMA Tohru Tokyo Univ., Dept. Agr., Prof., 農学部, 教授 (30011901)
SODA Kenji Kyoto Univ., Res. Inst. Chem., Prof., 化学研究所, 教授 (30027023)
AMEYAMA Minoru Kansai Univ., Dept. Eng., Prof., 工学部, 教授 (90022053)
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| Research Abstract |
The following enzymes have been treated to see whether they contain PQQ as cofactor : amine dehydrogenase, alcohol dehydrogenase, aldehyde dehydrogenase, phenylalanine ammonia-lyase, glutamate decarboxylase, ketoglutarate decarboxylase, lipoxygenase, tryptophan pyrrolase, amine oxidase, alcohol oxidase, p-hydroxybenzoate hydroxylase, dihydroxybenzoate decarboxylase, sarcosine dehydroginase, choline dehydrogenase, benzylamine oxidase, nitoralkane oxidase, nitrile hydratase, haloamino acid dehalogenase, aromatic alcohol dehydrogenase, sencondary alcohol dehydrogenase, polyethyleneglycol dehydrogenase, aniline decomposing enzyme, lignin decomposing enzyme, dinitrilehydratase, methanol dehvdrogenase, and so an. The enzyme sources for these enzymes were variable arranging from eucaryotes to procarytes. More than 50% of these enzymes have been confirmed to be quinoprotein.
Metabolic pathway involving PQQ was indicated in hydrogcnobacteria, cyanocobalamin biosynthesis, germination of pollen for the first time in this study. Importance of PQQ in various aspects of substrate metabolism has been emphasized through the present co-operative research.
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