Author Maemura, Tomomi| Uchitomi, Kumiko| Kusaka, Chika| Inagaki, Junko| Tamura, Takashi| Soda, Kenji| Inagaki, Kenji|
Published Date 2011-02-01
Publication Title 岡山大学農学部学術報告
Volume volume100
Content Type Departmental Bulletin Paper
Author Kobayashi, Fumiaki| Aomine, Hiroki| Mizunashi, Wataru| Yu, Fujio| Tamura, Takashi| Inagaki, Kenji|
Published Date 2012-02-01
Publication Title 岡山大学農学部学術報告
Volume volume101
Content Type Departmental Bulletin Paper
Author Nakai, Ryuichiro| Fujino, Shihoko| Utsumi, Tomohiro| Tamura, Takashi| Kusakabea, Hitoshi| Inagaki, Kenji|
Published Date 2014-02-01
Publication Title 岡山大学農学部学術報告
Volume volume103
Content Type Departmental Bulletin Paper
Author Oshima, Kenshiro| Hattori, Masahira| Shimizu, Hitomi| Fukuda, Koji| Nemoto, Michiko| Inagaki, Kenji| Tamura, Takashi|
Published Date 2015-07-09
Publication Title Genome Announcements
Volume volume3
Issue issue4
Content Type Journal Article
Author Tamura, Takashi| Tsunekawa, Naoki| Nemoto, Michiko| Inagaki, Kenji| Hirano, Toshiyuki| Sato, Fumitoshi|
Published Date 2016-01-28
Publication Title Scientific reports
Volume volume6
Content Type Journal Article
Author Tamura, T.| Ibi, T.| Inagaki, K.| Kubo, Y.| Okuda, K.|
Published Date 2016-02-01
Publication Title 岡山大学農学部学術報告
Volume volume105
Content Type Departmental Bulletin Paper
Title Alternative Recombinant expression and characterization of quinone-containing novel glycine oxidase from Marinomonas mediterranea
FullText URL srfa_109_001_006.pdf
Author Kajiyama, Yuki| Mizobata, Satsuki| Akaji, Shusaku| Nemoto, Michiko| Tamura, Takashi| Inagaki, Kenji|
Abstract  Novel glycine oxidase (GlyOX) from Marinomonas mediterranea depends on cysteine tryptophilquinone (CTQ) and catalyzes the oxidative deamination of glycine to produce a glyoxylate, ammonia, and hydrogen peroxide. M. mediterranea GlyOX genes (goxA and goxB) were cloned and recombinant GlyOX was heterologously expressed by E. coli. The purification of recombinant GlyOX was carried out by metal affinity and DEAE-Toyopearl 650M column chromatographies. M. mediterranea GlyOX was homotetramic with a molecular mass of 76kDa and showed optimum activity around 30°C and at pH 5.0, and stability below 50°C and between pH 5.0 to 9.0. M. mediterranea GlyOX shows a strict substrate specificity toward glycine, and the Michaelis constant for glycine was 0.5mM. M. mediterranea GlyOX could determine the quantity of glycine in human serum and human blood plasma with high sensitivity. This study revealed the catalytic and structural properties of M. mediterranea GlyOX with high substrate specificity.
Abstract Alternative , , ,
Keywords glycine oxidase Marinomonas mediterranea cysteine tryptophilquinone recombinant expression enzymatic glycine assay
Publication Title Scientific Reports of the Faculty of Agriculture, Okayama University
Published Date 2020-02-01
Volume volume109
Start Page 1
End Page 6
ISSN 2186-7755
language 日本語
File Version publisher