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Cryo-EM SPA dataset of arginine oxidase from Pseudomonas sp. TRU 7192

ABSTRACT:

SUBMITTER: Hiroki Yamaguchi 

PROVIDER: EMPIAR-13426 | biostudies-other |

REPOSITORIES: biostudies-other

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Open and closed structures of L-arginine oxidase by cryo-electron microscopy and X-ray crystallography.

Yamaguchi Hiroki H   Takahashi Kazutoshi K   Numoto Nobutaka N   Suzuki Hiroshi H   Tatsumi Moemi M   Kamegawa Akiko A   Nishikawa Kouki K   Asano Yasuhisa Y   Mizukoshi Toshimi T   Miyano Hiroshi H   Fujiyoshi Yoshinori Y   Sugiki Masayuki M  

Journal of biochemistry 20250101 1

L-arginine oxidase (AROD, EC 1.4.3.25) is an oxidoreductase that catalyses the deamination of L-arginine, with flavin adenine dinucleotide (FAD) as a cofactor. Recently identified AROD from Pseudomonas sp. TPU 7192 (PT-AROD) demonstrates high selectivity for L-arginine. This enzyme is useful for accurate assays of L-arginine in biological samples. The structural characteristics of the FAD-dependent AROD, however, remain unknown. Here, we report the structure of PT-AROD at a resolution of 2.3 Å b  ...[more]

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