Structure of L-arginine oxidase from Pseudomonas sp. TPU 7192
Author Information
Author(s): Yamaguchi Hiroki, Takahashi Kazutoshi, Numoto Nobutaka, Suzuki Hiroshi, Tatsumi Moemi, Kamegawa Akiko, Nishikawa Kouki, Asano Yasuhisa, Mizukoshi Toshimi, Miyano Hiroshi, Fujiyoshi Yoshinori, Sugiki Masayuki
Primary Institution: Ajinomoto Co. Inc.
Hypothesis
The study aims to elucidate the structure and substrate specificity of L-arginine oxidase (AROD) derived from Pseudomonas sp. TPU 7192.
Conclusion
The study reveals that PT-AROD has an octameric structure and high substrate specificity for L-arginine, with key residues influencing its selectivity.
Supporting Evidence
- PT-AROD was characterized using cryo-electron microscopy at a resolution of 2.3 Å.
- PT-AROD exhibits high substrate specificity, with 100% activity towards L-arginine.
- Mutations in specific residues significantly affect the substrate selectivity of PT-AROD.
Takeaway
Scientists studied an enzyme that helps measure a substance called L-arginine in the body, and they found out how its shape helps it work really well with L-arginine.
Methodology
The structure of PT-AROD was determined using cryo-electron microscopy and X-ray crystallography.
Digital Object Identifier (DOI)
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