Crystal structure of heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96

Journal Article · Fri Jul 29 04:00:00 EDT 2005 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2005.05.116· OSTI ID:20710869

Ida, Koh ^[1]; kitasato-u ac jp, E-mail: idakoh@sci; Moriguchi, Tomotaka ^[2]; Suzuki, Haruo ^[1]; kitasato-u ac jp, E-mail: suzuki@sci

---

1. Department of Biosciences, School of Science, Kitasato University, 1-15-1 Kitasato, Sagamihara, Kanagawa 228-8555 (Japan)
2. Division of Biosciences, Graduate School of Fundamental Life Science, Kitasato University, 1-15-1 Kitasato, Sagamihara, Kanagawa 228-8555 (Japan)

Sarcosine oxidase from Corynebacterium sp. U-96 is a heterotetrameric enzyme. Here we report the crystal structures of the enzyme in complex with dimethylglycine and folinic acid. The {alpha} subunit is composed of two domains, contains NAD{sup +}, and binds folinic acid. The {beta} subunit contains dimethylglycine, FAD, and FMN, and these flavins are approximately 10 A apart. The {gamma} subunit is in contact with two domains of {alpha} subunit and has possibly a folate-binding structure. The {delta} subunit contains a single atom of zinc and has a Cys{sub 3}His zinc finger structure. Based on the structures determined and on the previous works, the structure-function relationship on the heterotetrameric sarcosine oxidase is discussed.

• OSTI ID: 20710869
• Journal Information: Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 2 Vol. 333; ISSN BBRCA9; ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
CITROVORUM FACTOR
CRYSTAL STRUCTURE
ISOALLOXAZINES
NAD
OXIDASES
SARCOSINE
ZINC