Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.5.3.1 extracted from

  • Moriguchi, T.; Ida, K.; Hikima, T.; Ueno, G.; Yamamoto, M.; Suzuki, H.
    Channeling and conformational changes in the heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96 (2010), J. Biochem., 148, 491-505.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
complexed with methylthioacetate, pyrrole 2-carboxylate and sulfite, and sarcosine-reduced enzyme. Sarcosine oxidase comprises alpha-, beta-, gamma- and delta-subunits, FAD and FMN cofactors, and a large internal cavity. Methylthioacetate and pyrrole 2-carboxylate are sandwiched between the re-face of the FAD isoalloxazine ring and the beta-subunit C-terminal residues. Reduction of flavin cofactors shifts the beta-subunit A1 residue towards the alpha-subunit M55, forming a surface cavity at the oxygen-channel vestibule and rendering the beta-subunit C-terminal residues mobile. Three channels connect the cavity and the enzyme surface. Two of them exist in the inter-subunit space between alpha- and beta-subunits, and the substrate sarcosine seems to enter the active site through either of these channels and reaches the reside of the FAD isoalloxazine ring by traversing the mobile beta-subunit C-terminal residues. The third channel goes through the alpha-subunit and has a folinic acid-binding site Corynebacterium sp.

Organism

Organism UniProt Comment Textmining
Corynebacterium sp.
-
-
-