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Literature summary for 1.5.3.1 extracted from

  • Chen, Z.W.; Hassan-Abdulah, A.; Zhao, G.; Jorns, M.S.; Mathews, F.S.
    Heterotetrameric sarcosine oxidase: structure of a diflavin metalloenzyme at 1.85 A resolution (2006), J. Mol. Biol., 360, 1000-1018.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
alpha subunit contains NAD+ and putative folate binding site. The FAD binding site is in the beta subunit, FMN is bound at the interface of the alpha and beta subunit. A zinc ion, coordinated by three cysteine and one histidine side-chains, is bound to the delta subunit Stenotrophomonas maltophilia

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+
-
Stenotrophomonas maltophilia

Organism

Organism UniProt Comment Textmining
Stenotrophomonas maltophilia
-
-
-

Subunits

Subunits Comment Organism
heterotetramer crystallization data Stenotrophomonas maltophilia

Cofactor

Cofactor Comment Organism Structure
FAD
-
Stenotrophomonas maltophilia
FMN
-
Stenotrophomonas maltophilia
NAD+
-
Stenotrophomonas maltophilia