Sarcosine oxidase
From Proteopedia
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| - | {{STRUCTURE_3ad8| PDB=3ad8 | SIZE=400| SCENE= |right|CAPTION= | + | {{STRUCTURE_3ad8| PDB=3ad8 | SIZE=400| SCENE= |right|CAPTION=Heterotetramer of sarcosine oxidase containing FAD, FMN and NAD showing α subunit (grey), β subunit (green), γ subunit (pink) and δ subunit (yellow). Complex with pyrrole-2-carboxylate, sulfate and Zn+2 ions, [[3ad8]] }} |
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Revision as of 09:23, 15 November 2012
Template:STRUCTURE 3ad8 Sarcosine oxidase (SOX) catalyzes the demethylation of sarcosine+O2+H4-tetrahydrofolate to produce glycine, hydrogen peroxide and 5, 10-methylene-tetrahydrofolate. Sarcosine metabolism can be the source of carbon and energy for many microorganisms. SOXs are found as monomers, heterodirmers and heterotetramers. Monomeric SOX uses FAD as cofactor. Heterotetrameric SOX uses FAD and FMN as cofactors.
3D structures of sarcosine oxidase
SOX monomer
1el5, 1el7, 1el8, 1eli, 2gf3 – BaSOX + inhibitor – Bacillus
1l9c, 1l9d, 1l9e, 3bhf, 3bhk, 3m0o, 3m12, 3m13 – BaSOX (mutant)
2a89, 2gb0, 1zov - BaSOX
SOX heterotetramer
1vrg – CoSOX + folinic acid – Corynebacterium
3ad7 – CoSOX + methylthio acetate
3ad8 – CoSOX + pyrrole 2-carboxylate
3ada – CoSOX + sulfite
1x31, 3ad9 – CoSOX
2gag, 2gah – SOX + furoic acid – Stenotrophomonas maltophilia
