Sarcosine oxidase

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{{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 (grey), [[3ad8]] }}
 
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'''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<ref>PMID:24185971</ref>. Monomeric SOX uses FAD as cofactor. Heterotetrameric SOX uses FAD and FMN as cofactors.
 
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<StructureSection load='3ad8' size='450' side='right' scene='' 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 (grey) [[3ad8]]'>
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'''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<ref>PMID:24185971</ref>. Monomeric SOX uses FAD as cofactor. Heterotetrameric SOX uses FAD and FMN as cofactors.
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</StructureSection>
==3D structures of sarcosine oxidase==
==3D structures of sarcosine oxidase==

Revision as of 21:47, 2 October 2017

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 (grey) 3ad8

Drag the structure with the mouse to rotate

3D structures of sarcosine oxidase

Updated on 02-October-2017

References

  1. ↑ Suzuki H. Sarcosine oxidase: structure, function, and the application to creatinine determination. Amino Acids. 1994 Feb;7(1):27-43. doi: 10.1007/BF00808444. PMID:24185971 doi:http://dx.doi.org/10.1007/BF00808444

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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