Sarcosine oxidase

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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. Monomeric SOX uses FAD as cofactor. Heterotetrameric SOX uses FAD and FMN as cofactors.
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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.
==3D structures of sarcosine oxidase==
==3D structures of sarcosine oxidase==
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**[[2gag]], [[2gah]] – SOX + furoic acid – ''Stenotrophomonas maltophilia''
**[[2gag]], [[2gah]] – SOX + furoic acid – ''Stenotrophomonas maltophilia''
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:53, 23 August 2016

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[1]. Monomeric SOX uses FAD as cofactor. Heterotetrameric SOX uses FAD and FMN as cofactors.

3D structures of sarcosine oxidase

Updated on 23-August-2016

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

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Michal Harel, Alexander Berchansky

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