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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2006-9-12
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pubmed:abstractText |
Heterotetrameric sarcosine oxidase (TSOX) is a complex bifunctional flavoenzyme that contains two flavins. Most of the FMN in recombinant TSOX is present as a covalent adduct with an endogenous ligand. Enzyme denaturation disrupts the adduct, accompanied by release of a stoichiometric amount of sulfide. Enzyme containing>or=90% unmodified FMN is prepared by displacement of the endogenous ligand with sulfite, a less tightly bound competing ligand. Reaction of adduct-depleted TSOX with sodium sulfide produces a stable complex that resembles the endogenous TSOX adduct and known 4a-S-cysteinyl flavin adducts. The results provide definitive evidence for sulfide as the endogenous TSOX ligand and strongly suggest that the modified FMN is a 4a-sulfide adduct. A comparable reaction with sodium sulfide is not detected with other flavoprotein oxidases. A model of the postulated TSOX adduct suggests that it is stabilized by nearby residues that may be important in the electron transferase/oxidase function of the coenzyme.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-10220347,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-10368302,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-10708574,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-10913292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-10913293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-11170472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-11330998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-12501208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-12506204,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-13650640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-14299649,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-15248773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-15922624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-1657156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-2475174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-2565232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-3427080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-4382016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-4389773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-4705987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-6614472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-7543100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-7692961,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-8527444,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-8973328,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16934831-9485355
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
362
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
656-63
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16934831-Dithionitrobenzoic Acid,
pubmed-meshheading:16934831-Flavin Mononucleotide,
pubmed-meshheading:16934831-Methyl Methanesulfonate,
pubmed-meshheading:16934831-Models, Molecular,
pubmed-meshheading:16934831-Protein Structure, Quaternary,
pubmed-meshheading:16934831-Pseudomonas,
pubmed-meshheading:16934831-Sarcosine Oxidase,
pubmed-meshheading:16934831-Sulfhydryl Compounds,
pubmed-meshheading:16934831-Sulfides,
pubmed-meshheading:16934831-Sulfites
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pubmed:year |
2006
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pubmed:articleTitle |
Identification of a stable flavin-thiolate adduct in heterotetrameric sarcosine oxidase.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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