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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2003-6-25
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pubmed:abstractText |
The diverse reactions catalyzed by the radical-SAM superfamily of enzymes are thought to proceed via a set of common mechanistic steps, key among which is the reductive cleavage of S-adenosyl-L-methionine (SAM) by a reduced [4Fe-4S] cluster to generate an intermediate deoxyadenosyl radical. A number of spectroscopic studies have provided evidence that SAM interacts directly with the [4Fe-4S] clusters in several of the radical-SAM enzymes; however, the molecular mechanism for the reductive cleavage has yet to be elucidated. Selenium X-ray absorption spectroscopy (Se-XAS) was used previously to provide evidence for a close interaction between the Se atom of selenomethionine (a cleavage product of Se-SAM) and an Fe atom of the [4Fe-4S] cluster of lysine-2,3-aminomutase (KAM). Here, we utilize the same approach to investigate the possibility of a similar interaction in pyruvate formate-lyase activating enzyme (PFL-AE) and biotin synthase (BioB), two additional members of the radical-SAM superfamily. The results show that the latter two enzymes do not exhibit the same Fe-Se interaction as was observed in KAM, indicating that the methionine product of reductive cleavage of SAM does not occupy a well-defined site close to the cluster in PFL-AE and BioB. These results are interpreted in terms of the differences among these enzymes in their use of SAM as either a cofactor or a substrate.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-10403368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-10708574,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-10747808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-10766431,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-11123891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-11222759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-11315557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-11395404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-11578923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-11683640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-11829592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-11902903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-12236732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-12440894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-3117791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-6369325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-8135930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-8142361,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-8554581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-9022980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-9235882,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-9240449,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-9305874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-9305972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-9428635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-9478932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12824504-9485408
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Coenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Iron-Sulfur Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Methionine,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/S-Adenosylmethionine,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfurtransferases,
http://linkedlifedata.com/resource/pubmed/chemical/adhE protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/biotin synthetase,
http://linkedlifedata.com/resource/pubmed/chemical/pyruvate formate-lyase activating...
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1573-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12824504-Alcohol Dehydrogenase,
pubmed-meshheading:12824504-Aldehyde Oxidoreductases,
pubmed-meshheading:12824504-Coenzymes,
pubmed-meshheading:12824504-Enzyme Activation,
pubmed-meshheading:12824504-Enzymes,
pubmed-meshheading:12824504-Escherichia coli Proteins,
pubmed-meshheading:12824504-Iron,
pubmed-meshheading:12824504-Iron-Sulfur Proteins,
pubmed-meshheading:12824504-Lysine,
pubmed-meshheading:12824504-Methionine,
pubmed-meshheading:12824504-Multienzyme Complexes,
pubmed-meshheading:12824504-S-Adenosylmethionine,
pubmed-meshheading:12824504-Spectrometry, X-Ray Emission,
pubmed-meshheading:12824504-Spectrum Analysis,
pubmed-meshheading:12824504-Substrate Specificity,
pubmed-meshheading:12824504-Sulfurtransferases
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pubmed:year |
2003
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pubmed:articleTitle |
Structural studies of the interaction of S-adenosylmethionine with the [4Fe-4S] clusters in biotin synthase and pyruvate formate-lyase activating enzyme.
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pubmed:affiliation |
Department of Chemistry, University of Georgia, Athens, GA 30602-2556, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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