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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
1994-10-4
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pubmed:abstractText |
Many and diverse modifications of the myosin subfragment 1 (S-1) increase (modulate) its ATPase activity, including interaction of this particle with actin; a recent addition to these modifications is the extensive lysine modification of S-1 that seems prerequisite to crystallizing it for structure analysis. In this study we first established kinetically the ATPase modulations induced by various treatments of the myosin S-1 enzyme, and we also measured two properties of the S-1 active site--the affinity with which the site binds (a fluorescent analog of) the enzymatic nucleotide product and the access that a fluorescence quencher has to the bound ADP product--in an effort to get at the mechanism of modulation. Modulations achieved by substituting Ca2+ for the normal Mg2+ cocatalyst or by substituting Cl- for the normal carboxylate anion seem due to the product being held more loosely by the modulated enzyme. In other illustrative modulations (lysine methylation, or alkylation of Cys-707, or transition from neutral pH to pH 9.2) nucleotide product affinity and access to quencher do change, but not in a pattern explained simply by a lifting of product inhibition. Lysine methylation results in weaker binding of nucleotide product.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-13295220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-14163781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-14229661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-159070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-1946397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-4243908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-4285658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-6218804,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-6237680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-6480589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-651665,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-7277493,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-8175707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-8316857,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-8316858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-8373783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8078940-8373784
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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 |
Aug
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8665-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
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pubmed:year |
1994
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pubmed:articleTitle |
Effect of lysine methylation and other ATPase modulators on the active site of myosin subfragment 1.
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pubmed:affiliation |
Physiology Department, University of the Pacific, San Francisco, CA 94115.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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