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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1977-1-28
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pubmed:abstractText |
The nature of the feedback inhibition of the bifunctional enzyme, aspartokinase I-homoserine dehydrogenase I of Escherichia coli was studied using 13C nuclear magnetic resonance (NMR). Since aspartokinase is activated by Mn(II), the interaction of the inhibitor L-threonine (specifically enriched to 90% 13C in the carboxyl carbon) with the metal-enzyme complex was studied. Spin-lattice (T1) and spin-spin (T2) relaxation times were determined by the partially relaxed Fourier transform method and line-width measurements respectively at 20 MHz. The pronounced broadening of the DL-threonine carboxyl peak in the presence of the Mn(II)-enzyme complex indicates that an L-threonine binding site is close to the metal binding site of the kinase active site. The non-identity of (T1)*M and (T2)*M indicates that conditions of fast exchange prevail. The (T1)*M/(T2)*M ratio was used to estimate a correlation time of 2.0 ns for the dipolar interaction at 25 degrees C. An estimate for the distance between Mn(II) and the threonine carboxyl carbon of 4.4 A (0.44 nm) was obtained. This 13C NMR study has thus located one of the two classes of threonine regulatory sites which exist per subunit; the threonine site identified here is at the aspartokinase active site, adjacent to the catalytic metal site.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
69
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
249-55
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:186263-Aspartate Kinase,
pubmed-meshheading:186263-Binding Sites,
pubmed-meshheading:186263-Escherichia coli,
pubmed-meshheading:186263-Feedback,
pubmed-meshheading:186263-Fourier Analysis,
pubmed-meshheading:186263-Kinetics,
pubmed-meshheading:186263-Magnetic Resonance Spectroscopy,
pubmed-meshheading:186263-Manganese,
pubmed-meshheading:186263-Mathematics,
pubmed-meshheading:186263-Phosphotransferases,
pubmed-meshheading:186263-Protein Binding,
pubmed-meshheading:186263-Protein Conformation,
pubmed-meshheading:186263-Temperature,
pubmed-meshheading:186263-Threonine
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pubmed:year |
1976
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pubmed:articleTitle |
Nuclear-magnetic-relaxation studies of the interaction of inhibitor with the threonine-sensitive aspartokinase of Escherichia coli.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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