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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
44
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pubmed:dateCreated |
1992-12-8
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pubmed:abstractText |
Lysine 2,3-aminomutase from Clostridia catalyzes the interconversion of L-alpha-lysine with L-beta-lysine. The purified enzyme contains iron-sulfur ([Fe-S]) clusters, pyridoxal phosphate, and Co(II) [Petrovich, R. M., Ruzicka, F. J., Reed, G. H., & Frey, P. A. (1991) J. Biol. Chem. 266, 7656-7660]. Enzymatic activity depends upon the presence and integrity of these cofactors. In addition, the enzyme is activated by S-adenosylmethionine, which participates in the transfer of a substrate hydrogen atom between carbon-3 of lysine and carbon-2 of beta-lysine [Moss, M., & Frey, P. A. (1987) J. Biol. Chem. 262, 14859-14862]. This paper describes the electron paramagnetic resonance (EPR) properties of the [Fe-S] clusters. Purified samples of the enzyme also contain low and variable levels of a stable radical. The radical spectrum is centered at g = 2.006 and is subject to inhomogeneous broadening at 10 K, with a p1/2 value of 550 +/- 100 microW. The low-temperature EPR spectrum of the [Fe-S] cluster is centered at g = 2.007 and undergoes power saturation at 10 K in a homogeneous manner, with a p1/2 of 15 +/- 2 mW. The signals are consistent with the formulation [4Fe-4S] and are adequately simulated by a rhombic spectrum, in which gxx = 2.027, gyy = 2.007, and gzz = 1.99. Treatment of the enzyme with reducing agents converts the cluster into an EPR-silent form. Oxidation of the purified enzyme by air or ferricyanide converts the [Fe-S] complex into a species with an EPR spectrum that is consistent with the formulation [3Fe-4S].(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Dithionite,
http://linkedlifedata.com/resource/pubmed/chemical/Ferricyanides,
http://linkedlifedata.com/resource/pubmed/chemical/Free Radicals,
http://linkedlifedata.com/resource/pubmed/chemical/Intramolecular Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/Iron-Sulfur Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/hexacyanoferrate III,
http://linkedlifedata.com/resource/pubmed/chemical/lysine 2,3-aminomutase
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
31
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
10774-81
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1329954-Amino Acid Isomerases,
pubmed-meshheading:1329954-Dithionite,
pubmed-meshheading:1329954-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:1329954-Enzyme Activation,
pubmed-meshheading:1329954-Ferricyanides,
pubmed-meshheading:1329954-Free Radicals,
pubmed-meshheading:1329954-Intramolecular Transferases,
pubmed-meshheading:1329954-Iron-Sulfur Proteins,
pubmed-meshheading:1329954-Macromolecular Substances,
pubmed-meshheading:1329954-Oxidation-Reduction
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pubmed:year |
1992
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pubmed:articleTitle |
Characterization of iron-sulfur clusters in lysine 2,3-aminomutase by electron paramagnetic resonance spectroscopy.
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pubmed:affiliation |
Institute of Enzyme Research, Graduate School, University of Wisconsin, Madison 53705.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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