How an enzyme tames reactive intermediates: Positioning of the active-site components of lysine 2,3-aminomutase during enzymatic turnover as determined by ENDOR spectroscopy

Journal of the American Chemical Society

Volumn 128, Issue 31, 2006, Pages 10145-10154

  Lees, Nicholas S ^a   Chen, Dawei ^b   Walsby, Charles J ^c   Behshad, Elham ^b   Frey, Perry A ^b   Hoffman, Brian M ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

^c SIMON FRASER UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; FREE RADICALS; HYDROGEN; SPECTROSCOPIC ANALYSIS; SUBSTRATES;

4-THIA-L-LYSINE (SLYS); HYDROGEN ATOM TRANSFER; LYSINE 2,3-AMINOMUTASE (LAM); TRANS-4,5-DEHYDRO-L-LYSINE (DHLYS);

ENZYMES;

DEOXYADENOSINE; LYSINE; LYSINE 2,3 AMINOMUTASE; MUTASE; PYRIDOXAL 5 PHOSPHATE; RADICAL; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CLUSTER ANALYSIS; CRYSTAL STRUCTURE; DRUG DETERMINATION; ELECTRON NUCLEAR DOUBLE RESONANCE; ELECTRON TRANSPORT; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; ISOMERISM; PROTON TRANSPORT;

BINDING SITES; INTRAMOLECULAR TRANSFERASES; MODELS, MOLECULAR; SPECTRUM ANALYSIS;

EID: 33746918356     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja061282r     Document Type: Article

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