The Chemical Mechanism of D-1-Deoxyxylulose-5-phosphate Reductoisomerase from Escherichia coli

Find the way: 3‐[2H]‐ and 4‐[2H]‐labeled 1‐deoxyxylulose‐5‐phosphate were synthesized and used to investigate the chemical mechanism of 1‐deoxyxylulose‐5‐phosphate reductoisomerase (DXR) from E. coli. The observation of inverse secondary kinetic isotope effects for both labeled substrates indicates...

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Veröffentlicht in:	Angewandte Chemie International Edition 2007-01, Vol.46 (26), p.4926-4929
Hauptverfasser:	Wong, Ursula, Cox, Russell J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Aldose-Ketose Isomerases - chemistry Aldose-Ketose Isomerases - metabolism Catalysis enzymes Escherichia coli Escherichia coli - enzymology isotopic labeling kinetic isotope effects Kinetics Molecular Structure Multienzyme Complexes - chemistry Multienzyme Complexes - metabolism Oxidoreductases - chemistry Oxidoreductases - metabolism reaction mechanisms Stereoisomerism Substrate Specificity Valine - chemistry Valine - metabolism
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Beschreibung
Zusammenfassung:	Find the way: 3‐[2H]‐ and 4‐[2H]‐labeled 1‐deoxyxylulose‐5‐phosphate were synthesized and used to investigate the chemical mechanism of 1‐deoxyxylulose‐5‐phosphate reductoisomerase (DXR) from E. coli. The observation of inverse secondary kinetic isotope effects for both labeled substrates indicates that DXR uses a retro‐aldol/aldol mechanism in which the recombination reaction is the rate‐limiting step (see scheme).
ISSN:	1433-7851 1521-3773
DOI:	10.1002/anie.200700647