期刊
JOURNAL OF INORGANIC BIOCHEMISTRY
卷 111, 期 -, 页码 187-194出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2012.02.011
关键词
Enolase; Homodimer asymmetry; Heteroinhibition; Active site cooperativity
资金
- NIH [CA 76560]
- U.S. Department of Energy, Office of Basic Energy Sciences [W-31-109-Eng-38]
In the presence of magnesium, enolase catalyzes the dehydration of 2-phospho-D-glycerate (PGA) to phosphoenolpyruvate (PEP) in glycolysis and the reverse reaction in gluconeogensis at comparable rates. The structure of human neuron specific enolase (hNSE) crystals soaked in PGA showed that the enzyme is active in the crystals and produced PEP; conversely soaking in PEP produced PGA. Moreover, the hNSE dimer contains PGA bound in one subunit and PEP or a mixture of PEP and PGA in the other. Crystals soaked in a mixture of competitive inhibitors tartronate semialdehyde phosphate (TSP) and lactic acid phosphate (LAP) showed asymmetry with TSP binding in the same site as PGA and LAP in the PEP site. Kinetic studies showed that the inhibition of NSE by mixtures of TSP and LAP is stronger than predicted for independently acting inhibitors. This indicates that in some cases inhibition of homodimeric enzymes by mixtures of inhibitors (heteroinhibition) may offer advantages over single inhibitors. (C) 2012 Elsevier Inc. All rights reserved.
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