An essential arginyl residue in yeast hexokinase |
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| Affiliation: | 1. Department of Ophthalmology and Visual Sciences, Moran Eye Center, University of Utah School of Medicine, 65 Mario Capecchi Drive, Salt Lake City, UT, 84132, USA;2. Macular Pigment Research Group, Vision Research Centre, School of Health Science, Carriganore House, Waterford Institute of Technology West Campus, Carriganore, Waterford, Ireland;1. Department of Chemistry, Indian Institute of Technology Patna, Bihta, Patna, 801106, India;2. Department of Chemistry, National Institute of Technology Patna, Ashok Rajpath, Patna, 800005, Bihar, India |
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| Abstract: | The inactivation of yeast hexokinase A (ATP:d-hexose 6-phosphotransferase, EC 2.7.1.1) by phenylglyoxal obeys pseudo first-order kinetics. Formation of a reversible enzyme-reagent complex prior to modification is suggested by the observed saturation kinetics. Loss of activity correlates with the incorporation of 1 mol of [14C]phenylglyoxal per mol 50 000 dalton subunit. No significant conformational occurs concomitantly. Inactivation is attributable to modification of an arginyl residue. The pattern of protection by substrates and analogs favors an interaction of this essential residue with the terminal phosphoryl group of ATP or glucose 6-phosphate. |
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