FRUCTOSE-6-PHOSPHATE KINASE

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Glycation is the reaction of glucose, fructose, or galactose with proteins that occurs primarily in the bloodstream and is the first step in a complex series of very slow reactions in the body leading to advanced glycation endproducts (AGEs). AGEs are frequently more reactive than the sugars they are derived from, and are implicated in many age-related chronic diseases including: type II diabetes, cardiovascular diseases, Alzheimer's disease, cancer, peripheral neuropathy, and sensory losses such as deafness and blindness.Deglycation enzymes repair the initial damage caused by glycation. At present very little is known about the structure of deglycation enzymes, how they recognize glycated proteins, and how they catalyse deglycation. As a model system, several enzymes that are involved in deglycation reactions in E. coli bacteria have been cloned, expressed and purified in milligrams amounts. Screens have identified crystallization conditions for several of these enzymes and are awaiting diffraction analyses for structure determination. One of these, the structure of a fructose-6-phosphate kinase which catalysis the first step in a deglycation pathway was recently solved to 2.1A resolution and is subject of on-going structural study.