Inhibition of microbial β-N-acetylhexosaminidases by 4-deoxy- and galacto-analogues of NAG-thiazoline |
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| Institution: | 1. Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, CZ 14220 Praha 4, Czech Republic;2. Department of Biochemistry and Microbiology, Institute of Chemical Technology Prague, Technická 5, CZ 16628 Praha 6, Czech Republic;1. Department of Chemical Engineering, Federal University of São Carlos-UFSCar, Rodovia Washington Luiz, km 235, São Carlos, SP 13565-905, Brazil;2. Institute of Chemistry, São Paulo State University-UNESP, Rua Prof. Francisco Degni s/n, Araraquara, SP 14800-900, Brazil;3. Department of Physics, Federal University of São Carlos-UFSCar, Rodovia Washington Luiz, km 235, São Carlos, SP, 13565-905, Brazil;1. TEDA Institute of Biological Sciences and Biotechnology, Nankai University, 23 Hongda Street, Tianjin 300457, China;2. N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, 119991 Moscow, Russian Federation;3. The Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, Tianjin, China;4. Tianjin Key Laboratory of Microbial Functional Genomics, Tianjin, China;5. State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China;2. Murcia Biomedical Research Institute (IMIB), 30120 Murcia, Spain;1. Department of Food Science & Biotechnology, College of BioNano Technology, Gachon University, Seongnam, Republic of Korea;2. Department of Food Science & Technology, BK21+ Project Team, and Carbohydrate Bioproduct Research Center, Sejong University, Seoul, Republic of Korea;3. Department of Radiology and Imaging Sciences, Indiana University, School of Medicine, Indianapolis, IN, USA;4. Graduate School of Biotechnology, and Institute of Life Science and Resources, Kyung Hee University, Yongin, Republic of Korea;5. Whistler Center for Carbohydrate Research and Department of Food Science, Purdue University, West Lafayette, IN, USA |
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| Abstract: | NAG-thiazoline is a well-established competitive inhibitor of two physiologically relevant glycosidase families—β-N-acetylhexosaminidases (GH20) and β-N-acetylglucosaminidases (GH84). Based on the different substrate flexibilities of these enzyme groups, we designed and synthesized the 4-deoxy derivative of NAG-thiazoline aiming at the selective inhibition of GH20 β-N-acetylhexosaminidases. One GH84 and two GH20 microbial glycosidases were employed as model enzymes for the inhibition assays. Surprisingly, the new compound 4-deoxy-thiazoline exhibited no activity inhibition with either of the enzyme families of interest. Unlike with the substrates, the 4-hydroxyl group of the inhibitor’s sugar ring seems to be crucial for binding the inhibitor to the active sites of these enzymes. |
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| Keywords: | NAG-thiazoline Enzyme inhibition |
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