substrate promiscuity of n-acetylhexosamine 1-kinases衬底的滥交n-acetylhexosamine 1-kinases.pdfVIP

Molecules 2011, 16, 6396-6407; doi:10.3390/molecule OPEN ACCESS molecules ISSN 1420-3049 /journal/molecules Article Substrate Promiscuity of N-Acetylhexosamine 1-Kinases Yanhong Li 1, Hai Yu 1, Yi Chen 1, Kam Lau 1, Li Cai 2, Hongzhi Cao 1,†, Vinod Kumar Tiwari 1,‡, Jingyao Qu 1, Vireak Thon 1, Peng George Wang 2 and Xi Chen 1,* 1 Department of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA; E-Mails: yhzli@ (Y.L.); hyu@ (H.Y.); syichen@ (Y.C.); edlau@ (K.L.); jqu@ (J.Q.); vthon@ (V.T.) 2 Departments of Biochemistry and Chemistry, Ohio State University, Columbus, OH 43210, USA; E-Mails: lcai@ (L.C.); wang.892@ (P.G.W.) † Current Address: National Glycoengineering Research Center, Shandong University, Jinan, Shandong 250012, China ‡ Current Address: Department of Chemistry, Faculty of Science, Banaras Hindu University, Varanasi, UP 221 005, India * Author to whom correspondence should be addressed; E-Mail: chen@; Tel.: +1-530-754-6037; Fax: +1-530-752-8995. Received: 1 July 2011; in revised form: 22 July 2011 / Accepted: 25 July 2011 / Published: 28 July 2011 Abstract: N-Acetylhexosamine 1-kinase (NahK) catalyzes the direct addition of a phosphate from adenosine 5-triphosphate (ATP) to the anomeric position of N-acetylhexosamine and shows similar activity towards N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc). Herein we report the cloning, characterization, and substrate specificity studies of two NahKs from Bifidobacterium infantis ATCC15697 a