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Article

Substrate Promiscuity of N-Acetylhexosamine 1-Kinases

1
Department of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA
2
Departments of Biochemistry and Chemistry, Ohio State University, Columbus, OH 43210, USA
*
Author to whom correspondence should be addressed.
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
Molecules 2011, 16(8), 6396-6407; https://doi.org/10.3390/molecules16086396
Received: 1 July 2011 / Revised: 22 July 2011 / Accepted: 25 July 2011 / Published: 28 July 2011
(This article belongs to the Special Issue Enzyme-Catalyzed Reactions)
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 and Bifidobacterium longum ATCC55813, respectively. A new capillary electrophoresis assay method has been developed for enzyme activity assays. Both enzymes have a good expression level in E. coli (180–185 mg/L culture) and can tolerate diverse modifications at C2 of GlcNAc and GalNAc. Various GlcNAc derivatives with C6, both C2 and C6, as well as both C2 and C3 modifications are tolerable substrates for the newly cloned NahKs. Quite interestingly, despite of their low activities toward glucose and galactose, the activities of both NahKs are much higher for mannose and some of its C2, C4, and C6 derivatives. These NahKs are excellent catalysts for enzymatic and chemoenzymatic synthesis of carbohydrates. View Full-Text
Keywords: N-acetylgalactosamine; N-acetylglucosamine; N-acetylhexosamine 1-kinase; mannose; substrate specificity N-acetylgalactosamine; N-acetylglucosamine; N-acetylhexosamine 1-kinase; mannose; substrate specificity
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MDPI and ACS Style

Li, Y.; Yu, H.; Chen, Y.; Lau, K.; Cai, L.; Cao, H.; Tiwari, V.K.; Qu, J.; Thon, V.; Wang, P.G.; Chen, X. Substrate Promiscuity of N-Acetylhexosamine 1-Kinases. Molecules 2011, 16, 6396-6407. https://doi.org/10.3390/molecules16086396

AMA Style

Li Y, Yu H, Chen Y, Lau K, Cai L, Cao H, Tiwari VK, Qu J, Thon V, Wang PG, Chen X. Substrate Promiscuity of N-Acetylhexosamine 1-Kinases. Molecules. 2011; 16(8):6396-6407. https://doi.org/10.3390/molecules16086396

Chicago/Turabian Style

Li, Yanhong, Hai Yu, Yi Chen, Kam Lau, Li Cai, Hongzhi Cao, Vinod Kumar Tiwari, Jingyao Qu, Vireak Thon, Peng George Wang, and Xi Chen. 2011. "Substrate Promiscuity of N-Acetylhexosamine 1-Kinases" Molecules 16, no. 8: 6396-6407. https://doi.org/10.3390/molecules16086396

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