Molecules 2011, 16(8), 6396-6407; doi:10.3390/molecules16086396
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 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.
Received: 1 July 2011; in revised form: 22 July 2011 / Accepted: 25 July 2011 / Published: 28 July 2011
(This article belongs to the Special Issue Enzyme-Catalyzed Reactions)
PDF Full-text Download PDF Full-Text [628 KB, uploaded 28 July 2011 15:32 CEST]
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 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.
Keywords: N-acetylgalactosamine; N-acetylglucosamine; N-acetylhexosamine 1-kinase; mannose; substrate specificity

Article Statistics

Load and display the download statistics.

Citations to this Article

Cite This Article

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.

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.

Chicago/Turabian Style

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

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert