4.6 Article

Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-biose I/Galacto-N-Biose metabolic pathway in Bifidobactetium longum

Journal

APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Volume 73, Issue 20, Pages 6444-6449

Publisher

AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.01425-07

Keywords

-

Ask authors/readers for more resources

We have determined the functions of the enzymes encoded by the lnpB, InpC, and InpD genes, located downstream of the lacto-N-biose phosphorylase gene (lnpA), in Bifidobacterium longum JCM1217. The lnpB gene encodes a novel kinase, N-acetylhexosamine 1-kinase, which produces N-acetylhexosamine I-phosphate; the InpC gene encodes UDP-glucose hexose 1-phosphate uridylyltransferase, which is also active on N-acetylhexosamine I-phosphate; and the lnpD gene encodes a UDP-glucose 4-epimerase, which is active on both UDPgalactose and UDP-N-acetylgalactosamine. These results suggest that the gene operon lnpABCD encodes a previously undescribed lacto-N-biose I/galacto-N-biose metabolic pathway that is involved in the intestinal colonization of bifidobacteria and that utilizes lacto-N-biose I from human milk oligosaccharides or galacto-N-biose from mucin sugars.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.6
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available