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Applied and Environmental Microbiology, October 2007, p. 6444-6449, Vol. 73, No. 20
0099-2240/07/$08.00+0     doi:10.1128/AEM.01425-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Identification of N-Acetylhexosamine 1-Kinase in the Complete Lacto-N-Biose I/Galacto-N-Biose Metabolic Pathway in Bifidobacterium longum{triangledown}

Mamoru Nishimoto and Motomitsu Kitaoka*

National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan

Received 27 June 2007/ Accepted 11 August 2007

We have determined the functions of the enzymes encoded by the lnpB, lnpC, and lnpD 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 1-phosphate; the lnpC gene encodes UDP-glucose hexose 1-phosphate uridylyltransferase, which is also active on N-acetylhexosamine 1-phosphate; and the lnpD gene encodes a UDP-glucose 4-epimerase, which is active on both UDP-galactose 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.

* Corresponding author. Mailing address: National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan. Phone: 81-29-838-8071. Fax: 81-29-838-7321. E-mail: mkitaoka{at}affrc.go.jp

{triangledown} Published ahead of print on 24 August 2007.

Applied and Environmental Microbiology, October 2007, p. 6444-6449, Vol. 73, No. 20
0099-2240/07/$08.00+0     doi:10.1128/AEM.01425-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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