Novel putative galactose operon involving lacto-N-biose phosphorylase in Bifidobacterium longum - PubMed (original) (raw)

Novel putative galactose operon involving lacto-N-biose phosphorylase in Bifidobacterium longum

Motomitsu Kitaoka et al. Appl Environ Microbiol. 2005 Jun.

Abstract

A lacto-N-biose phosphorylase (LNBP) was purified from the cell extract of Bifidobacterium bifidum. Its N-terminal and internal amino acid sequences were homologous with those of the hypothetical protein of Bifidobacterium longum NCC2705 encoded by the BL1641 gene. The homologous gene of the type strain B. longum JCM1217, lnpA, was expressed in Escherichia coli to confirm that it encoded LNBP. No significant identity was found with any proteins with known function, indicating that LNBP should be classified in a new family. The lnpA gene is located in a novel putative operon for galactose metabolism that does not contain a galactokinase gene. The operon seems to be involved in intestinal colonization by bifidobacteria mediated by metabolism of mucin sugars. In addition, it may also resolve the question of the nature of the bifidus factor in human milk as the lacto-N-biose structure found in milk oligosaccharides.

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Figures

FIG. 1.

Alignment of the amino acid sequences of LNBPs. The origins of the enzymes are indicated in the left column. Conserved amino acid residues are highlighted.

FIG. 2.

Putative lacto-_N_-biose operon found in the genomic sequence of B. longum NCC2705. BL1641 was identified as LNBP in this study. BL1638-1640 genes are annotated as component proteins of the ABC-type sugar transporter. BL1642, BL1643, and BL1644 are annotated as mucin desulfatase, galactose-1-phosphate uridylyltransferase (EC 2.7.7.10), and UDP-glucose 4-epimerase (EC 5.1.3.2), respectively.

FIG. 3.

Proposed scheme of lacto-_N_-biose metabolism.

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Novel putative galactose operon involving lacto-N-biose phosphorylase in Bifidobacterium longum - PubMed (original) (raw)