Structural highlights
Publication Abstract from PubMedGlycoside hydrolase family 136 (GH136) was established after the discovery and structural analysis of lacto-N-biosidase (LNBase) from the infant gut bacterium Bifidobacterium longum subsp. longum JCM1217 (BlLnbX). Homologous genes of BlLnbX are widely distributed in the genomes of human gut bacteria and monkey Bifidobacterium spp., although only two crystal structures were reported in the GH136 family. Cell suspensions of Bifidobacterium saguini, Tyzzerella nexilis, and Ruminococcus lactaris exhibited the LNBase activity. Recombinant LNBases of these three species were functionally expressed with their specific chaperones in Escherichia coli, and their kinetic parameters against p-nitrophenol substrates were determined. The crystal structures of the LNBases from B. saguini and T. nexilis in complex with lacto-N-biose I were determined at 2.5 A and 1.9 A resolutions, respectively. These structures conserve a beta-helix fold characteristic of GH136 and the catalytic residues, but they lack the metal ions that were present in BlLnbX. Crystal structures of glycoside hydrolase family 136 lacto-N-biosidases from monkey gut- and human adult gut bacteria.,Yamada C, Katayama T, Fushinobu S Biosci Biotechnol Biochem. 2022 Jan 29. pii: 6517306. doi: 10.1093/bbb/zbac015. PMID:35092420[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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