An F-type lectin domain directs the activity of Streptosporangium roseum alpha-l-fucosidase

Glycobiology
Ritika BishnoiT N C Ramya

Abstract

F-type lectins are phylogenetically widespread but selectively distributed fucose-binding lectins with L-fucose- and calcium-binding sequence motifs and an F-type lectin fold. Bacterial F-type lectin domains frequently occur in tandem with various protein domains in diverse architectures, indicating a possible role in directing enzyme activities or other biological functions to distinct fucosylated niches. Here, we report the biochemical characterization of a Streptosporangium roseum protein containing an F-type lectin domain in tandem with an NPCBM-associated domain and a family GH 29A alpha-l-fucosidase domain. We show that the F-type lectin domain of this protein recognizes fucosylated glycans in both α and β linkages but has high affinity for a Fuc-α-1,2-Gal motif and that the alpha-l-fucosidase domain displays hydrolytic activity on glycan substrates with α1-2 and α1-4 linked fucose. We also show that the F-type lectin domain does not have any effect on the activity of the cis-positioned alpha-l-fucosidase domain with the synthetic substrate, 4-Methylumbelliferyl-alpha-l-fucopyranoside or on inhibition of this activity by l-fucose or deoxyfuconojirimycin hydrochloride. However, the F-type lectin domain together with the NP...Continue Reading

References

Nov 1, 1977·Archives of Biochemistry and Biophysics·G Dawson, G Tsay
Jun 9, 1978·Biochimica Et Biophysica Acta·T Alam, A S Balsubramanian
Jan 1, 1984·Annual Review of Biochemistry·M McNeilP Albersheim
Aug 31, 2000·Journal of Molecular Biology·C NotredameJ Heringa
Mar 29, 2001·Bioscience, Biotechnology, and Biochemistry·M K AliK Ohmiya
Jul 2, 2002·Nature Structural Biology·Mario A BianchetL Mario Amzel
Mar 26, 2003·Glycobiology·Daniel J Becker, John B Lowe
Jun 6, 2003·The Journal of Biological Chemistry·Yasuo OdaKazuaki Kakehi
Sep 1, 1965·Analytical Chemistry·G G GUILBAULT, D N KRAMER
Dec 19, 2003·Nucleic Acids Research·Ivica LetunicPeer Bork
Jun 1, 2004·Journal of Molecular Evolution·Emanuele LibertiniSimon J McQueen-Mason
Jun 28, 2005·Nucleic Acids Research·Lukasz JaroszewskiAdam Godzik
Oct 28, 2005·The Journal of Biological Chemistry·Eric W Odom, Gerardo R Vasta
Sep 16, 2006·Glycobiology·Bing MaDiane E Taylor
Sep 22, 2006·The Journal of Biological Chemistry·Alisdair B BorastonRobert D Burke
Dec 26, 2006·Nature Structural & Molecular Biology·Alicia Lammerts van BuerenAlisdair B Boraston
Mar 27, 2007·The Journal of Biological Chemistry·Kengo MatsumuraNaoyuki Taniguchi
Nov 23, 2007·Molecular Biology and Evolution·D Wade AbbottAlisdair B Boraston
Oct 8, 2008·Nucleic Acids Research·Brandi L CantarelBernard Henrissat
Jun 22, 2010·Journal of Molecular Biology·Mario A BianchetL Mario Amzel
Apr 8, 2011·Nucleic Acids Research·Ivica Letunic, Peer Bork
May 9, 2012·Applied and Environmental Microbiology·Kimiya MizutaniKazuo Sakka
Dec 4, 2012·Applied and Environmental Microbiology·Fei Zheng, Shaojun Ding
Dec 6, 2012·Proceedings of the National Academy of Sciences of the United States of America·Fiona CuskinHarry J Gilbert

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