Trends in Glycoscience and Glycotechnology
Online ISSN : 1883-2113
Print ISSN : 0915-7352
ISSN-L : 0915-7352
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Volume 24, Issue 139
Displaying 1-5 of 5 articles from this issue
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MINIREVIEW
  • Molecular and Structural Basis for Sugar Recognition by Mannose 6-Phosphate Receptor Homology Domain-Containing Lectins and Proteins
    Tadashi Satoh
    Article type: MINIREVIEW
    2012 Volume 24 Issue 139 Pages 193-202
    Published: 2012
    Released on J-STAGE: September 29, 2012
    DOIhttps://doi.org/10.4052/tigg.24.193
    JOURNAL FREE ACCESS
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    N-Linked glycans play important roles in the determination of glycoprotein fates in cells through interactions with a variety of intracellular lectins. Most of the intracellular lectins possess carbohydrate recognition domain, which is homologous to legume lectins or mannose 6-phosphate receptors (MPRs). These lectins are categorized as L-type or P-type lectins. Besides L-type lectins, recently accumulated frontal affinity chromatography and glycan microarray data have demonstrated that P-type lectins and the MPR homology (MRH) domain-containing proteins have distinct sugar-binding specificity profiles. Furthermore, newly emerged three-dimensional structural data have revealed sugar recognition mechanisms at an atomic level. This review summarizes the current state of knowledge of molecular and structural basis for sugar recognition by P-type lectins and MRH domain-containing proteins that control folding, transport, and degradation of N-linked glycoproteins in the secretory pathway.
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  • Sulfonium Ions as Reactive Glycosylation Intermediates
    Toshiki Nokami
    Article type: MINIREVIEW
    2012 Volume 24 Issue 139 Pages 203-214
    Published: 2012
    Released on J-STAGE: September 29, 2012
    DOIhttps://doi.org/10.4052/tigg.24.203
    JOURNAL FREE ACCESS
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    Glycosyl sulfonium ions are positively charged organosulfur compounds having the positive charge on a sulfur atom that is covalently attached to the anomeric carbon. These species have received attention because of their potential as glycosylation intermediates. Recently, novel methods for the preparation of glycosyl sulfonium ions have been reported. The reactivity of glycosyl sulfonium ions can be controlled by changing the substituents on the sulfur atom and the protecting groups of the hydroxyl groups. Recent studies have also shown that glycosyl sulfonium ions are unique glycosylation intermediates that have modifiable reactivity.
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  • Functional Analysis of Degradative Enzymes for Hydroxyproline-linked β-L-Arabinofuranosides in Bifidobacterium longum
    Kiyotaka Fujita, Kanefumi Kitahara, Toshihiko Suganuma
    Article type: MINIREVIEW
    2012 Volume 24 Issue 139 Pages 215-224
    Published: 2012
    Released on J-STAGE: September 29, 2012
    DOIhttps://doi.org/10.4052/tigg.24.215
    JOURNAL FREE ACCESS
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    β-L-Arabinofuranosides are hydroxyproline (Hyp)-linked sugar chains of extensin observed in plant cell wall fractions. Despite the broad distribution of β-L-arabinofuranosyl residues in plants, degradative enzymes have not yet been identified. In 2011, we cloned and characterized the first degradative enzymes for Hyp-linked β-L-arabinofuranosides from Bifidobacterium longum. These enzymes were composed of a glycoside hydrolase (GH) family 43 α-L-arabinofuranosidase (HypAA) releasing L-arabinose from Arafα1-3Arafβ1-2Arafβ1-2Arafβ-Hyp, a GH121 β-L-arabinobiosidase (HypBA2) releasing Arafβ1-2Araf (β-Ara2) from Arafβ1-2Arafβ1-2Arafβ-Hyp, and a GH127 β-L-arabinofuranosidase (HypBA1) degrading β-Ara2 to L-arabinose. These enzymes are encoded in a conserved gene cluster on several B. longum genomes, but not in genome sequences of other intestinal bacteria. Hyp-linked β-L-arabinofuranosides were utilized as carbohydrate sources by B. longum. This review presents the functional features of enzymes for Hyp-linked β-L-arabinofuranosides and the predicted metabolic pathway in B. longum.
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