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Structure-Function Relationships of Glucansucrase and Fructansucrase Enzymes from Lactic Acid Bacteria

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van Hijum, Sacha A. F. T., Kralj, Slavko, Ozimek, Lukasz K., Dijkhuizen, Lubbert, van Geel-Schutten, Ineke G. H.·2006·Microbiology and Molecular Biology Reviews

Abstract

SUMMARY: Lactic acid bacteria (LAB) employ sucrase-type enzymes to convert sucrose into homopolysaccharides consisting of either glucosyl units (glucans) or fructosyl units (fructans). The enzymes involved are labeled glucansucrases (GS) and fructansucrases (FS), respectively. The available molecular, biochemical, and structural information on sucrase genes and enzymes from various LAB and their fructan and α-glucan products is reviewed. The GS and FS enzymes are both glycoside hydrolase enzymes that act on the same substrate (sucrose) and catalyze (retaining) transglycosylation reactions that result in polysaccharide formation, but they possess completely different protein structures. GS enzymes (family GH70) are large multidomain proteins that occur exclusively in LAB. Their catalytic domain displays clear secondary-structure similarity with α-amylase enzymes (family GH13), with a predicted permuted (β/α) 8 barrel structure for which detailed structural and mechanistic information is available. Emphasis now is on identification of residues and regions important for GS enzyme activity and product specificity (synthesis of α-glucans differing in glycosidic linkage type, degree and type of branching, glucan molecular mass, and solubility). FS enzymes (family GH68) occur in both gram-negative and gram-positive bacteria and synthesize β-fructan polymers with either β-(2→6) (inulin) or β-(2→1) (levan) glycosidic bonds. Recently, the first high-resolution three-dimensional structures have become available for FS (levansucrase) proteins, revealing a rare five-bladed β-propeller structure with a deep, negatively charged central pocket. Although these structures have provided detailed mechanistic insights, the structural features in FS enzymes dictating the synthesis of either β-(2→6) or β-(2→1) linkages, degree and type of branching, and fructan molecular mass remain to be identified.

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Crossref · 10.1128/mmbr.70.1.157-176.2006

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Metadata

Authors
van Hijum, S. A. F. T., Kralj, S., Ozimek, L. K., Dijkhuizen, L., & van Geel-Schutten, I. G. H.
Venue
Microbiology and Molecular Biology Reviews
Published
2006-03
Volume
70
Issue
1
Pages
157-176
ISSN
  • 1092-2172 (ISSN-L)
  • 1098-5557
OpenAlex
W2111051779
Cited by
466
References
3
FWCI
2.07
Type
journal article
Language
en
Open access
green

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