Structure-function relationships of glucansucrase and fructansucrase enzymes from lactic acid bacteria
| Autor: | Sacha A. F. T. van Hijum, Lukasz K. Ozimek, Lubbert Dijkhuizen, Ineke G. H. van Geel-Schutten, Slavko Kralj |
|---|---|
| Přispěvatelé: | Faculty of Science and Engineering, GBB Microbiology Cluster, Host-Microbe Interactions, TNO Kwaliteit van Leven |
| Jazyk: | angličtina |
| Rok vydání: | 2006 |
| Předmět: |
synthesis
Protein Conformation Negibacteria TRANSITION-STATE STABILIZATION calcium ion glucan sucrase Glycoside hydrolase gene mutation Bacteria (microorganisms) chemistry.chemical_classification STREPTOCOCCUS-MUTANS GLUCOSYLTRANSFERASES SALIVARIUS ATCC 25975 CELL-BOUND FRUCTOSYLTRANSFERASE MESENTEROIDES NRRL B-512F glucan fructan Enzyme structure unclassified drug enzyme activity enzyme structure Infectious Diseases fructan sucrase Posibacteria Biochemistry BACILLUS-SUBTILIS LEVANSUCRASE nomenclature NEISSERIA-POLYSACCHAREA AMYLOSUCRASE amino acid substitution lactic acid bacterium polymer Molecular Sequence Data review Reviews Biology Gram-Positive Bacteria Microbiology Food technology NUCLEOTIDE-SEQUENCE ANALYSIS Structure-Activity Relationship ALPHA-AMYLASE FAMILY Bacterial Proteins Glycosyltransferase sucrase Glucansucrase oligosaccharide signal peptide enzyme mechanism Amino Acid Sequence Lactic Acid Molecular Biology Nutrition Glucan nonhuman catalysis bacterial enzyme binding site ACETOBACTER-DIAZOTROPHICUS SRT4 Glycosyltransferases Levansucrase nucleotide sequence Glycosidic bond Fructans Enzyme chemistry biology.protein |
| Zdroj: | Microbiology and Molecular Biology Reviews, 70(1), 157-176. AMER SOC MICROBIOLOGY Microbiology and Molecular Biology Reviews, 1, 70, 157-176 |
| ISSN: | 1092-2172 |
| DOI: | 10.1128/mmbr.70.1.157-176.2006 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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