ArticleThe Journal of biological chemistry2012
The molecular mechanism of thermostable α-galactosidases AgaA and AgaB explained by x-ray crystallography and mutational studies.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 50 citations in OpenAlex.
- Characterization of galactose catabolic pathways inJournal of bacteriology · 2024Article
- Activity-based metaproteomics driven discovery and enzymological characterization of potential α-galactosidases in the mouse gut microbiome.Communications chemistry · 2024Article
- Cross-Feeding and Enzymatic Catabolism for Mannan-Oligosaccharide Utilization by the Butyrate-Producing Gut BacteriumMicroorganisms · 2022Article
- Molecular advances in microbial α-galactosidases: challenges and prospects.World journal of microbiology & biotechnology · 2022Review
- Heterologous Expression of a Thermostable α-Galactosidase fromJournal of microbiology and biotechnology · 2022Article
- Identification and Characterization of a Thermostable GH36 α-Galactosidase fromInternational journal of molecular sciences · 2021Article
- Article
- Extremophile Microbial Communities and Enzymes for Bioenergetic Application Based on Multi-Omics Tools.Current genomics · 2020Review
- α-Galactosidase and Sucrose-Kinase Relationships in a Bi-functional AgaSK Enzyme Produced by the Human Gut SymbiontFrontiers in microbiology · 2020Article
- Molecular analysis of an enigmaticThe Journal of biological chemistry · 2019Article
- Galactomannan degradation by thermophilic enzymes: a hot topic for biotechnological applications.World journal of microbiology & biotechnology · 2019Review
- Characterization of a long-chain α-galactosidase from Papiliotrema flavescens.World journal of microbiology & biotechnology · 2018Article
- Article
- Sugar Metabolism of the First Thermophilic PlanctomyceteFrontiers in microbiology · 2017Article
- Structural Snapshots for Mechanism-Based Inactivation of a Glycoside Hydrolase by Cyclopropyl Carbasugars.Angewandte Chemie (International ed. in English) · 2016Article
- A β-mannan utilization locus in Bacteroides ovatus involves a GH36 α-galactosidase active on galactomannans.FEBS letters · 2016Article
- Genomic analysis of six new Geobacillus strains reveals highly conserved carbohydrate degradation architectures and strategies.Frontiers in microbiology · 2015Article
- Site-Directed Mutagenesis of a Hyperthermophilic Endoglucanase Cel12B from Thermotoga maritima Based on Rational Design.PloS one · 2015Article
- Multifunctional fructans and raffinose family oligosaccharides.Frontiers in plant science · 2013Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The α-galactosidase AgaA from the thermophilic microorganism Geobacillus stearothermophilus has great industrial potential because it is fully active at 338 K against raffinose and can increase the yield of manufactured sucrose. AgaB has lower affinity for its natural substrates but is a powerful tool for the enzymatic synthesis of disaccharides by transglycosylation. These two enzymes have 97% identity and belong to the glycoside hydrolase (GH) family GH36 for which few structures are available. To understand the structural basis underlying the differences between these two enzymes, we determined the crystal structures of AgaA and AgaB by molecular replacement at 3.2- and 1.8 Å-resolution, respectively. We also solved a 2.8-Å structure of the AgaA(A355E) mutant, which has enzymatic properties similar to those of AgaB. We observe that residue 355 is located 20 Å away from the active site and that the A355E substitution causes structural rearrangements resulting in a significant displacement of the invariant Trp(336) at catalytic subsite -1. Hence, the active cleft of AgaA is narrowed in comparison with AgaB, and AgaA is more efficient than AgaB against its natural substrates. The structure of AgaA(A355E) complexed with 1-deoxygalactonojirimycin reveals an induced fit movement; there is a rupture of the electrostatic interaction between Glu(355) and Asn(335) and a return of Trp(336) to an optimal position for ligand stacking. The structures of two catalytic mutants of AgaA(A355E) complexed with raffinose and stachyose show that the binding interactions are stronger at subsite -1 to enable the binding of various α-galactosides.
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