ArticleThe Journal of biological chemistry2013
Structural insights into the substrate specificity of a 6-phospho-β-glucosidase BglA-2 from Streptococcus pneumoniae TIGR4.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 23 citations in OpenAlex.
- A high-sensitivity strategy to screen NAD(P)H-dependent reductase activity by coupled enzyme cascade.The Journal of biological chemistry · 2026Article
- Multi-omics profiling reveals atypical sugar utilization and a key membrane composition regulator in Streptococcus pneumoniae.Nature communications · 2025Article
- Adaptive laboratory evolution under oxidative stress in lactococcus lactis subsp. lactis LM1009: transcriptomic remodeling and functional enhancement.World journal of microbiology & biotechnology · 2025Article
- Dual 6Pβ-Galactosidase/6Pβ-Glucosidase GH1 Family for Lactose Metabolism in the Probiotic BacteriumJournal of agricultural and food chemistry · 2023Article
- Impact of the pentose phosphate pathway on metabolism and pathogenesis of Staphylococcus aureus.PLoS pathogens · 2023Article
- ThermophilicFrontiers in microbiology · 2022Article
- Comparative genome analysis of fourComputational and structural biotechnology journal · 2022Article
- Gut Microbiome in Chronic Coronary Syndrome Patients.Journal of clinical medicine · 2021Article
- Antimicrobial susceptibilities and comparative whole genome analysis of two isolates of the probiotic bacterium Lactiplantibacillus plantarum, strain ATCC 202195.Scientific reports · 2021Article
- Cross-utilization of β-galactosides and cellobiose inThe Journal of biological chemistry · 2020Article
- Molecular analysis of an enigmaticThe Journal of biological chemistry · 2019Article
- Pneumococcal 6-Phospho-β-Glucosidase (BglA3) Is Involved in Virulence and Nutrient Metabolism.Infection and immunity · 2016Article
- Phylogenomically guided identification of industrially relevant GH1 β-glucosidases through DNA synthesis and nanostructure-initiator mass spectrometry.ACS chemical biology · 2014Article
- Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases.PloS one · 2014Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
The 6-phospho-β-glucosidase BglA-2 (EC 3.2.1.86) from glycoside hydrolase family 1 (GH-1) catalyzes the hydrolysis of β-1,4-linked cellobiose 6-phosphate (cellobiose-6'P) to yield glucose and glucose 6-phosphate. Both reaction products are further metabolized by the energy-generating glycolytic pathway. Here, we present the first crystal structures of the apo and complex forms of BglA-2 with thiocellobiose-6'P (a non-metabolizable analog of cellobiose-6'P) at 2.0 and 2.4 Å resolution, respectively. Similar to other GH-1 enzymes, the overall structure of BglA-2 from Streptococcus pneumoniae adopts a typical (β/α)8 TIM-barrel, with the active site located at the center of the convex surface of the β-barrel. Structural analyses, in combination with enzymatic data obtained from site-directed mutant proteins, suggest that three aromatic residues, Tyr(126), Tyr(303), and Trp(338), at subsite +1 of BglA-2 determine substrate specificity with respect to 1,4-linked 6-phospho-β-glucosides. Moreover, three additional residues, Ser(424), Lys(430), and Tyr(432) of BglA-2, were found to play important roles in the hydrolytic selectivity toward phosphorylated rather than non-phosphorylated compounds. Comparative structural analysis suggests that a tryptophan versus a methionine/alanine residue at subsite -1 may contribute to the catalytic and substrate selectivity with respect to structurally similar 6-phospho-β-galactosidases and 6-phospho-β-glucosidases assigned to the GH-1 family.
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