ArticleJournal of bacteriology2006
Molecular and biochemical characterization of alpha-glucosidase and alpha-mannosidase and their clustered genes from the thermoacidophilic archaeon Picrophilus torridus.
Article in Journal of bacteriology, 2006. 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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Who cites it
19 citing papers in PubMed, 49 citations in OpenAlex.
- Spatiotemporal Profiling of Starch-Degrading Enzymes in Nong-Flavor Daqu: Molecular Markers for Quantitative Quality Evaluation.Foods (Basel, Switzerland) · 2025Article
- Evolutionary patterns of archaea predominant in acidic environment.Environmental microbiome · 2023Article
- Insight into broad substrate specificity and synergistic contribution of a fungal α-glucosidase in Chinese Nong-flavor daqu.Microbial cell factories · 2023Article
- Expression and Characterization of a GH38 α-Mannosidase from the Hyperthermophile Pseudothermotoga thermarum.Applied biochemistry and biotechnology · 2023Article
- Archaea as a Model System for Molecular Biology and Biotechnology.Biomolecules · 2023Review
- Valorization of Biomasses from Energy Crops for the Discovery of Novel Thermophilic Glycoside Hydrolases through Metagenomic Analysis.International journal of molecular sciences · 2022Article
- Characterization of an α-Glucosidase Enzyme Conserved inJournal of bacteriology · 2021Article
- Influence of Supplementation of Lactoferrin, Melittin and Cecropin A to Rat Diet on Changes in Faecal Ammonia Concentrations, Short-Chain Fatty Acid Concentrations and Activities of Bacterial Enzymes.Animals : an open access journal from MDPI · 2021Article
- Biomass-degrading glycoside hydrolases of archaeal origin.Biotechnology for biofuels · 2020Review
- Purification and characterization of a novel thermophilic β-galactosidase from Picrophilus torridus of potential industrial application.Extremophiles : life under extreme conditions · 2019Article
- Biotechnological applications of archaeal enzymes from extreme environments.Biological research · 2018Review
- Cloning and Molecular Characterization of an Alpha-Glucosidase (MalH) from the Halophilic Archaeon Haloquadratum walsbyi.Life (Basel, Switzerland) · 2017Article
- GlnR and PhoP Directly Regulate the Transcription of Genes Encoding Starch-Degrading, Amylolytic Enzymes in Saccharopolyspora erythraea.Applied and environmental microbiology · 2016Article
- Sequential processing of mannose-containing glycans by two α-mannosidases from Solitalea canadensis.Glycoconjugate journal · 2016Article
- Identification and characterization of MalA in the maltose/maltodextrin operon of Sulfolobus acidocaldarius DSM639.Journal of bacteriology · 2013Article
- A hydrolytic γ-glutamyl transpeptidase from thermo-acidophilic archaeon Picrophilus torridus: binding pocket mutagenesis and transpeptidation.Extremophiles : life under extreme conditions · 2013Article
- Characterization of plasmid pPO1 from the hyperacidophile Picrophilus oshimae.Archaea (Vancouver, B.C.) · 2011Article
- Functional role of Bradyrhizobium japonicum trehalose biosynthesis and metabolism genes during physiological stress and nodulation.Applied and environmental microbiology · 2010Article
- Pantothenate kinase from the thermoacidophilic archaeon Picrophilus torridus.Journal of bacteriology · 2010Article
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The genes encoding a putative alpha-glucosidase (aglA) and an alpha-mannosidase (manA) appear to be physically clustered in the genome of the extreme acidophile Picrophilus torridus, a situation not found previously in any other organism possessing aglA or manA homologs. While archaeal alpha-glucosidases have been described, no alpha-mannosidase enzymes from the archaeal kingdom have been reported previously. Transcription start site mapping and Northern blot analysis revealed that despite their colinear orientation and the small intergenic space, the genes are independently transcribed, both producing leaderless mRNA. aglA and manA were cloned and overexpressed in Escherichia coli, and the purified recombinant enzymes were characterized with respect to their physicochemical and biochemical properties. AglA displayed strict substrate specificity and hydrolyzed maltose, as well as longer alpha-1,4-linked maltooligosaccharides. ManA, on the other hand, hydrolyzed all possible linkage types of alpha-glycosidically linked mannose disaccharides and was able to hydrolyze alpha3,alpha6-mannopentaose, which represents the core structure of many triantennary N-linked carbohydrates in glycoproteins. The probable physiological role of the two enzymes in the utilization of exogenous glycoproteins and/or in the turnover of the organism's own glycoproteins is discussed.
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