ArticleExtremophiles : life under extreme conditions2015
Membrane-bound amylopullulanase is essential for starch metabolism of Sulfolobus acidocaldarius DSM639.
Article in Extremophiles : life under extreme conditions, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Leveraging AI-driven predictors of enzyme pH optima to unravel microbial adaptation to environmental pH.Frontiers in microbiology · 2026Article
- In silico and structural analysis of Bacillus licheniformis FAO.CP7 pullulanase isolated from cocoa (Theobroma cacao L.) pod waste.BMC microbiology · 2025Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- Biotechnology and bioengineering of pullulanase: state of the art and perspectives.World journal of microbiology & biotechnology · 2021Review
- Biomass-degrading glycoside hydrolases of archaeal origin.Biotechnology for biofuels · 2020Review
- In silico analysis of the α-amylase family GH57: eventual subfamilies reflecting enzyme specificities.3 Biotech · 2018Article
- Structure and function of α-glucan debranching enzymes.Cellular and molecular life sciences : CMLS · 2016Review
- The apt/6-Methylpurine Counterselection System and Its Applications in Genetic Studies of the Hyperthermophilic Archaeon Sulfolobus islandicus.Applied and environmental microbiology · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Sulfolobus acidocaldarius DSM639 produced an acid-resistant membrane-bound amylopullulanase (Apu) during growth on starch as a sole carbon and energy source. The physiological role of Apu in starch metabolism was investigated by the growth and starch degradation pattern of apu disruption mutant as well as biochemical properties of recombinant Apu. The Δapu mutant lost the ability to grow in minimal medium in the presence of starch, and the amylolytic activity observed in the membrane fraction of the wild-type strain was not detected in the Δapu mutant when the cells were grown in YT medium. The purified membrane-bound Apu initially hydrolyzed starch, amylopectin, and pullulan into various sizes of maltooligosaccharides, and then produced glucose, maltose, and maltotriose in the end, indicating Apu is a typical endo-acting glycoside hydrolase family 57 (GH57) amylopullulanase. The maltose and maltotriose observed in the culture medium during the exponential and stationary phase growth indicates that Apu is the essential enzyme to initially hydrolyze the starch into small maltooligosaccharides to be transported into the cell.
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