ArticlePloS one2014
Biochemical properties and atomic resolution structure of a proteolytically processed β-mannanase from cellulolytic Streptomyces sp. SirexAA-E.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Unravelling the genomic potential of sponge-associated Streptomyces sp. BLC 17-3 from Indonesia for mannooligosaccharide production.Journal, genetic engineering & biotechnology · 2026Article
- Multi-proteomics reveals integrated metabolic and regulatory networks for xylan catabolism inMicrobiology spectrum · 2026Article
- A modular enzyme with combined hemicellulose-removing and LPMO activity increases cellulose accessibility in softwood.The FEBS journal · 2025Article
- Research and application progress of microbial β-mannanases: a mini-review.World journal of microbiology & biotechnology · 2024Review
- Comparative genomics of the niche-specific plant pathogenApplied and environmental microbiology · 2023Article
- Impact of Modular Architecture on Activity of Glycoside Hydrolase Family 5 Subfamily 8 Mannanases.Molecules (Basel, Switzerland) · 2022Article
- Mannose- and Mannobiose-Specific Responses of the Insect-Associated Cellulolytic BacteriumApplied and environmental microbiology · 2021Article
- Carbohydrate-binding modules targeting branched polysaccharides: overcoming side-chain recalcitrance in a non-catalytic approach.Bioresources and bioprocessing · 2021Review
- Characterization of the starch-acting MaAmyB enzyme from Microbacterium aurum B8.A representing the novel subfamily GH13_42 with an unusual, multi-domain organization.Scientific reports · 2016Article
- Active site and laminarin binding in glycoside hydrolase family 55.The Journal of biological chemistry · 2015Article
- Natalamycin A, an Ansamycin from a Termite-AssociatedChemical science · 2014Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-Mannanase SACTE_2347 from cellulolytic Streptomyces sp. SirexAA-E is abundantly secreted into the culture medium during growth on cellulosic materials. The enzyme is composed of domains from the glycoside hydrolase family 5 (GH5), fibronectin type-III (Fn3), and carbohydrate binding module family 2 (CBM2). After secretion, the enzyme is proteolyzed into three different, catalytically active variants with masses of 53, 42 and 34 kDa corresponding to the intact protein, loss of the CBM2 domain, or loss of both the Fn3 and CBM2 domains. The three variants had identical N-termini starting with Ala51, and the positions of specific proteolytic reactions in the linker sequences separating the three domains were identified. To conduct biochemical and structural characterizations, the natural proteolytic variants were reproduced by cloning and heterologously expressed in Escherichia coli. Each SACTE_2347 variant hydrolyzed only β-1,4 mannosidic linkages, and also reacted with pure mannans containing partial galactosyl- and/or glucosyl substitutions. Examination of the X-ray crystal structure of the GH5 domain of SACTE_2347 suggests that two loops adjacent to the active site channel, which have differences in position and length relative to other closely related mannanases, play a role in producing the observed substrate selectivity.
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