ArticleThe Journal of biological chemistry2011
Terminal amino acids disturb xylanase thermostability and activity.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- In Silico Analysis and Development of the Secretory Expression of D-Psicose-3-Epimerase inMicroorganisms · 2024Article
- Improvement of thermostability and catalytic efficiency of xylanase fromFrontiers in microbiology · 2024Article
- Fusion of a proline-rich oligopeptide to the C-terminus of a ruminal xylanase improves catalytic efficiency.Bioengineered · 2022Article
- The Emergence of New Catalytic Abilities in an Endoxylanase from Family GH10 by Removing an Intrinsically Disordered Region.International journal of molecular sciences · 2022Article
- Single Residue Substitution atMolecules (Basel, Switzerland) · 2020Article
- Intra-Molecular Homologous Recombination of Scarless Plasmid.International journal of molecular sciences · 2020Article
- Article
- Modeling, Mutagenesis andIranian journal of biotechnology · 2020Article
- Mutagenesis of N-terminal residues confer thermostability on a Penicillium janthinellum MA21601 xylanase.BMC biotechnology · 2019Article
- High-level expression of improved thermo-stable alkaline xylanase variant in Pichia Pastoris through codon optimization, multiple gene insertion and high-density fermentation.Scientific reports · 2016Article
- Thermostable microbial xylanases for pulp and paper industries: trends, applications and further perspectives.World journal of microbiology & biotechnology · 2016Review
- Transposon for protein engineering.Mobile genetic elements · 2016Article
- Distinct roles for carbohydrate-binding modules of glycoside hydrolase 10 (GH10) and GH11 xylanases from Caldicellulosiruptor sp. strain F32 in thermostability and catalytic efficiency.Applied and environmental microbiology · 2015Article
- Unscrambling the effect of C-terminal tail deletion on the stability of a cold-adapted, organic solvent stable lipase from Staphylococcus epidermidis AT2.Molecular biotechnology · 2014Article
- Article
- Effect of codon message on xylanase thermal activity.The Journal of biological chemistry · 2012Article
- Domain-swapping of mesophilic xylanase with hyper-thermophilic glucanase.BMC biotechnology · 2012Article
- Emerging role of N- and C-terminal interactions in stabilizing (β/α)8 fold with special emphasis on Family 10 xylanases.Computational and structural biotechnology journal · 2012Review
- Deletional protein engineering based on stable fold.PloS one · 2012Article
- Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein structure is composed of regular secondary structural elements (α-helix and β-strand) and non-regular region. Unlike the helix and strand, the non-regular region consists of an amino acid defined as a disordered residue (DR). When compared with the effect of the helix and strand, the effect of the DR on enzyme structure and function is elusive. An Aspergillus niger GH10 xylanase (Xyn) was selected as a model molecule of (β/α)(8) because the general structure consists of ~10% enzymes. The Xyn has five N-terminal DRs and one C-terminal DR, respectively, which were deleted to construct three mutants, XynΔN, XynΔC, and XynΔNC. Each mutant was ~2-, 3-, or 4-fold more thermostable and 7-, 4-, or 4-fold more active than the Xyn. The N-terminal deletion decreased the xylanase temperature optimum for activity (T(opt)) 6 °C, but the C-terminal deletion increased its T(opt) 6 °C. The N- and C-terminal deletions had opposing effects on the enzyme T(opt) but had additive effects on its thermostability. The five N-terminal DR deletions had more effect on the enzyme kinetics but less effect on its thermo property than the one C-terminal DR deletion. CD data showed that the terminal DR deletions increased regular secondary structural contents, and hence, led to slow decreased Gibbs free energy changes (ΔG(0)) in the thermal denaturation process, which ultimately enhanced enzyme thermostabilities.
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