ArticleExtremophiles : life under extreme conditions2008
Biochemical characterization of engineered amylopullulanase from Thermoanaerobacter ethanolicus 39E-implicating the non-necessity of its 100 C-terminal amino acid residues.
Article in Extremophiles : life under extreme conditions, 2008. 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.
- The crystal structure of GH57 family amylopullulanase reveals its dual binding pockets sharing the same catalytic dyad.Communications biology · 2025Article
- Molecular Cloning, Characterization, and Application of a Novel Multifunctional Isoamylase (MIsA) fromFoods (Basel, Switzerland) · 2024Article
- Functional study of C-terminal domain of the thermoacidophilic raw starch-hydrolyzing α-amylase Gt-amy.Food science and biotechnology · 2020Article
- Parallel N- and C-Terminal Truncations Facilitate Purification and Analysis of a 155-kDa Cold-Adapted Type-I Pullulanase.The protein journal · 2017Article
- Structure of aBiotechnology for biofuels · 2017Article
- Cohnella amylopullulanases: Biochemical characterization of two recombinant thermophilic enzymes.PloS one · 2017Article
- 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
- Degradation of Granular Starch by the Bacterium Microbacterium aurum Strain B8.A Involves a Modular α-Amylase Enzyme System with FNIII and CBM25 Domains.Applied and environmental microbiology · 2015Article
- Novel characteristics of a carbohydrate-binding module 20 from hyperthermophilic bacterium.Extremophiles : life under extreme conditions · 2015Article
- Ectopic expression of bacterial amylopullulanase enhances bioethanol production from maize grain.Plant cell reports · 2013Article
- A high molecular-mass Anoxybacillus sp. SK3-4 amylopullulanase: characterization and its relationship in carbohydrate utilization.International journal of molecular sciences · 2013Article
- Effect of C-terminal truncation on enzyme properties of recombinant amylopullulanase from Thermoanaerobacter pseudoethanolicus.Extremophiles : life under extreme conditions · 2012Article
- A GH57 family amylopullulanase from deep-sea Thermococcus siculi: expression of the gene and characterization of the recombinant enzyme.Current microbiology · 2011Article
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Abstract
The functional and structural significance of the C-terminal region of Thermoanaerobacter ethanolicus 39E amylopullulanase (TetApu) was explored using C-terminal truncation mutagenesis. Comparative studies between the engineered full-length (TetApuM955) and its truncated mutant (TetApuR855) included initial rate kinetics, fluorescence and CD spectrometric properties, substrate-binding and hydrolysis abilities, thermostability, and thermodenaturation kinetics. Kinetic analyses revealed that the overall catalytic efficiency, k (cat)/K (m), was slightly decreased for the truncated enzymes toward the soluble starch or pullulan substrate. Changes to the substrate affinity, K (m), and turnover rate, k (cat), varied in different directions for both types of substrates between TetApuM955 and TetApuR855. TetApuR855 exhibited a higher thermostability than TetApuM955, and retained similar substrate-binding ability and hydrolyzing efficiency against the raw starch substrate as TetApuM955 did. Fluorescence spectroscopy indicated that TetApuR855 retained an active folding conformation similar to TetApuM955. A CD-melting unfolding study was able to distinguish between TetApuM955 and TetApuR855 by the higher apparent transition temperature in TetApuR855. These results indicate that up to 100 amino acid residues, including most of the C-terminal fibronectin typeIII (FnIII) motif of TetApuM955, could be further removed without causing a seriously aberrant change in structure and a dramatic decrease in soluble starch and pullulan hydrolysis.
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