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- W19229969 abstract "α-Amylases catalyze the hydrolytic cleavage of α-glycosidic linkages in starch, glycogen and a number of other related compounds and play an important role in the metabolism of plants, archaea, bacteria, fungi and animals. Due to the biotechnological relevance of these enzymes, which are widely used in the starch-processing and pharmaceutical industry, there is a strong interest in their three-dimensional structure. In particular proteins from hyperthermophilic organisms have attracted attention in this context, since they are easier to handle and often have a higher specific activity than their mesophilic homologues. This thesis describes the crystallization, structure solution, refinement and analysis of the α-amylase A (AmyA, 59 kDa) from the hyperthermophilic bacterium Thermotoga maritima MSB8 and its complex with the inhibitor acarbose at 1.75 and 1.9 Å resolution, respectively. The resulting models, consisting of 535 amino acid residues each, enable the active site of the enzyme to be characterized and the binding mode of the physiological substrate amylose to be derived. Comparisons with several other structures of sugar cleaving enzymes from psychrophilic, mesophilic and (hyper-)thermophilic organisms provide indications for a structural basis of the exceptional thermal stability of AmyA. In particular the proportion and distribution of hydrophobic, uncharged polar and charged residues along the peptide chain and on the water accessible surface of the enzyme appear to contribute significantly to thermostability." @default.
- W19229969 created "2016-06-24" @default.
- W19229969 creator A5006340362 @default.
- W19229969 date "2022-02-20" @default.
- W19229969 modified "2023-09-30" @default.
- W19229969 title "Die Kristallstruktur der α-Amylase A aus dem hyperthermophilen Bakterium Thermotoga maritima MSB8" @default.
- W19229969 doi "https://doi.org/10.53846/goediss-1981" @default.
- W19229969 hasPublicationYear "2022" @default.
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