Artikel
Open Access
An optional C-terminal domain is ancestral in α-amylases of bilaterian animals
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Jean-Luc Da Lage
Veröffentlicht/Copyright:
28. April 2017
Received: 2017-2-17
Accepted: 2017-3-28
Published Online: 2017-4-28
Published in Print: 2017-2-23
© 2017
Artikel in diesem Heft
- The evolutionary origin and possible functional roles of FNIII domains in two Microbacterium aurum B8.A granular starch degrading enzymes, and in other carbohydrate acting enzymes
- Raw starch degrading α-amylases: an unsolved riddle
- An optional C-terminal domain is ancestral in α-amylases of bilaterian animals
- New insight in cereal starch degradation: identification and structural characterization of four α-amylases in bread wheat
- Purification and characterization of a novel α-glucosidase from an Antarctic yeast Dioszegia fristingensis isolate
- Recent progress toward understanding the role of starch biosynthetic enzymes in the cereal endosperm
- Complete signal peptide of Tk1884, an α-amylase from Thermococcus kodakarensis, is not necessary for extracellular secretion of the enzyme by Escherichia coli
- Production of isomelezitose from sucrose by engineered glucansucrases
Schlagwörter für diesen Artikel
domain shuffling;
evolution;
intron;
horizontal gene transfer;
carbohydrate binding module
Creative Commons
BY-NC-ND 4.0
Artikel in diesem Heft
- The evolutionary origin and possible functional roles of FNIII domains in two Microbacterium aurum B8.A granular starch degrading enzymes, and in other carbohydrate acting enzymes
- Raw starch degrading α-amylases: an unsolved riddle
- An optional C-terminal domain is ancestral in α-amylases of bilaterian animals
- New insight in cereal starch degradation: identification and structural characterization of four α-amylases in bread wheat
- Purification and characterization of a novel α-glucosidase from an Antarctic yeast Dioszegia fristingensis isolate
- Recent progress toward understanding the role of starch biosynthetic enzymes in the cereal endosperm
- Complete signal peptide of Tk1884, an α-amylase from Thermococcus kodakarensis, is not necessary for extracellular secretion of the enzyme by Escherichia coli
- Production of isomelezitose from sucrose by engineered glucansucrases
