Abstract Amylolytic enzymes belonging to three distinct families of glycosidases (13, 14, 15) contain the starch-binding domain (SBD) positioned almost exclusively at the C-terminus. Detailed analysis of all available SBD sequences from 43 different amylases revealed its independent evolutionary beha-viour with regard to the catalytic domains. In the evolutionary tree based on sequence alignment of the SBDs, taxonomy is respected so that fungi and actinomycetes form their own separate parts surrounded by bacteria that are also clustered according to taxonomy. The only known N-terminal SBD from Rhizopus oryzae glucoamylase is on the longest branch separated from all C-terminal SBDs. The 3-dimensional (3-D) structures of fungal glucoamylase a...
The starch binding domain of glucoamylase from Aspergillus niger: overview of its structure
Abstract: The Lipomyces kononenkoae α-amylases LKA1 and LKA2 belong to the glycoside hydrolase famil...
<p>A. Evolutionary scenarios for the GH13 enzymes. A few α-amylases identified as heterologous α-amy...
AbstractAmylolytic enzymes belonging to three distinct families of glycosidases (13, 14, 15) contain...
AbstractThe present bioinformatics analysis was focused on the starch-binding domains (SBDs) and SBD...
AbstractA novel starch-binding domain (SBD) that represents a new carbohydrate-binding module family...
Fungal amylolytic enzymes, including a-amylase, gluocoamylase and a-glucosidase, have been extensive...
The Lipomyces kononenkoae ?-amylases LKA1 and LKA2 belong to the glycoside hydrolase family 13 and e...
Abstract: Amylolytic enzymes represent a group of starch hydrolases and related enzymes that are act...
AbstractBackground: Carbohydrate-binding domains are usually small and physically separate from the ...
'To whom correspondence should be addressed The model of the catalytic domain of AspergUlus awa...
Amylases are enzymes capable of hydrolysing starch and related saccharides. The best known are -amyl...
Microbacterium aurum B8.A is a bacterium that originates from a potato starch-processing plant and e...
AbstractAmylases possess short, conserved regions near functional side chains. Sequence comparison e...
AbstractThe full-length glucoamylase from Aspergillus niger, G1, consists of an N-terminal catalytic...
The starch binding domain of glucoamylase from Aspergillus niger: overview of its structure
Abstract: The Lipomyces kononenkoae α-amylases LKA1 and LKA2 belong to the glycoside hydrolase famil...
<p>A. Evolutionary scenarios for the GH13 enzymes. A few α-amylases identified as heterologous α-amy...
AbstractAmylolytic enzymes belonging to three distinct families of glycosidases (13, 14, 15) contain...
AbstractThe present bioinformatics analysis was focused on the starch-binding domains (SBDs) and SBD...
AbstractA novel starch-binding domain (SBD) that represents a new carbohydrate-binding module family...
Fungal amylolytic enzymes, including a-amylase, gluocoamylase and a-glucosidase, have been extensive...
The Lipomyces kononenkoae ?-amylases LKA1 and LKA2 belong to the glycoside hydrolase family 13 and e...
Abstract: Amylolytic enzymes represent a group of starch hydrolases and related enzymes that are act...
AbstractBackground: Carbohydrate-binding domains are usually small and physically separate from the ...
'To whom correspondence should be addressed The model of the catalytic domain of AspergUlus awa...
Amylases are enzymes capable of hydrolysing starch and related saccharides. The best known are -amyl...
Microbacterium aurum B8.A is a bacterium that originates from a potato starch-processing plant and e...
AbstractAmylases possess short, conserved regions near functional side chains. Sequence comparison e...
AbstractThe full-length glucoamylase from Aspergillus niger, G1, consists of an N-terminal catalytic...
The starch binding domain of glucoamylase from Aspergillus niger: overview of its structure
Abstract: The Lipomyces kononenkoae α-amylases LKA1 and LKA2 belong to the glycoside hydrolase famil...
<p>A. Evolutionary scenarios for the GH13 enzymes. A few α-amylases identified as heterologous α-amy...