enzyme Amy from Paenibacillus sp. SSG-1 exhibits unexpectedly sequence similarity and evolutionary relationships with alpha-glucanotransferase, homology modelling, using the crystal structure of a secretory alpha-amylase AmyA (PDB ID: 1WZA) as the template, and phylogenetic analysis
the alpha-amylase has an alpha-1,4-glucan-maltose-1-phosphate maltosyltransferase domain (IPR021828) (aa 20-206) and a GH13 family domain (aa 199-574) of glycoside hydrolase (IPR015902)
the enzyme belongs to glycosyl hydrolase family 13, GH13, capable of acting on alpha-1,4-bonds only. The peptide sequence (residues 22-399) is homologous to glycoside hydrolase superfamily (IPR017853) containing glycosyl hydrolase, family 13, catalytic domain (residues 34-390) (IPR006047-Interpro), and alpha-amylase catalytic domain, AmyAc_euk_AmyA (residues 26-395) (cd11319-CDD NCBI). Near the C-terminal (residues 407-496), the deduced peptide sequence also contains an alpha-amylase domain DUF1966 (IPR015340, pfam09260)
the enzyme belongs to the glycosyl hydrolase family 13, GH13. The enzyme has the characteristic structure of alpha-amylases belonging to the GH family 13 with a single polypeptide chain folded into the three domains A-C
the enzyme belongs to glycosyl hydrolase family 13, GH13, capable of acting on alpha-1,4-bonds only. The peptide sequence (residues 22-399) is homologous to glycoside hydrolase superfamily (IPR017853) containing glycosyl hydrolase, family 13, catalytic domain (residues 34-390) (IPR006047-Interpro), and alpha-amylase catalytic domain, AmyAc_euk_AmyA (residues 26-395) (cd11319-CDD NCBI). Near the C-terminal (residues 407-496), the deduced peptide sequence also contains an alpha-amylase domain DUF1966 (IPR015340, pfam09260)
the enzyme belongs to the glycosyl hydrolase family 13, GH13. The enzyme has the characteristic structure of alpha-amylases belonging to the GH family 13 with a single polypeptide chain folded into the three domains A-C
the enzyme belongs to the glycosyl hydrolase family 13, GH13. The enzyme has the characteristic structure of alpha-amylases belonging to the GH family 13 with a single polypeptide chain folded into the three domains A-C
the alpha-amylase has an alpha-1,4-glucan-maltose-1-phosphate maltosyltransferase domain (IPR021828) (aa 20-206) and a GH13 family domain (aa 199-574) of glycoside hydrolase (IPR015902)
the enzyme belongs to the glycosyl hydrolase family 13, GH13. The enzyme has the characteristic structure of alpha-amylases belonging to the GH family 13 with a single polypeptide chain folded into the three domains A-C
the enzyme belongs to the glycosyl hydrolase family 13, GH13. The enzyme has the characteristic structure of alpha-amylases belonging to the GH family 13 with a single polypeptide chain folded into the three domains A-C
construction of the alpha-amylase deletion strain. Inactivation of the amyA gene results in a complete loss of activity, suggesting that the same protein is responsible for the alpha-amylase activity at both locations, extracellular and intracellular
effects of BGTG-1 silencing in males on precopulatory behaviour and reproductive performance, overview. The attenuation of BGTG-1 gene and protein expression has no impact on precopulatory behaviours exhibited by paired adult males and females
late maturity alpha-amylase (LMA) and preharvest sprouting (PHS) are genetic defects in wheat. They are both characterized by the expression of specific isoforms of alpha-amylase in particular genotypes in the grain prior to harvest. The enhanced expression of alpha-amylase in both LMA and PHS results in a reduction in Falling Number (FN), a test of gel viscosity, and subsequent downgrading of the grain, along with a reduced price for growers. Wheat in which isoform alpha-amylase (TaAmy3) is overexpressed in the endosperm of developing grain to levels of up to 100fold higher than the wild-type shows low FN similar to those seen in LMA- or PHS-affected grains. This increase has no detrimental effect on starch structure, flour composition and enhanced baking quality, in small-scale baking tests
construction of the alpha-amylase deletion strain. Inactivation of the amyA gene results in a complete loss of activity, suggesting that the same protein is responsible for the alpha-amylase activity at both locations, extracellular and intracellular
alpha-amylases catalyze the hydrolysis of internal alpha-D-(1,4)-glucosidic linkages in starch, glycogen, and related oligo- and polysaccharides to produce maltodextrins, maltooligosaccharides, and glucose
comparison of chloride-dependent alpha-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete reveals striking continuum in the functional properties of the enzymes coupled to their structural stability and related to the thermal regime of the source organism
comparison of chloride-dependent alpha-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete reveals striking continuum in the functional properties of the enzymes coupled to their structural stability and related to the thermal regime of the source organism
comparison of chloride-dependent alpha-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete reveals striking continuum in the functional properties of the enzymes coupled to their structural stability and related to the thermal regime of the source organism
comparison of chloride-dependent alpha-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete reveals striking continuum in the functional properties of the enzymes coupled to their structural stability and related to the thermal regime of the source organism
alpha-amylases are classical calcium-binding enzymes, which randomly hydrolyze internal alpha-1,4-glucosidic linkages in starch to produce smaller molecular mass maltodextrins, maltooligosaccharides and glucose
as one of receptors of the acquired membrane, human salivary alpha-amylase (HSA) plays an important role in the formation of caries. The conformation of the enzyme is altered in the presence of SPC-tetramer. The conformation changes of enzyme HSA might contribute to the reduction of the adhesion of cariogenic bacteria and finally decrease the occurrence of dental caries. Preventive effect of Sorghum procyanidins on dental caries
enzyme Amy may play an important role in utilizing maltooligosaccharides that are released from extracellular alpha-glucan or storage alpha-glucan (glycogen) in Paenibacillus sp. SSG-1
alpha-amylases catalyze the hydrolysis of internal alpha-D-(1,4)-glucosidic linkages in starch, glycogen, and related oligo- and polysaccharides to produce maltodextrins, maltooligosaccharides, and glucose
determination of the structure of carbohydrate binding CBM58-binding site, the active site, and the surface starch-binding site, directly adjacent to the reducing end of the active site
enzyme modification using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride in the presence of a nucleophile, AME, to activate the carboxyl groups of the enzyme, comparisons in anion and cation exchange chromatographies and by native PAGE, overview. The modifications project into the bulk solvent. The enhanced thermostability leads to increased productivity
enzyme structure homology model building and structure analysis using analysis multiple sequence alignment, overview. The overall structure of amylase AMY121 is composed by three distinct domains (A-C), which are typical in liquefying-type bacterial alpha-amylases, location of residue Lys209 in domain B
homology modeling and molecular docking of alpha-amylase from Callosobruchus chinensis and comparison to the alpha-amylase from Tribolium castaneum showing structural differences between these two enzymes, overview
homology modeling and molecular docking of alpha-amylase from Callosobruchus chinensis and comparison to the alpha-amylase from Tribolium castaneum showing structural differences between these two enzymes, overview
homology modeling and molecular docking of alpha-amylase from Callosobruchus chinensis and comparison to the alpha-amylase from Tribolium castaneum showing structural differences between these two enzymes, overview
homology modeling and molecular docking of alpha-amylase from Callosobruchus chinensis and comparison to the alpha-amylase from Tribolium castaneum showing structural differences between these two enzymes, overview
homology modeling of native AmyS and mutant AmySxadDELTAR179-G180 structures are created using the wild-type BStA (PDB ID 1HVX) as a template. A small extra loop containing residues Arg179-Gly180 is located in domain B of AmyS
presence of three conserved catalytic residues of alpha-amylase, two Ca2+-binding sites, and seven conserved peptide sequences. The enzyme also carries two potential surface/secondary-binding site (SBS) residues (Trp 237 and Tyr 409) that might be playing crucial roles in both the enzyme activity and also the binding of starch granules. Enzyme structure homology modelling using the structure of alpha-amylase from Aspergillus oryzae strain RIB40 (PDB ID 2TAA)
structure-function analysis of recombinant enzyme Blamy-I, homology modeling of the three-dimensional structure of Blamy-I using the X-ray crystallography structure of alpha-amylase, PDB ID 1ob0A, as the template
structure-function analysis of recombinant enzyme Blamy-I, homology modeling of the three-dimensional structure of Blamy-I using the X-ray crystallography structure of alpha-amylase, PDB ID 1ob0A, as the template
presence of three conserved catalytic residues of alpha-amylase, two Ca2+-binding sites, and seven conserved peptide sequences. The enzyme also carries two potential surface/secondary-binding site (SBS) residues (Trp 237 and Tyr 409) that might be playing crucial roles in both the enzyme activity and also the binding of starch granules. Enzyme structure homology modelling using the structure of alpha-amylase from Aspergillus oryzae strain RIB40 (PDB ID 2TAA)
structure-function analysis of recombinant enzyme Blamy-I, homology modeling of the three-dimensional structure of Blamy-I using the X-ray crystallography structure of alpha-amylase, PDB ID 1ob0A, as the template