Glycosyl Hydrolases
Mostrando 13-24 de 63 artigos, teses e dissertações.
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13. Mannan-Degrading Enzymes from Cellulomonas fimi
The genes man26a and man2A from Cellulomonas fimi encode mannanase 26A (Man26A) and β-mannosidase 2A (Man2A), respectively. Mature Man26A is a secreted, modular protein of 951 amino acids, comprising a catalytic module in family 26 of glycosyl hydrolases, an S-layer homology module, and two modules of unknown function. Exposure of Man26A produced by Escheri
American Society for Microbiology.
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14. Relationship between Glycosyl Hydrolase Inventory and Growth Physiology of the Hyperthermophile Pyrococcus furiosus on Carbohydrate-Based Media
Utilization of a range of carbohydrates for growth by the hyperthermophile Pyrococcus furiosus was investigated by examining the spectrum of glycosyl hydrolases produced by this microorganism and the thermal labilities of various saccharides. Previously, P. furiosus had been found to grow in batch cultures on several α-linked carbohydrates and cellobiose bu
American Society for Microbiology.
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15. Characterization of Two New Glycosyl Hydrolases from the Lactic Acid Bacterium Carnobacterium piscicola Strain BA
Three genes with homology to glycosyl hydrolases were detected on a DNA fragment cloned from a psychrophilic lactic acid bacterium isolate, Carnobacterium piscicola strain BA. A 2.2-kb region corresponding to an α-galactosidase gene, agaA, was followed by two genes in the same orientation, bgaB, encoding a 2-kb β-galactosidase, and bgaC, encoding a structu
American Society for Microbiology.
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16. Cloning and Expression of the Gene Which Encodes a Tube Precipitin Antigen and Wall-Associated β-Glucosidase of Coccidioides immitis
We report the structure and expression of the Coccidioides immitis BGL2 gene which encodes a previously characterized 120-kDa glycoprotein of this fungal respiratory pathogen. The glycoprotein is recognized by immunoglobulin M tube precipitin (TP) antibody present in sera of patients with coccidioidomycosis, a reaction which has been used for serodiagnosis o
American Society for Microbiology.
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17. Computer assisted cloning of human neutral α-glucosidase C (GANC): A new paralog in the glycosyl hydrolase gene family 31
The exponential expansion of the publicly available human DNA sequence database has increasingly facilitated cloning by homology of genes for biochemically defined, functionally similar proteins. We hypothesized that an as-yet uncloned human α-glucosidase (human neutral α-glucosidase C or GANC) is a previously uncharacterized member of a paralogous human g
The National Academy of Sciences.
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18. Characterization of a Neocallimastix patriciarum cellulase cDNA (celA) homologous to Trichoderma reesei cellobiohydrolase II.
The nucleotide sequence of a cellulase cDNA (celA) from the rumen fungus Neocallimastix patriciarum and the primary structure of the protein which it encodes were characterized. The celA cDNA was 1.95 kb long and had an open reading frame of 1,284 bp, which encoded a polypeptide having 428 amino acid residues. A sequence alignment showed that cellulase A (CE
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19. Regulation of Endo-Acting Glycosyl Hydrolases in the Hyperthermophilic Bacterium Thermotoga maritima Grown on Glucan- and Mannan-Based Polysaccharides
The genome sequence of the hyperthermophilic bacterium Thermotoga maritima encodes a number of glycosyl hydrolases. Many of these enzymes have been shown in vitro to degrade specific glycosides that presumably serve as carbon and energy sources for the organism. However, because of the broad substrate specificity of many glycosyl hydrolases, it is difficult
American Society for Microbiology.
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20. Detachment of Actinobacillus actinomycetemcomitans Biofilm Cells by an Endogenous β-Hexosaminidase Activity
When cultured in broth, fresh clinical isolates of the gram-negative periodontal pathogen Actinobacillus actinomycetemcomitans form tenaciously adherent biofilm colonies on surfaces such as plastic and glass. These biofilm colonies release adherent cells into the medium, and the released cells can attach to the surface of the culture vessel and form new colo
American Society for Microbiology.
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21. Molecular and Biochemical Characterization of Two Xylanase-Encoding Genes from Cellulomonas pachnodae
Two xylanase-encoding genes, named xyn11A and xyn10B, were isolated from a genomic library of Cellulomonas pachnodae by expression in Escherichia coli. The deduced polypeptide, Xyn11A, consists of 335 amino acids with a calculated molecular mass of 34,383 Da. Different domains could be identified in the Xyn11A protein on the basis of homology searches. Xyn11
American Society for Microbiology.
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22. A Novel β-N-Acetylglucosaminidase from Streptomyces thermoviolaceus OPC-520: Gene Cloning, Expression, and Assignment to Family 3 of the Glycosyl Hydrolases
A β-N-acetylglucosaminidase gene (nagA) of Streptomyces thermoviolaceus OPC-520 was cloned in Streptomyces lividans 66. The nucleotide sequence of the gene, which encodes NagA, revealed an open reading frame of 1,896 bp, encoding a protein with an Mr of 66,329. The deduced primary structure of NagA was confirmed by comparison with the N-terminal amino acid
American Society for Microbiology.
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23. Structural Basis for Thermostability of β-Glycosidase from the Thermophilic Eubacterium Thermus nonproteolyticus HG102
The three-dimensional structure of a thermostable β-glycosidase (GlyTn) from the thermophilic eubacterium Thermus nonproteolyticus HG102 was determined at a resolution of 2.4 Å. The core of the structure adopts the (βα)8 barrel fold. The sequence alignments and the positions of the two Glu residues in the active center indicate that GlyTn belongs to the
American Society for Microbiology.
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24. Abnormal fucosylation of-ileal mucus in cystic fibrosis: II. A histochemical study using monoclonal antibodies to fucosyl oligosaccharides.
Abnormal fucosylation of cystic fibrosis mucin was previously shown using peroxidase conjugated lectins on ileal tissue sections. These abnormally fucosylated glycoproteins were investigated further using monoclonal antibodies to fucosyl oligosaccharides based on type 1 and type 2 blood group precursor chains. The results of this study, using monoclonal anti