grafit version 7.0.2 (ERITHACUS SOFTWARE LIMITED)
90
Structured Review
ERITHACUS SOFTWARE LIMITED
grafit version 7.0.2
Grafit Version 7.0.2, supplied by ERITHACUS SOFTWARE LIMITED, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/grafit+version+7%2E0%2E2/grafit+5/pm40121185-74-14-17
Average 90 stars, based on 1 article reviews
Grafit Version 7.0.2, supplied by ERITHACUS SOFTWARE LIMITED, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/grafit+version+7%2E0%2E2/grafit+5/pm40121185-74-14-17
Average 90 stars, based on 1 article reviews
grafit version 7.0.2 - by Bioz Stars,
2026-11
90/100 stars
Images
Related Articles
Activity Assay:Article Title: Discovery of solabiose phosphorylase and its application for enzymatic synthesis of solabiose from sucrose and lactose. Article Snippet: 1) was fitted to the reaction rates at various substate concentrations using Article Title: Alteration of Substrate Specificity and Transglucosylation Activity of GH13_31 α-Glucosidase from Bacillus sp. AHU2216 through Site-Directed Mutagenesis of Asn258 on β→α Loop 5. Article Snippet: Non-linear regression of the rate equations to reaction rates was carried out using Article Title: Biochemical characteristics of maltose phosphorylase MalE from Bacillus sp. AHU2001 and chemoenzymatic synthesis of oligosaccharides by the enzyme. Article Snippet: The kinetic parameters were calculated by fitting the reaction equation Equation (1) for a sequential Bi–Bi mechanism [39] to the reaction rates with Grafit version 7.0.2 ( Article Title: Function and structure of GH13_31 α-glucosidase with high α-(1→4)-glucosidic linkage specificity and transglucosylation activity. Article Snippet: Article Title: Effect of C-6 Methylol Groups on Substrate Recognition of Glucose/Xylose Mixed Oligosaccharides by Cellobiose Dehydrogenase from the Basidiomycete Phanerochaete chrysosporium Article Snippet: Each measurement was done in triplicate unless otherwise noted, and steady-state kinetic parameters ( K m and k cat ) were estimated by non-linear fitting of the data to the Michaelis-Menten equation using Article Title: Biochemical and structural characterization of Marinomonas mediterranead-mannose isomerase Marme_2490 phylogenetically distant from known enzymes. Article Snippet: D-Mannose isomerase (MI) reversibly isomerizes D-mannose to D-fructose, and is attractive for producing D-mannose from inexpensive D-fructose.. It belongs to the N-acylglucosamine 2-epimerase (AGE) superfamily along with AGE, cellobiose 2-epimerase (CE), and aldose-ketose isomerase (AKI).. In this study, Marinomonas mediterranea Marme_2490, showing low sequence identity with any known enzymes, was found to isomerize D-mannose as its primary substrate. Article Title: Substrate specificity of glycoside hydrolase family 1 β-glucosidase AtBGlu42 from Arabidopsis thaliana and its molecular mechanism. Article Snippet: Fitting was done using Article Title: Biochemical and structural analysis of the mechanism for the catalysis and specificity of cellobiose 2-epimerase from Rhodothermus marinus. Article Snippet: ion of the 2-H of the aldehyde form of the D-mannose residue.. As the sugar alcohol residues of mannitol and cellobiitol adopted a similar orientation, and 2-C of the sugar alcohol residues was located at the intermediate position of the two catalytic His residues (Fig. 1(c)), 2-C of the cis-enediolate intermediate was also predicted to be located at the intermediate position of the two catalytic His residues for reversible epimerization.. The complete loss of epilactoseand lactose-producing activity toward lactulose in H259A and H390A, respectively, indicates that His259 and His390 protonate the intermediate to produce D-mannose and D-glucose residues, respectively, as the general acid catalyst (Fig. 4). Recombinant:Article Title: Discovery of solabiose phosphorylase and its application for enzymatic synthesis of solabiose from sucrose and lactose. Article Snippet: 1) was fitted to the reaction rates at various substate concentrations using Article Title: Alteration of Substrate Specificity and Transglucosylation Activity of GH13_31 α-Glucosidase from Bacillus sp. AHU2216 through Site-Directed Mutagenesis of Asn258 on β→α Loop 5. Article Snippet: Non-linear regression of the rate equations to reaction rates was carried out using Article Title: Biochemical characteristics of maltose phosphorylase MalE from Bacillus sp. AHU2001 and chemoenzymatic synthesis of oligosaccharides by the enzyme. Article Snippet: The kinetic parameters were calculated by fitting the reaction equation Equation (1) for a sequential Bi–Bi mechanism [39] to the reaction rates with Grafit version 7.0.2 ( Article Title: Function and structure of GH13_31 α-glucosidase with high α-(1→4)-glucosidic linkage specificity and transglucosylation activity. Article Snippet: Article Title: Effect of C-6 Methylol Groups on Substrate Recognition of Glucose/Xylose Mixed Oligosaccharides by Cellobiose Dehydrogenase from the Basidiomycete Phanerochaete chrysosporium Article Snippet: Each measurement was done in triplicate unless otherwise noted, and steady-state kinetic parameters ( K m and k cat ) were estimated by non-linear fitting of the data to the Michaelis-Menten equation using Article Title: Biochemical and structural characterization of Marinomonas mediterranead-mannose isomerase Marme_2490 phylogenetically distant from known enzymes. Article Snippet: D-Mannose isomerase (MI) reversibly isomerizes D-mannose to D-fructose, and is attractive for producing D-mannose from inexpensive D-fructose.. It belongs to the N-acylglucosamine 2-epimerase (AGE) superfamily along with AGE, cellobiose 2-epimerase (CE), and aldose-ketose isomerase (AKI).. In this study, Marinomonas mediterranea Marme_2490, showing low sequence identity with any known enzymes, was found to isomerize D-mannose as its primary substrate. Article Title: Substrate specificity of glycoside hydrolase family 1 β-glucosidase AtBGlu42 from Arabidopsis thaliana and its molecular mechanism. Article Snippet: Fitting was done using Article Title: Biochemical and structural analysis of the mechanism for the catalysis and specificity of cellobiose 2-epimerase from Rhodothermus marinus. Article Snippet: ion of the 2-H of the aldehyde form of the D-mannose residue.. As the sugar alcohol residues of mannitol and cellobiitol adopted a similar orientation, and 2-C of the sugar alcohol residues was located at the intermediate position of the two catalytic His residues (Fig. 1(c)), 2-C of the cis-enediolate intermediate was also predicted to be located at the intermediate position of the two catalytic His residues for reversible epimerization.. The complete loss of epilactoseand lactose-producing activity toward lactulose in H259A and H390A, respectively, indicates that His259 and His390 protonate the intermediate to produce D-mannose and D-glucose residues, respectively, as the general acid catalyst (Fig. 4). |