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evolution
the enzyme belongs to the glycosyl hydrolae famiyl 5, GH5
evolution
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the enzyme belongs to the glycosyl hydrolase family 5, GH5
evolution
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the enzyme belongs to the glycosyl hydrolase family 5, GH5
evolution
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the enzyme belongs to the glycosyl hydrolase family 5, GH5
evolution
the enzyme belongs to the glycosyl hydrolase family 5, GH5
evolution
the enzyme belongs to the glycosyl hydrolase family 5, GH5
evolution
the enzyme belongs to the glycosyl hydrolase family 5, GH5, structure comparisons, the overall fold of the enzyme is strongly conserved, overview. The enzyme displays the typical (beta/alpha)8-barrel fold and a unique structural arrangement of three surface loops that stretch over the active centre, promoting an altered topography of the binding cleft
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5, structure comparisons, the overall fold of the enzyme is strongly conserved, overview. The enzyme displays the typical (beta/alpha)8-barrel fold and a unique structural arrangement of three surface loops that stretch over the active centre, promoting an altered topography of the binding cleft
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evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 5, GH5
-
evolution
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the enzyme belongs to the glycosyl hydrolase family 5, GH5
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metabolism
key enzyme for hydrolyzing mannan, a major constituent of hemicellulose
metabolism
the enzyme is involved in the hydrolysis of plant cell wall mannans and heteromannans
metabolism
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key enzyme for hydrolyzing mannan, a major constituent of hemicellulose
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physiological function
when endo-beta-mannanase activity is much reduced by RNAi and antisense RNA strategies, their firmness is higher compared to those of control fruits at the turning and orange-color stages, but at the red-ripe stage firmness is similar between the two fruit-types
physiological function
enzyme strongly binds to ivory nut mannan, Avicel, chitosan, and chitin, but does not attach to curdlan, insoluble oat spelt xylan, lignin, or poly(3-hydroxybutyrate)
physiological function
germination time in T-DNA insertion mutant almost doubles compared to wild-type. Enzyme is important for the germination of Arabidopsis thaliana seeds by facilitating the hydrolysis of the mannan-rich endosperm cell walls
physiological function
T-DNA insertion mutant germinates later than the wild type. Enzyme is important for the germination of Arabidopsis thaliana seeds by facilitating the hydrolysis of the mannan-rich endosperm cell walls
physiological function
the enzyme beta-mannanase is responsible for the cleavage of beta-1,4-linked internal linkages of the mannan polymer to produce new chain ends
physiological function
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strain is not an effective producer of mannan-degrading enzymes. Oat spelt xylan is the best inducer of mannanase, feruloyl esterase, arabinofuranosidase, glucosidase and acetyl xylan esterase
physiological function
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enzyme strongly binds to ivory nut mannan, Avicel, chitosan, and chitin, but does not attach to curdlan, insoluble oat spelt xylan, lignin, or poly(3-hydroxybutyrate)
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physiological function
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strain is not an effective producer of mannan-degrading enzymes. Oat spelt xylan is the best inducer of mannanase, feruloyl esterase, arabinofuranosidase, glucosidase and acetyl xylan esterase
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physiological function
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the enzyme beta-mannanase is responsible for the cleavage of beta-1,4-linked internal linkages of the mannan polymer to produce new chain ends
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additional information
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catalytic residues are Glu181 as catalytic acid/base and Glu288 as nucleophile, molecular docking study with different manno-configured ligands from mannobiose to mannohexose as well as galactomannan. The ability to accommodate larger ligand molecules in the active site of CtManT is probably due to the long loops enclosing the active site that provides the depth of the cavity, structure overview
additional information
tertiary structure, active site and substrate binding site structures analysis, detailed overview. Two tryptophan residues that provide the hydrophobic stacking of the +1 subsite Trp125 and Trp271,is 9.5 A, making bulkier branched substrates difficult to accommodate
additional information
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tertiary structure, active site and substrate binding site structures analysis, detailed overview. Two tryptophan residues that provide the hydrophobic stacking of the +1 subsite Trp125 and Trp271,is 9.5 A, making bulkier branched substrates difficult to accommodate
additional information
the enzyme has an extended loop that alters topography of the active site, structural and mutational analyses, overview. The extended loop is linked to the cold-adapted enzymatic activity, structure of mannose-recognition subsites. Glu181 and Glu312 are highly conserved catalytic residues, Glu181 is the catalytic acid/base, and Glu312 is the nucleophile. Trp341, which is located in the vicinity of the catalytic residues, acts as a hydrophobic platform for sugar binding in catalytic site, the enzyme also has a second mannan binding site. Sequence comparisons, overview
additional information
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the enzyme has an extended loop that alters topography of the active site, structural and mutational analyses, overview. The extended loop is linked to the cold-adapted enzymatic activity, structure of mannose-recognition subsites. Glu181 and Glu312 are highly conserved catalytic residues, Glu181 is the catalytic acid/base, and Glu312 is the nucleophile. Trp341, which is located in the vicinity of the catalytic residues, acts as a hydrophobic platform for sugar binding in catalytic site, the enzyme also has a second mannan binding site. Sequence comparisons, overview
additional information
the enzyme is composed of three distinct domains and shows some level of molecular flexibility in solution, nevertheless it has a preferred conformation, which can be described by the rigid-body modeling procedure, structure analysis. The enzyme contains a linker with a compact structure that occupies a small volume with respect to its large number of amino acids, role of the length and flexibility of the linker on the spatial arrangement of the constitutive domains. The linker can optimize the geometry between the other two domains with respect to the substrate at high temperatures. The hydrodynamic radii of full-length enzyme and single catalytic domain are independent of protein concentration over the range 0.5 to 8 mg/ml at 20°C and pH 6
additional information
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the enzyme is composed of three distinct domains and shows some level of molecular flexibility in solution, nevertheless it has a preferred conformation, which can be described by the rigid-body modeling procedure, structure analysis. The enzyme contains a linker with a compact structure that occupies a small volume with respect to its large number of amino acids, role of the length and flexibility of the linker on the spatial arrangement of the constitutive domains. The linker can optimize the geometry between the other two domains with respect to the substrate at high temperatures. The hydrodynamic radii of full-length enzyme and single catalytic domain are independent of protein concentration over the range 0.5 to 8 mg/ml at 20°C and pH 6
additional information
the structure of the catalytic domain reveals a canonical (alpha/beta)8-barrel scaffold surrounded by loops and short helices that form the catalytic interface, subsites forming the active-site cleft with residues W134, E198, R200, E235, H283 and W284 are directly involved in glucose binding, structure analysis of full-length enzyme and catalytic domain, overview
additional information
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the structure of the catalytic domain reveals a canonical (alpha/beta)8-barrel scaffold surrounded by loops and short helices that form the catalytic interface, subsites forming the active-site cleft with residues W134, E198, R200, E235, H283 and W284 are directly involved in glucose binding, structure analysis of full-length enzyme and catalytic domain, overview
additional information
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tertiary structure, active site and substrate binding site structures analysis, detailed overview. Two tryptophan residues that provide the hydrophobic stacking of the +1 subsite Trp125 and Trp271,is 9.5 A, making bulkier branched substrates difficult to accommodate
-
additional information
-
catalytic residues are Glu181 as catalytic acid/base and Glu288 as nucleophile, molecular docking study with different manno-configured ligands from mannobiose to mannohexose as well as galactomannan. The ability to accommodate larger ligand molecules in the active site of CtManT is probably due to the long loops enclosing the active site that provides the depth of the cavity, structure overview
-
additional information
-
the structure of the catalytic domain reveals a canonical (alpha/beta)8-barrel scaffold surrounded by loops and short helices that form the catalytic interface, subsites forming the active-site cleft with residues W134, E198, R200, E235, H283 and W284 are directly involved in glucose binding, structure analysis of full-length enzyme and catalytic domain, overview
-
additional information
-
the enzyme is composed of three distinct domains and shows some level of molecular flexibility in solution, nevertheless it has a preferred conformation, which can be described by the rigid-body modeling procedure, structure analysis. The enzyme contains a linker with a compact structure that occupies a small volume with respect to its large number of amino acids, role of the length and flexibility of the linker on the spatial arrangement of the constitutive domains. The linker can optimize the geometry between the other two domains with respect to the substrate at high temperatures. The hydrodynamic radii of full-length enzyme and single catalytic domain are independent of protein concentration over the range 0.5 to 8 mg/ml at 20°C and pH 6
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