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evolution
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depending on the presence or absence of the PME inhibitor (PMEI) domain at the N-terminus (also known as the PRO region), PMEs are grouped into either type-1 PME (with PMEI domain) or type-2 PME (without PMEI domain), phylogenetic analysis
evolution
in Arabidopsis thaliana, 66 PMEs and a similarly high number of pectin methylesterase inhibitors, PMEIs, have so far been identified
evolution
sequence comparisons of pectinesterase enzymes from Citrus sinensis, Arabidopsis thaliana, and Botrytis cinerea
evolution
sequence comparisons of pectinesterase enzymes from Citrus sinensis, Arabidopsis thaliana, and Botrytis cinerea
evolution
sequence comparisons of pectinesterase enzymes from Citrus sinensis, Arabidopsis thaliana, and Botrytis cinerea
evolution
the deduced PME-ZJ5A protein structure contains a catalytic domain and a putative N-terminal signal peptide (residues 1-19) of carbohydrate esterase family 8
evolution
the enzyme belongs to the family 8 of carbohydrate esterases (CE8) of the pectin methylesterase superfamily
evolution
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the enzyme belongs to the family of class 8 carbohydrate esterases. PMEs are classified into either Type-1 (with a PMEI domain at the N-terminus) or Type-2 (no PMEI domain). The highest PME activity is detected in samples isolated from green fruits, whereas soluble proteins isolated from green and red fruit possess the lowest PMEI inhibitor activity. Root and stems possess high PME activities, while low activities are detected in leaf tissues, suggesting that vegetative tissues also undergo dynamic pectin modification
evolution
thermostable pectin methylesterase (CtPME) from Clostridium thermocellum belongs to family 8 carbohydrate esterase (CE8)
evolution
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the enzyme belongs to the family 8 of carbohydrate esterases (CE8) of the pectin methylesterase superfamily
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evolution
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the enzyme belongs to the family 8 of carbohydrate esterases (CE8) of the pectin methylesterase superfamily
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evolution
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the deduced PME-ZJ5A protein structure contains a catalytic domain and a putative N-terminal signal peptide (residues 1-19) of carbohydrate esterase family 8
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evolution
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in Arabidopsis thaliana, 66 PMEs and a similarly high number of pectin methylesterase inhibitors, PMEIs, have so far been identified
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evolution
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the enzyme belongs to the family 8 of carbohydrate esterases (CE8) of the pectin methylesterase superfamily
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evolution
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thermostable pectin methylesterase (CtPME) from Clostridium thermocellum belongs to family 8 carbohydrate esterase (CE8)
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evolution
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the enzyme belongs to the family 8 of carbohydrate esterases (CE8) of the pectin methylesterase superfamily
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evolution
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the enzyme belongs to the family 8 of carbohydrate esterases (CE8) of the pectin methylesterase superfamily
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evolution
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the enzyme belongs to the family 8 of carbohydrate esterases (CE8) of the pectin methylesterase superfamily
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evolution
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sequence comparisons of pectinesterase enzymes from Citrus sinensis, Arabidopsis thaliana, and Botrytis cinerea
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malfunction
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the number of adventitious roots is 30% increased in the pme3-1 mutant
malfunction
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loss-of-function mutant alleles of pectin methylesterase35 show a pendant stem phenotype and an increased deformation rate of the stem
malfunction
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suppressing expression of PMEs in tomato fruit reduces the amount of Ca2+ bound to the cell wall, and also reduces fruit susceptibility to Blossom-end rot
malfunction
a defect in mucilage extrusion is observed in a PME6 mutant and is shown to be a pleiotropic effect of the changes in embryo. hms-1 Embryo defect phenotype, the embryo cell size is decreased, the hms-1 radicals and cotyledons both have a reduced cell perimeter compared with the wild-type, overview. The PME activity is decreased and the degree of methyl esterification is increased in hms-1 7-DPA mutant seeds
malfunction
Atpme3-1 loss-of-function mutants exhibit phenotypes distinct from the wild-type, and show earlier germination and reduction of root hair production, correlated with the accumulation of a 21.5-kDa protein in the different organs of 4-day-old Atpme3-1 seedlings grown in the dark, as well as in 6-week-old mutant plants. Microarray analysis shows significant downregulation of the genes encoding several pectin-degrading enzymes and enzymes involved in lipid and protein metabolism in the hypocotyl of 4-day-old dark grown mutant seedlings. Accordingly, there is a decrease in proteolytic activity of the mutant as compared with the wild-type. Among the genes specifying seed storage proteins, two encoding cruciferins are upregulated. Overexpression of four cruciferin genes in the mutant Atpme3-1, in which precursors of the alpha- and beta-subunits of CRUCIFERIN accumulate
malfunction
expression analysis of enzyme inhibiting PMEI genes in response to male sterility, overview
malfunction
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inhibition of the activation of the enzyme PME retardes the hydrolysis of pectin and texture softening during storage, e.g. by lowering pH and ethylene concentration
malfunction
mutations in the pglA, pmt, pel and pelL genes have minimal effects on virulence
malfunction
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mutations in the pglA, pmt, pel and pelL genes have minimal effects on virulence
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malfunction
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mutations in the pglA, pmt, pel and pelL genes have minimal effects on virulence
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malfunction
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Atpme3-1 loss-of-function mutants exhibit phenotypes distinct from the wild-type, and show earlier germination and reduction of root hair production, correlated with the accumulation of a 21.5-kDa protein in the different organs of 4-day-old Atpme3-1 seedlings grown in the dark, as well as in 6-week-old mutant plants. Microarray analysis shows significant downregulation of the genes encoding several pectin-degrading enzymes and enzymes involved in lipid and protein metabolism in the hypocotyl of 4-day-old dark grown mutant seedlings. Accordingly, there is a decrease in proteolytic activity of the mutant as compared with the wild-type. Among the genes specifying seed storage proteins, two encoding cruciferins are upregulated. Overexpression of four cruciferin genes in the mutant Atpme3-1, in which precursors of the alpha- and beta-subunits of CRUCIFERIN accumulate
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malfunction
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mutations in the pglA, pmt, pel and pelL genes have minimal effects on virulence
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metabolism
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the role of PME on CH4 efflux potential is examined. PME is found to substantially reduce the potential for aerobic CH4 emissions upon demethylation of pectin
metabolism
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the role of PME on CH4 efflux potential is examined. PME is found to substantially reduce the potential for aerobic CH4 emissions upon demethylation of pectin
metabolism
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the role of PME on CH4 efflux potential is examined. PME is found to substantially reduce the potential for aerobic CH4 emissions upon demethylation of pectin
metabolism
guard cell walls concerted with the action of cell-wall enzymes, acting on the cell wall polymers for stomatal movements, regulation, overview
physiological function
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compared to six fruit rot fungi, Aspergillus niger and Aspergillus flavus produce higher PME after 14 days of incubation and in both these species are responsible for higher PME after 4 days of incubation in grape juice extract
physiological function
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compared to six fruit rot fungi, Aspergillus niger and Aspergillus flavus produce higher PME after 14 days of incubation and in both these species are responsible ofr higher PME after 4 days of incubation period in grape juice extract
physiological function
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although foliar pectin methylesterase activity is related to methanol emission, other factors must also be considered when predicting methanol emission
physiological function
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in tubers containing a higher level of total PME activity, there is a reduced degree of methylation of cell wall pectin and consistently higher peak force and work done values during the fracture of cooked tuber samples
physiological function
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in tubers containing a higher level of total PME activity, there is a reduced degree of methylation of cell wall pectin and consistently higher peak force and work done values during the fracture of cooked tuber samples
physiological function
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isoform PME3 plays a role in adventitious rooting
physiological function
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the enzyme is involved in the metabolism (i.e., remodelling) of the cell-wall pectin and, hence, takes part in important physiological processes associated with both vegetative and reproductive plant development, including cell wall extension and stiffening, cellular adhesion and separation, fruit ripening, wood development, stem elongation, leaf growth, microsporogenesis, seed germination, and pollen tube growth. In addition, the enzyme is associated with plant defence responses upon biotic (including insect herbivory) or abiotic (e.g., cold, wounding) stresses. Pectin methylesterase is a ribosome-inactivating protein, inhibiting the translation process
physiological function
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the enzyme is involved in the metabolism (i.e., remodelling) of the cell-wall pectin and, hence, takes part in important physiological processes associated with both vegetative and reproductive plant development, including cell wall extension and stiffening, cellular adhesion and separation, fruit ripening, wood development, stem elongation, leaf growth, microsporogenesis, seed germination, and pollen tube growth. In addition, the enzyme is associated with plant defence responses upon biotic (including insect herbivory) or abiotic (e.g., cold, wounding) stresses. Pectin methylesterase is a ribosome-inactivating protein, inhibiting the translation process
physiological function
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the recovery of heat shock protein-released Ca2+ in Ca2+-pectate reconstitution through pectin methylesterase activity is required for cell wall remodelling during heat shock protein in soybean which, in turn, retains plasma membrane integrity and co-ordinates with heat shock proteins to confer thermotolerance
physiological function
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high expression of pectin methylesterases increases Ca2+ bound to the cell wall, subsequently decreasing Ca2+ available for other cellular functions and thereby increasing fruit susceptibility to Blossom-end rot
physiological function
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isoform PME3 acts as a susceptibility factor and is required for the initial colonization of the host tissue by Pectobacterium carotovorum and Botrytis cinerea
physiological function
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isoform PME35-mediated demethylesterification of the primary cell wall directly regulates the mechanical strength of the supporting tissue
physiological function
the enzyme catalyzes the de-methylesterification of pectin in plant cell walls during cell elongation
physiological function
Aspergillus niger contains a non-processive, salt-requiring, and acidophilic pectin methylesterase
physiological function
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enzyme pectin methylesterase catalyzes hydrolysis of the methoxyl group of pectins, producing pectin acid. The decrease in the degree of pectin methoxylation may, in turn, trigger various processes that can affect fruit texture and firmness. PME activity is related to fruit softening with the disintegration of the cell wall and modifications of the pectin fraction. Because their principal substrate is the methoxyl group of pectins, hydrolysis of these compounds occurs. The fruits pass from the ripe to overripe stage with increased pectin hydrolysis. Activity of pectin methylesterase affets the layer of candeuba wax solid lipid nanoparticles (SLN) and xanthan gum (XG, xanthan gum derived from Xanthomonas campestris) as coatings on guava fruits, that shall inhibit the maturation process of the fruits. The best results are achieved from the fruits coated with 65 g/L of SLN and stored at 10°C, as they show the lowest O2 and CO2 respiration rates and, consequently, less weight loss. They also have the best retention of ascorbic acid and total phenol content, with less change in fruit color compared to the control guava and those coated only with XG. These findings indicate that this batch continues the natural maturation process, but at a slower rate than the other samples. The firmness is affected by the activity of the enzyme pectin methylesterase, but results show that the 65 g/l coating is efficient in maintaining fruit texture. 75 g/l Coating produces epoxy compounds in the fruit, causing physiological damage, and the guava coated with XG only have a maturation rate similar to that of the control fruit. Coating with lower concentration of submicron particles presenting a greater firmness can be related to its higher total phenol content, phenolic-pectin interactions demonstrate conservation of cell wall integrity explained by the cross-linking between a hydroxycinnamic acid, such as gallic acid, and the polysaccharide, such as pectin, in the cell wall, which leads to the formation of esterified phenolic compounds. This crosslinking may increase plant cell wall rigidity which helps to preserve firmness
physiological function
functional properties of pectin rely on molecular weight and degree of esterification, and thus deesterification by PME influences the pectin functionality
physiological function
highly methyl esterified seeds' (gene PME6) is a pectin methyl esterase involved in embryo development, it is required for normal embryo development. Enzyme HMS causes the softening of plant tissues. Isozyme HMS plays an important role in embryo growth
physiological function
pectin is an important cell wall polysaccharide required for cellular adhesion, extension, and plant growth. The pectic methylesterification status of guard cell walls influences the movement of stomata in response to different stimuli. Pectin methylesterase (PME) has a profound effect on cell wall modification, especially on the degree of pectic methylesterification during heat response. Isozyme PME34 plays a significant role in heat tolerance through the regulation of stomatal movement, PME34 specifically regulates stomatal aperture in response to heat, overview. The opening and closure of stomata is mediated by changes in response to a given stimulus, might require a specific cell wall modifying enzyme to function properly
physiological function
pectin methylesterases (PMEs) are present in phytopathogens such as bacteria and fungi
physiological function
pectin methylesterases (PMEs) belonging to carbohydrate esterase family 8 cleave the ester bond between a galacturonic acid and an methyl group. The resulting change in methylesterification level plays an important role during the growth and development of plants. Optimal pectin methylesterification status in each cell type is determined by the balance between PME activity and posttranslational PME inhibition by PME inhibitors (PMEIs)
physiological function
pectin methylesterases (PMEs) play a central role in pectin remodeling during plant development
physiological function
pectin methylesterases (PMEs) play a central role in pectin remodeling during plant development
physiological function
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pectin, which is enriched in primary cell walls and middle lamellae, is an essential polysaccharide in all higher plants. Homogalacturonans (HGA), a major form of pectin, are synthesized and methylesterified by enzymes localized in the Golgi apparatus and transported into the cell wall. Depending on cell type, the degree and pattern of pectin methylesterification are strictly regulated by cell wall-localized pectin methylesterases (PMEs). The removal of methyl groups by PMEs play important roles in rice growth and development. Optimal pectin methylesterification status in each cell type is determined by the balance between PME activity and posttranslational PME inhibition by PME inhibitors (PMEIs)
physiological function
plant and bacterial pectin methylesterases (PMEs) perform the catalysis with a processive catalytic mechanism, unlike fungal PME whose activity leads to a random repartition of non-esterified carboxyl groups
physiological function
presence of four pectin homogalacturonan (HG) degrading genes in the genome of Xoo. The four HG degrading genes include one polygalacturonase (pglA), one pectin methyl esterase (pmt) and two pectate lyases (pel and pelL). PglA is the major pectin degrading enzyme produced by Xoo. The pectin methyl esterase, Pmt, is the pectin deesterifying enzyme secreted by Xoo as evident from the enzymatic activity assay performed using pectin as the substrate. Compared to cellulases and xylanases, the HG degrading enzymes may not have a major role in the pathogenicity of strain BXO43
physiological function
regulation of enzyme PME may control the physical properties and structure of the plant cell wall. Evidence for a link between AtPME3, present in the cell wall, and CRUCIFERIN metabolism that occurs in vacuoles is provided
physiological function
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presence of four pectin homogalacturonan (HG) degrading genes in the genome of Xoo. The four HG degrading genes include one polygalacturonase (pglA), one pectin methyl esterase (pmt) and two pectate lyases (pel and pelL). PglA is the major pectin degrading enzyme produced by Xoo. The pectin methyl esterase, Pmt, is the pectin deesterifying enzyme secreted by Xoo as evident from the enzymatic activity assay performed using pectin as the substrate. Compared to cellulases and xylanases, the HG degrading enzymes may not have a major role in the pathogenicity of strain BXO43
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physiological function
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presence of four pectin homogalacturonan (HG) degrading genes in the genome of Xoo. The four HG degrading genes include one polygalacturonase (pglA), one pectin methyl esterase (pmt) and two pectate lyases (pel and pelL). PglA is the major pectin degrading enzyme produced by Xoo. The pectin methyl esterase, Pmt, is the pectin deesterifying enzyme secreted by Xoo as evident from the enzymatic activity assay performed using pectin as the substrate. Compared to cellulases and xylanases, the HG degrading enzymes may not have a major role in the pathogenicity of strain BXO43
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physiological function
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regulation of enzyme PME may control the physical properties and structure of the plant cell wall. Evidence for a link between AtPME3, present in the cell wall, and CRUCIFERIN metabolism that occurs in vacuoles is provided
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physiological function
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pectin methylesterases (PMEs) are present in phytopathogens such as bacteria and fungi
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physiological function
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presence of four pectin homogalacturonan (HG) degrading genes in the genome of Xoo. The four HG degrading genes include one polygalacturonase (pglA), one pectin methyl esterase (pmt) and two pectate lyases (pel and pelL). PglA is the major pectin degrading enzyme produced by Xoo. The pectin methyl esterase, Pmt, is the pectin deesterifying enzyme secreted by Xoo as evident from the enzymatic activity assay performed using pectin as the substrate. Compared to cellulases and xylanases, the HG degrading enzymes may not have a major role in the pathogenicity of strain BXO43
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additional information
analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
additional information
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analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
additional information
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meta-analysis of biotic stress responsive expression of Oryza sativa PMEs
additional information
molecular dynamics simulations and electrostatic potential calculations. The substrate-binding groove is negatively charged. Enzyme sequence and activity comparisons to processive pectin methylesterases, e.g. from Aspergillus (Emericella) nidulans and Trichoderma reesei (Hypocrea jecorina), overview. Detailed structure analysis of a fungal isozyme Ani-PME2, which, while preserving key active-site residues, has distinctly different loop structures and surface electrostatic potential compared with plant, bacterial, and insect PMEs, molecular dynamics simulations on Ani-PME2. Homology modeling of the structure of isozyme Ani-PME1
additional information
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molecular dynamics simulations and electrostatic potential calculations. The substrate-binding groove is negatively charged. Enzyme sequence and activity comparisons to processive pectin methylesterases, e.g. from Aspergillus (Emericella) nidulans and Trichoderma reesei (Hypocrea jecorina), overview. Detailed structure analysis of a fungal isozyme Ani-PME2, which, while preserving key active-site residues, has distinctly different loop structures and surface electrostatic potential compared with plant, bacterial, and insect PMEs, molecular dynamics simulations on Ani-PME2. Homology modeling of the structure of isozyme Ani-PME1
additional information
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analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
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additional information
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analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
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additional information
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analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
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additional information
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analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
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additional information
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analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
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additional information
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analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
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