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evolution
analysis of evolution of allosteric regulation in plant chorismate mutases
evolution
analysis of evolution of allosteric regulation in plant chorismate mutases. Phylogentically, the AtCM3-like clade is found only in the Brassicaceae, which suggests a possible specialized role for this enzyme in those plants
evolution
evolution of allosteric regulation in plant chorismate mutases, overview
evolution
evolution of allosteric regulation in plant chorismate mutases, overview
evolution
evolution of allosteric regulation in plant chorismate mutases, overview
evolution
isozyme MtbCM belongs to the ?AroQ/AroQc family. The family members exhibit sequence similarity only in the N-terminal moiety, and lack a catalytically crucial and conserved arginine residue in helix H1. The proteins contain a catalytic site which is formed within a single protomer and lacks regulatory domain
evolution
primitive molten globular enzymes might, like mMjCM, have had substantial advantages in forming stronger transition state interactions, since they could be more effective to explore different conformational states favorable to tighter binding of transition state
evolution
the N-terminal domain of DAHPS from Bacillus subtilis is homologous to the AroQ class of chorismate mutase, type II. Bacillus subtilis also contains a monofunctional AroH class of chorismate mutase situated downstream of the shikimate pathway
evolution
there are two classes of chorismate mutase: AroQ and AroH. The bacterial subclass AroQgamma has reported roles in virulence. Chorismate mutase from Burkholderia phymatum has the prototypical AroQgamma topology and retains the characteristic chorismate mutase active site
evolution
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the N-terminal domain of DAHPS from Bacillus subtilis is homologous to the AroQ class of chorismate mutase, type II. Bacillus subtilis also contains a monofunctional AroH class of chorismate mutase situated downstream of the shikimate pathway
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evolution
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isozyme MtbCM belongs to the ?AroQ/AroQc family. The family members exhibit sequence similarity only in the N-terminal moiety, and lack a catalytically crucial and conserved arginine residue in helix H1. The proteins contain a catalytic site which is formed within a single protomer and lacks regulatory domain
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evolution
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there are two classes of chorismate mutase: AroQ and AroH. The bacterial subclass AroQgamma has reported roles in virulence. Chorismate mutase from Burkholderia phymatum has the prototypical AroQgamma topology and retains the characteristic chorismate mutase active site
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malfunction
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single-cell transient-induced gene silencing of CM1 in mildew resistance locus a (Mla) compromised cells results in increased susceptibility to Blumeria graminis f. sp. hordei
malfunction
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Xanthomonas oryzae pv. oryzae chorismate mutase knock-out mutants are hypervirulent to rice
malfunction
compared to wild-type enzyme, decreased levels of Tparo7 expression in the silenced transformants are accompanied by reduced chorismate mutase activity, lower growth rates on different culture media, and reduced mycoparasitic behavior against the phytopathogenic fungi Rhizoctonia solani strain 19, Fusarium oxysporum strain CECT 2866, and Botrytis cinerea strain B05.10 in dual cultures. By contrast, higher amounts of the aromatic metabolites tyrosol, 2-phenylethanol and salicylic acid are detected in supernatants from the silenced transformants, which are able to inhibit the growth of Fusarium oxysporum and Botrytis cinerea. In in vitro plant assays, Tparo7-silenced transformants also show a reduced capacity to colonize tomato roots. The growth of tomato plants colonized by the silenced transformants is reduced and the plants exhibit an increased susceptibility to Bortrytis cinerea in comparison with the responses observed for control plants. In addition, the plants turn yellowish and are defective in jasmonic acid- and ethylene-regulated signaling pathways which is seen by expression analysis of lipoxygenase 1 (LOX1), ethylene-insensitive protein 2 (EIN2) and pathogenesis-related protein 1 (PR-1) genes
malfunction
mutant Arg90Cit, a sluggish variant of Bacillus subtilis chorismate mutase, in which a cationic active-site arginine is replaced by a neutral citrulline, is a poor catalyst even though it effectively preorganizes chorismate for the reaction
malfunction
the inhibition of secretory isozyme MtbCM may hinder the supply of nutrients to the organism
malfunction
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compared to wild-type enzyme, decreased levels of Tparo7 expression in the silenced transformants are accompanied by reduced chorismate mutase activity, lower growth rates on different culture media, and reduced mycoparasitic behavior against the phytopathogenic fungi Rhizoctonia solani strain 19, Fusarium oxysporum strain CECT 2866, and Botrytis cinerea strain B05.10 in dual cultures. By contrast, higher amounts of the aromatic metabolites tyrosol, 2-phenylethanol and salicylic acid are detected in supernatants from the silenced transformants, which are able to inhibit the growth of Fusarium oxysporum and Botrytis cinerea. In in vitro plant assays, Tparo7-silenced transformants also show a reduced capacity to colonize tomato roots. The growth of tomato plants colonized by the silenced transformants is reduced and the plants exhibit an increased susceptibility to Bortrytis cinerea in comparison with the responses observed for control plants. In addition, the plants turn yellowish and are defective in jasmonic acid- and ethylene-regulated signaling pathways which is seen by expression analysis of lipoxygenase 1 (LOX1), ethylene-insensitive protein 2 (EIN2) and pathogenesis-related protein 1 (PR-1) genes
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malfunction
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the inhibition of secretory isozyme MtbCM may hinder the supply of nutrients to the organism
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metabolism
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chorismate mutase is the first and the key enzyme that diverges the shikimate pathway to either tryptophan or phenylalanine and tyrosine
metabolism
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transgenic Arabidopsis plants expressing a truncated, feedback-insensitive chorismate mutase/prephenate dehydratase gene accumulate Phe (up to 100fold compared to control plants) and are more sensitive than wild-type plants to the Trp biosynthesis inhibitor 5-methyl-Trp. Thus Phe biosynthesis competes with Trp biosynthesis from their common precursor chorismate. A number of secondary metabolites derived from all three aromatic amino acids (Phe, Trp and Tyr) are altered in the transgenic plants, implying regulatory cross-interactions between the flux of aromatic amino acid biosynthesis from chorismate and their further metabolism into various secondary metabolites. Truncated PheA expression has a minimal effect on primary metabolism and on the Arabidopsis transcriptome. A high proportion of the feedback-insensitive chorismate mutase/prephenate dehydratase polypeptide produced by this transgene is translocated into the plastids
metabolism
the enzyme is involved in aromatic amino acid biosynthesis
metabolism
anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid
metabolism
anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid
metabolism
anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid
metabolism
anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid buildup of the amino acid
metabolism
chorismate mutase is located at the branch point of the shikimate pathway and channels chorismate into the Tyr/Phe-specific branch. The enzyme catalyzes the conversion of chorismate to prephenate
metabolism
Mycobacterium tuberculosis chorismate mutase (MtbCM) catalyzes the rearrangement of chorismate to prephenate in the shikimate biosynthetic pathway which forms the essential amino acids, phenylalanine and tyrosine
metabolism
the enzyme is involved in L-phenylalanine biosynthesis pathway
metabolism
the enzyme plays a central branch point role in the shikimate pathway, pathway and regulation, overview
metabolism
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the enzyme plays a central branch point role in the shikimate pathway, pathway and regulation, overview
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metabolism
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Mycobacterium tuberculosis chorismate mutase (MtbCM) catalyzes the rearrangement of chorismate to prephenate in the shikimate biosynthetic pathway which forms the essential amino acids, phenylalanine and tyrosine
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physiological function
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CM0819 significantly stimulates 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DS2098) activity, CM0819 interacts with 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase DS2098 from Corynebacterium glutamicum and this interaction results in allosteric regulation of DS2098 synthase activity
physiological function
isoform CM1 is the principal chorismate mutase responsible for the coupling of metabolites from the shikimate pathway to the synthesis of floral volatile benzenoid/phenylpropanoids in the corolla
physiological function
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isochorismate-pyruvate lyase, PchB EC 4.2.99.21, can also perform a nonphysiological role as a chorismate mutase albeit with considerably lower catalytic efficiency
physiological function
AtCM2 is a nonallosteric form
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen re-arrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. Allosteric regulation of plant enzymes, overview
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. Allosteric regulation of plant enzymes, overview
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. Allosteric regulation of plant enzymes, overview
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. The cytosolic chorismate mutase isozyme AtCM2 is unregulated
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. The plastid-localized chorismate mutase isozyme AtCM1 is allosterically regulated. The allosterically regulated chorismate mutases are repressed by tyrosine and phenylalanine and are activated by tryptophan. The aromatic amino acids bind an effector site on the enzyme and regulate the ability of chorismate to bind at the active site for catalysis
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. The plastid-localized chorismate mutase isozyme AtCM3 is allosterically regulated. The allosterically regulated chorismate mutases are repressed by tyrosine and phenylalanine and are activated by tryptophan. The aromatic amino acids bind an effector site on the enzyme and regulate the ability of chorismate to bind at the active site for catalysis
physiological function
enzyme chorismate mutase is a shikimate pathway branch point leading to the production of aromatic amino acids, which are not only essential components of protein synthesis but also the precursors of a wide range of secondary metabolites
physiological function
in Bacillus subtilis, the N-terminal domain of the bifunctional 3-deoxy-D-arabino-heptulosonate-7-phosphate-synthase (DAHPS), the first enzyme of the shikimate pathway, belongs to an AroQ class of chorismate mutase and is functionally homologous to the downstream AroH class chorismate mutase. BsCM_2 has a regulatory function in the bifunctional DAHPS enzyme, regulation of DAHPS enzyme activity by the CM2 domain, overview
physiological function
in Bacillus subtilis, the N-terminal domain of the bifunctional 3-deoxy-D-arabino-heptulosonate-7-phosphate-synthase (DAHPS), the first enzyme of the shikimate pathway, belongs to an AroQ class of chorismate mutase and is functionally homologous to the downstream AroH class chorismate mutase. BsCM_2 may also have a regulatory function in the bifunctional DAHPS enzyme
physiological function
isozyme AtCM1 is alosterically regulated
physiological function
isozyme AtCM3 is alosterically regulated
physiological function
Mycobacterium tuberculosis chorismate mutase (MtbCM) catalyzes the rearrangement of chorismate to prephenate in the shikimate biosynthetic pathway which forms the essential amino acids, phenylalanine and tyrosine. The secretory isozyme MtbCM (encoded by gene Rv1885c) is assumed to play a key role in pathogenesis of tuberculosis. Isozyme MtbCM is independent of regulation
physiological function
the enzyme catalyzes the rearrangement of chorismate to prephenate. Calculations have predicted the decisive factor in chorismate mutase catalysis to be ground state destabilization rather than transition state stabilization
physiological function
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in Bacillus subtilis, the N-terminal domain of the bifunctional 3-deoxy-D-arabino-heptulosonate-7-phosphate-synthase (DAHPS), the first enzyme of the shikimate pathway, belongs to an AroQ class of chorismate mutase and is functionally homologous to the downstream AroH class chorismate mutase. BsCM_2 may also have a regulatory function in the bifunctional DAHPS enzyme
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physiological function
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in Bacillus subtilis, the N-terminal domain of the bifunctional 3-deoxy-D-arabino-heptulosonate-7-phosphate-synthase (DAHPS), the first enzyme of the shikimate pathway, belongs to an AroQ class of chorismate mutase and is functionally homologous to the downstream AroH class chorismate mutase. BsCM_2 has a regulatory function in the bifunctional DAHPS enzyme, regulation of DAHPS enzyme activity by the CM2 domain, overview
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physiological function
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enzyme chorismate mutase is a shikimate pathway branch point leading to the production of aromatic amino acids, which are not only essential components of protein synthesis but also the precursors of a wide range of secondary metabolites
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physiological function
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Mycobacterium tuberculosis chorismate mutase (MtbCM) catalyzes the rearrangement of chorismate to prephenate in the shikimate biosynthetic pathway which forms the essential amino acids, phenylalanine and tyrosine. The secretory isozyme MtbCM (encoded by gene Rv1885c) is assumed to play a key role in pathogenesis of tuberculosis. Isozyme MtbCM is independent of regulation
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additional information
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structure-function relationships of chorismate-utilizing enzymes, structure comparisons, overview
additional information
AroH molecular docking, using crystal structure of BsAroH, PDB ID 2CHT, overview
additional information
AroH molecular docking, using crystal structure of BsAroH, PDB ID 2CHT, overview
additional information
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AroH molecular docking, using crystal structure of BsAroH, PDB ID 2CHT, overview
additional information
enzyme structure analysis, enzyme topology, and conserved residues in the substrate-binding sites of chorismate mutase, overview
additional information
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enzyme structure analysis, enzyme topology, and conserved residues in the substrate-binding sites of chorismate mutase, overview
additional information
isozyme PpCM1 structure-function analysis, structure comparisons, active site and allosteric effector sites of PpCM1, targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
additional information
isozyme PpCM1 structure-function analysis, structure comparisons, active site and allosteric effector sites of PpCM1, targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
additional information
structural basis of ligand binding into the active site of AroQ class of chorismate mutase from crystal structure analysis, conformational flexibility of active site loop, overview. Molecular dynamics results show that helix H2' undergoes uncoiling at the first turn and increases the mobility of loop L1'. The side chains of Arg45, Phe46, Arg52 and Lys76 undergo conformational changes, which may play an important role in DAHPS regulation by the formation of the domain-domain interface. BsCM_2 active site architecture and its regulatory role, molecular dynamics simulation, overview
additional information
structural basis of ligand binding into the active site of AroQ class of chorismate mutase from crystal structure analysis, conformational flexibility of active site loop, overview. Molecular dynamics results show that helix H2' undergoes uncoiling at the first turn and increases the mobility of loop L1'. The side chains of Arg45, Phe46, Arg52 and Lys76 undergo conformational changes, which may play an important role in DAHPS regulation by the formation of the domain-domain interface. BsCM_2 active site architecture and its regulatory role, molecular dynamics simulation, overview
additional information
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structural basis of ligand binding into the active site of AroQ class of chorismate mutase from crystal structure analysis, conformational flexibility of active site loop, overview. Molecular dynamics results show that helix H2' undergoes uncoiling at the first turn and increases the mobility of loop L1'. The side chains of Arg45, Phe46, Arg52 and Lys76 undergo conformational changes, which may play an important role in DAHPS regulation by the formation of the domain-domain interface. BsCM_2 active site architecture and its regulatory role, molecular dynamics simulation, overview
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
additional information
the crystal structure of AtCM1 in complex with tyrosine and phenylalanine identifies differences in the effector sites of the allosterically regulated yeast enzyme and the other two Arabidopsis isoforms. The catalytic efficiency (kcat/Km) of AtCM2 is 11 and 22fold higher than that of AtCM1 and AtCM3, respectively. This results from a combination of a more rapid turnover rate and a lower Km value for chorismate displayed by AtCM2 compared with the other two isoforms. Two catalytic residues (Arg229 and Lys240 in AtCM1) are invariant across the AtCM isoforms. These two basic residues are essential for substrate binding, orient the two negatively charged carboxylic acids of chorismate, and provide transition state stabilization during catalysis
additional information
the crystal structure of AtCM1 in complex with tyrosine and phenylalanine identifies differences in the effector sites of the allosterically regulated yeast enzyme and the other two Arabidopsis isoforms. The catalytic efficiency (kcat/Km) of AtCM2 is 11 and 22fold higher than that of AtCM1 and AtCM3, respectively. This results from a combination of a more rapid turnover rate and a lower Km value for chorismate displayed by AtCM2 compared with the other two isoforms. Two catalytic residues (Arg229 and Lys240 in AtCM1) are invariant across the AtCM isoforms. These two basic residues are essential for substrate binding, orient the two negatively charged carboxylic acids of chorismate, and provide transition state stabilization during catalysis
additional information
the crystal structure of AtCM1 in complex with tyrosine and phenylalanine identifies differences in the effector sites of the allosterically regulated yeast enzyme and the other two Arabidopsis isoforms. The catalytic efficiency (kcat/Km) of AtCM2 is 11 and 22fold higher than that of AtCM1 and AtCM3, respectively. This results from a combination of a more rapid turnover rate and a lower Km value for chorismate displayed by AtCM2 compared with the other two isoforms. Two catalytic residues (Arg229 and Lys240 in AtCM1) are invariant across the AtCM isoforms. These two basic residues are essential for substrate binding, orient the two negatively charged carboxylic acids of chorismate, and provide transition state stabilization during catalysis
additional information
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the crystal structure of AtCM1 in complex with tyrosine and phenylalanine identifies differences in the effector sites of the allosterically regulated yeast enzyme and the other two Arabidopsis isoforms. The catalytic efficiency (kcat/Km) of AtCM2 is 11 and 22fold higher than that of AtCM1 and AtCM3, respectively. This results from a combination of a more rapid turnover rate and a lower Km value for chorismate displayed by AtCM2 compared with the other two isoforms. Two catalytic residues (Arg229 and Lys240 in AtCM1) are invariant across the AtCM isoforms. These two basic residues are essential for substrate binding, orient the two negatively charged carboxylic acids of chorismate, and provide transition state stabilization during catalysis
additional information
the enzyme is a chorismate mutase with AroQgamma topology, enzyme structure analysis, enzyme topology, and conserved residues in the substrate-binding sites of chorismate mutase, overview
additional information
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the enzyme is a chorismate mutase with AroQgamma topology, enzyme structure analysis, enzyme topology, and conserved residues in the substrate-binding sites of chorismate mutase, overview
additional information
wild-type and molten globular chorismate mutase achieve comparable catalytic rates using very different enthalpy/entropy compensations, analysis using ab initio quantum mechanical/molecular mechanical minimum free-energy path method, overview. Site-specific, non-uniform rigidity changes of the enzymes during catalysis. The change of conformational entropy from the ground state to the transition state revealed distinctly contrasting entropy/enthalpy compensations in the dimeric wild-type enzyme and its molten globular monomeric variant. Molecular dynamics simulations
additional information
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AroH molecular docking, using crystal structure of BsAroH, PDB ID 2CHT, overview
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additional information
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structural basis of ligand binding into the active site of AroQ class of chorismate mutase from crystal structure analysis, conformational flexibility of active site loop, overview. Molecular dynamics results show that helix H2' undergoes uncoiling at the first turn and increases the mobility of loop L1'. The side chains of Arg45, Phe46, Arg52 and Lys76 undergo conformational changes, which may play an important role in DAHPS regulation by the formation of the domain-domain interface. BsCM_2 active site architecture and its regulatory role, molecular dynamics simulation, overview
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additional information
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the enzyme is a chorismate mutase with AroQgamma topology, enzyme structure analysis, enzyme topology, and conserved residues in the substrate-binding sites of chorismate mutase, overview
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additional information
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enzyme structure analysis, enzyme topology, and conserved residues in the substrate-binding sites of chorismate mutase, overview
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