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Results 1 - 10 of 11 > >>
EC Number General Information Commentary Reference
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10evolution PAM enzyme structures comparisons, overview 747670
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10evolution structural determinant that dictates the activity differences between a phenylalanine ammonia lyase (PAL, EC 4.3.1.24) and aminomutase (PAM), overview. An inner loop region closes the active sites of both PAM and PAL. The inner loop is a structural determinant of the lyase and mutase activities of PAM. Three-dimensional structure comparisons of Taxus canadensis PAM with PAM from Taxus chinensis and phenylalanine ammonia lyase from Petroselinum crispum (PcPAL) 746591
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10evolution structural determinant that dictates the activity differences between a phenylalanine ammonia lyase (PAL, EC 4.3.1.24) and aminomutase (PAM), overview. An inner loop region closes the active sites of both PAM and PAL. The inner loop is a structural determinant of the lyase and mutase activities of PAM. Three-dimensional structure comparisons of Taxus chinensis PAM with PAM from Taxus canadensis and phenylalanine ammonia lyase from Petroselinum crispum (PcPAL) 746591
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10evolution the enzyme belongs to the MIO-dependent aminomutases. Aminomutases (defined as isomerases mediating intramolecular transfer of amino groups) catalyze the synthetically challenging shift of an amine group along a saturated carbon chain, typically of an amino acid. PAMs and tyrosine aminomutases (TAMs) share the same structure, mechanistic pathway, and characteristics of phenylalanine ammonia-lyases (PALs), histidine ammonia-lyases (HALs), and tyrosine ammonia-lyases (TALs), being all members of the same MIO-dependent enzyme family, also called class I lyase-like enzymes 747524
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10metabolism phenylalanine aminomutase (PAM) catalyzes the 2,3-shift of the alpha-amino group of L-phenylalanine and L-tyrosine to afford beta-phenylalanine. Biocatalytic strategies for the production of (R)- or (S)-beta-arylalanines employing enzymes with enantiocomplementary aminomutase activity 747524
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10metabolism phenylalanine aminomutase (PAM) catalyzes the 2,3-shift of the alpha-amino group of L-phenylalanine and L-tyrosine to afford beta-phenylalanine. Biocatalytic strategies for the production of (R)- or (S)-beta-arylalanines employing enzymes with enantiocomplementary aminomutase activity. (R)-beta-phenylalanine is a precursor in biosynthesis of taxol in Taxus species 747524
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10metabolism phenylalanine aminomutase (PAM) catalyzes the 2,3-shift of the alpha-amino group of L-phenylalanine and L-tyrosine to afford beta-phenylalanine. Biocatalytic strategies for the production of (R)- or (S)-beta-arylalanines employing enzymes with enantiocomplementary aminomutase activity. Metabolites containing (R)-beta-phenylalanine are chemically similar astins from the plant Aster tataricus 747524
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10metabolism phenylalanine aminomutase (PAM) catalyzes the 2,3-shift of the alpha-amino group of L-phenylalanine and L-tyrosine to afford beta-phenylalanine. Biocatalytic strategies for the production of (R)- or (S)-beta-arylalanines employing enzymes with enantiocomplementary aminomutase activity. Metabolites containing (R)-beta-phenylalanine are chemically similar cyclochlorotines from the plant Talaromyces islandicum 747524
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10more the inner loop is a structural determinant of the lyase and mutase activities of PAM 746591
Show all pathways known for 5.4.3.10Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.10more the inner loop is a structural determinant of the lyase and mutase activities of PAM. Three-dimensional structure comparisons of Taxus chinensis PAM with PAM from Taxus canadensis and phenylalanine ammonia lyase from Petroselinum crispum (PcPAL). The latter contains an open inner loop conformation. The active-site inner loop, which contains the catalytic base Tyr, appears more rigid in PAM and more open or flexible in PAL. The rigidity of this loop in PAM is considered crucial for sequestering the trans-cinnamic acid and MIO-amine adduct in the active site to promote readdition of the amino-group to either the alpha- or beta-carbon positions of trans-cinnamic acid. Molecular dynamic simulations 746591
Results 1 - 10 of 11 > >>