5.4.3.10: phenylalanine aminomutase (L-beta-phenylalanine forming)
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For detailed information about phenylalanine aminomutase (L-beta-phenylalanine forming), go to the full flat file.
Word Map on EC 5.4.3.10
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5.4.3.10
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taxus
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ammonia
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enantioselectivity
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stereochemistry
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regioselectivity
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enantiopure
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pantoea
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chinensis
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biocatalytic
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isomerizes
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agglomerans
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isomerization
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prosthesis
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trans-cinnamic
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e-cinnamate
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enantiomeric
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biocatalyst
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unnatural
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acrylate
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canadensis
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rebind
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pro-3s
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beta-amino
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lyases
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non-natural
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lyase-like
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n-benzoyl
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intramolecularly
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beta-isomer
- 5.4.3.10
- taxus
- ammonia
-
enantioselectivity
-
stereochemistry
-
regioselectivity
-
enantiopure
- pantoea
- chinensis
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biocatalytic
-
isomerizes
- agglomerans
-
isomerization
-
prosthesis
-
trans-cinnamic
-
e-cinnamate
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enantiomeric
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biocatalyst
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unnatural
- acrylate
- canadensis
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rebind
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pro-3s
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beta-amino
- lyases
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non-natural
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lyase-like
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n-benzoyl
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intramolecularly
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beta-isomer
Reaction
Synonyms
(R)-PAM, (R)-selective PAM, admH, CctP, More, PAM, phenylalanine AM, phenylalanine aminomutase, phenylalanine-2,3-aminomutase, TcPAM
ECTree
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General Information
General Information on EC 5.4.3.10 - phenylalanine aminomutase (L-beta-phenylalanine forming)
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evolution
metabolism
additional information
evolution
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)
evolution
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)
evolution
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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
evolution
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
evolution
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
evolution
Pelliciarosea asterica
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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
Pelliciarosea asterica
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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
metabolism
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
metabolism
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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
metabolism
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
the inner loop is a structural determinant of the lyase and mutase activities of PAM
additional information
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
additional information
the stereochemistry of the PAM-catalyzed reaction originates from the enzyme's ability to bind trans-cinnamic acid in two different orientations, with either the si,si face or the re,re face directed toward the MIO group, as evidenced by two distinct carboxylate binding modes. The N231 side chain promotes prosthetic MIO group formation by increasing the nucleophilicity of the G177 N atom through acidification of the amide proton. PAM enzyme structures comparisons, overview
additional information
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the stereochemistry of the PAM-catalyzed reaction originates from the enzyme's ability to bind trans-cinnamic acid in two different orientations, with either the si,si face or the re,re face directed toward the MIO group, as evidenced by two distinct carboxylate binding modes. The N231 side chain promotes prosthetic MIO group formation by increasing the nucleophilicity of the G177 N atom through acidification of the amide proton. PAM enzyme structures comparisons, overview