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Information on EC 5.4.3.10 - phenylalanine aminomutase (L-beta-phenylalanine-forming)
for references in articles please use BRENDA:EC5.4.3.10
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EC Tree 5 Isomerases
5.4 Intramolecular transferases
5.4.3 Transferring amino groups
5.4.3.10 phenylalanine aminomutase (L-beta-phenylalanine-forming)
IUBMB Comments
The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO). This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. cf. EC 5.4.3.11, phenylalanine aminomutase (D-β-phenylalanine-forming).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 5.4.3.10
- taxus
- ammonia
-
enantioselectivity
-
stereochemistry
-
regioselectivity
-
enantiopure
- pantoea
- chinensis
-
biocatalytic
-
isomerizes
- agglomerans
-
isomerization
-
prosthesis
-
trans-cinnamic
-
e-cinnamate
-
enantiomeric
-
biocatalyst
-
unnatural
- acrylate
- canadensis
-
rebind
-
pro-3s
-
beta-amino
- lyases
-
non-natural
-
lyase-like
-
n-benzoyl
-
intramolecularly
-
beta-isomer
showSynonyms
tcpam, phenylalanine aminomutase, phenylalanine-2,3-aminomutase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-PAM
(R)-selective PAM
admH
PAM
phenylalanine AM
phenylalanine aminomutase
phenylalanine-2,3-aminomutase
TcPAM
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-phenylalanine = L-beta-phenylalanine
-
-
-
-
L-phenylalanine = L-beta-phenylalanine
(R)-selective PAM reaction mechanism, overview
L-phenylalanine = L-beta-phenylalanine
(R)-selective PAM reaction mechanism, overview
A0A0U1LSP0
L-phenylalanine = L-beta-phenylalanine
(R)-selective PAM reaction mechanism, overview
-
L-phenylalanine = L-beta-phenylalanine
(R)-selective PAM reaction mechanism, overview
Pelliciarosea asterica
-
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SYSTEMATIC NAME
IUBMB Comments
L-phenylalanine 2,3-aminomutase [(R)-3-amino-3-phenylpropanoate forming]
The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO). This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. cf. EC 5.4.3.11, phenylalanine aminomutase (D-beta-phenylalanine-forming).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S)-2-amino-3-(4-methoxyphenyl)propanoic acid
?
-
Substrates: 45% conversion rate
Products: -
Products: -
?
(2S)-2-amino-3-(4-methylphenyl)propanoic acid
?
-
Substrates: 45% conversion rate
Products: -
Products: -
?
(2S)-alpha-phenylalanine
(3S)-beta-phenylalanine
-
Substrates: -
Products: -
Products: -
?
(2S)-[3-2H2]-alpha-phenylalanine
(2R,3S)-[2,3-2H2]-beta-phenylalanine
-
Substrates: -
Products: -
Products: -
?
(2S,3S)-[2,3-2H2]-alpha-phenylalanine
(3S)-[2-2H2]-beta-phenylalanine
-
Substrates: -
Products: -
Products: -
?
3'-methyl-alpha-phenylalanine
3'-methyl-beta-phenylalanine
Substrates: -
Products: plus 3'-methylcinnamate, product of ammonia lyase reaction. Distribution of 3'-methyl-beta-phenylalanine and 3'-methylcinnamate is at about 1:1
Products: plus 3'-methylcinnamate, product of ammonia lyase reaction. Distribution of 3'-methyl-beta-phenylalanine and 3'-methylcinnamate is at about 1:1
?
4'-methyl-alpha-phenylalanine
4'-methyl-beta-phenylalanine
Substrates: -
Products: plus 4'-methylcinnamate, product of ammonia lyase reaction
Products: plus 4'-methylcinnamate, product of ammonia lyase reaction
?
L-beta-phenylalanine
D-alpha-phenylalanine
Substrates: -
Products: -
Products: -
r
styryl-alpha-alanine
5-phenyl-(2E,4E)-pentadienoate
Substrates: -
Products: -
Products: -
?
trans-cinnamic acid + NH3
L-phenylalanine
-
Substrates: cf. EC 4.3.1.24
Products: -
Products: -
r
D-alpha-phenylalanine
L-beta-phenylalanine
Substrates: -
Products: -
Products: -
r
D-alpha-phenylalanine
L-beta-phenylalanine
Substrates: -
Products: -
Products: -
r
D-alpha-phenylalanine
L-beta-phenylalanine
Substrates: (S)-alpha-phenylalanine, reaction mechanism
Products: -
Products: -
r
L-phenylalanine
L-beta-phenylalanine
-
Substrates: L-alpha-phenylalanine
Products: -
Products: -
r
L-phenylalanine
L-beta-phenylalanine
Pelliciarosea asterica
-
Substrates: L-alpha-phenylalanine
Products: -
Products: -
r
L-phenylalanine
L-beta-phenylalanine
A0A0U1LSP0
Substrates: -
Products: -
Products: -
r
L-phenylalanine
L-beta-phenylalanine
A0A0U1LSP0
Substrates: L-alpha-phenylalanine
Products: -
Products: -
r
L-phenylalanine
L-beta-phenylalanine
Substrates: L-alpha-phenylalanine
Products: -
Products: -
r
L-phenylalanine
L-beta-phenylalanine
Substrates: L-alpha-phenylalanine
Products: -
Products: -
r
additional information
?
-
Substrates: (E)-cinnamate is both a substrate and an intermediate of the reaction. To account for the distinct (3alpha)-beta-amino acid stereochemistry catalyzed by the enzyme, the cinnamate skeleton must rotate the C1-Calpha and Cipso-Cbeta bonds 180° in the active site prior to exchange and rebinding of theNH2/H pair to the cinnamate
Products: -
Products: -
?
additional information
?
-
-
Substrates: (E)-cinnamate is both a substrate and an intermediate of the reaction. To account for the distinct (3alpha)-beta-amino acid stereochemistry catalyzed by the enzyme, the cinnamate skeleton must rotate the C1-Calpha and Cipso-Cbeta bonds 180° in the active site prior to exchange and rebinding of theNH2/H pair to the cinnamate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes a 2,3-amine shift that reversibly interconverts alpha-Phe to beta-Phe
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes a 2,3-amine shift that reversibly interconverts alpha-Phe to beta-Phe
Products: -
Products: -
?
additional information
?
-
Substrates: TcPAM catalyzes the isomerization of alpha-phenylalanine to beta-phenylalanine through exchanging the position of the amine group (Calpha -> Cbeta) and pro-3S hydrogen proton (Cbeta -> Calpha) with retention of the configuration at the reaction termini, which requires reorientation after deamination of beta-phenylalanine to trans-cinnamic acid in which the reface of the Cbeta and the si-face of the Cbeta carton atoms are positioned for amine readdition and reprotonation. The enzyme TcPAM also catalyzes the regioselective hydroamination of trans-cinnamic acid (t-CA) to yield L-beta-Phe, TcPAL, EC 4.3.1.24. The final product mixture consists of both alpha- and beta-Phe owing to low regioselectivity of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: TcPAM catalyzes the isomerization of alpha-phenylalanine to beta-phenylalanine through exchanging the position of the amine group (Calpha -> Cbeta) and pro-3S hydrogen proton (Cbeta -> Calpha) with retention of the configuration at the reaction termini, which requires reorientation after deamination of beta-phenylalanine to trans-cinnamic acid in which the reface of the Cbeta and the si-face of the Cbeta carton atoms are positioned for amine readdition and reprotonation. The enzyme TcPAM also catalyzes the regioselective hydroamination of trans-cinnamic acid (t-CA) to yield L-beta-Phe, TcPAL, EC 4.3.1.24. The final product mixture consists of both alpha- and beta-Phe owing to low regioselectivity of the enzyme
Products: -
Products: -
?
additional information
?
-
Substrates: phenylalanine-2,3-aminomutase (PAM) from Taxus chinensis, a 4-methylidene-imidazole-5-one (MIO)-dependent enzyme, catalyzes the reversible conversion of (S)-alpha-phenylalanine into (R)-beta-phenylalanine via trans-cinnamic acid. The enzyme also catalyzes the direct addition of ammonia to trans-cinnamic acid, a reaction that can be used for the preparation of beta-amino acids, cf. EC 4.3.1.24, phenylalanine ammonia-lyase
Products: -
Products: -
?
additional information
?
-
-
Substrates: phenylalanine-2,3-aminomutase (PAM) from Taxus chinensis, a 4-methylidene-imidazole-5-one (MIO)-dependent enzyme, catalyzes the reversible conversion of (S)-alpha-phenylalanine into (R)-beta-phenylalanine via trans-cinnamic acid. The enzyme also catalyzes the direct addition of ammonia to trans-cinnamic acid, a reaction that can be used for the preparation of beta-amino acids, cf. EC 4.3.1.24, phenylalanine ammonia-lyase
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-alpha-phenylalanine
L-beta-phenylalanine
Substrates: -
Products: -
Products: -
r
D-alpha-phenylalanine
L-beta-phenylalanine
Substrates: -
Products: -
Products: -
r
L-phenylalanine
L-beta-phenylalanine
A0A0U1LSP0
Substrates: -
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,5-dihydro-5-methylidene-4H-imidazol-4-one
i.e. MIO, essential cofactor
3,5-dihydro-5-methylidene-4H-imidazol-4-one
A0A0U1LSP0
i.e. MIO, essential cofactor
3,5-dihydro-5-methylidene-4H-imidazol-4-one
Pelliciarosea asterica
-
i.e. MIO, essential cofactor
3,5-dihydro-5-methylidene-4H-imidazol-4-one
i.e. MIO, essential cofactor
3,5-dihydro-5-methylidene-4H-imidazol-4-one
i.e. MIO, essential cofactor
3,5-dihydro-5-methylidene-4H-imidazol-4-one
i.e. MIO, essential cofactor
3,5-dihydro-5-methylidene-4H-imidazol-4-one
i.e. MIO, essential cofactor, residues Y322 and N231 are essential for MIO group formation
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
has little effect on the enzyme activity, resulting in retention of about 90% of the initial activity
cetrimonium bromide
-
has little effect on the enzyme activity, resulting in retention of about 90% of the initial activity
-
Fe2+
-
has little effect on the enzyme activity, resulting in retention of about 90% of the initial activity
K+
-
has little effect on the enzyme activity, resulting in retention of about 90% of the initial activity
SDS
-
has little effect on the enzyme activity, resulting in retention of about 90% of the initial activity
Triton X-100
-
has little effect on the enzyme activity, resulting in retention of about 90% of the initial activity
Tween 80
-
has little effect on the enzyme activity, resulting in retention of about 90% of the initial activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008
D-alpha-phenylalanine
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.058
D-alpha-phenylalanine
pH and temperature not specified in the publication, recombinant mutant L97G/C89T
0.067
D-alpha-phenylalanine
pH and temperature not specified in the publication, recombinant mutant L97G
0.028
L-beta-phenylalanine
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.29
L-beta-phenylalanine
pH and temperature not specified in the publication, recombinant mutant L97G/C89T
0.31
L-beta-phenylalanine
pH and temperature not specified in the publication, recombinant mutant L97G
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0032
D-alpha-phenylalanine
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.0088
D-alpha-phenylalanine
pH and temperature not specified in the publication, recombinant mutant L97G/C89T
0.0184
D-alpha-phenylalanine
pH and temperature not specified in the publication, recombinant mutant L97G
0.0092
L-beta-phenylalanine
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.062
L-beta-phenylalanine
pH and temperature not specified in the publication, recombinant mutant L97G/C89T
0.117
L-beta-phenylalanine
pH and temperature not specified in the publication, recombinant mutant L97G
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
D-alpha-phenylalanine
pH and temperature not specified in the publication, recombinant mutant L97G/C89T
0.28
D-alpha-phenylalanine
pH and temperature not specified in the publication, recombinant mutant L97G
0.4
D-alpha-phenylalanine
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.21
L-beta-phenylalanine
pH and temperature not specified in the publication, recombinant mutant L97G/C89T
0.32
L-beta-phenylalanine
pH and temperature not specified in the publication, recombinant wild-type enzyme
0.38
L-beta-phenylalanine
pH and temperature not specified in the publication, recombinant mutant L97G
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
the enzyme shows more than 50% activity between 20 and 60°C with 80% of the maximum activity at 37°C. Enzymatic activity significantly decreases at temperatures higher than 50°C, and the enzyme is inactive at 80°C
30 - 70
no activity at 15°C, increasing activity with increasing temperature, highest at 70°C, profile overview
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
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
A0A0U1LSP0
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
-
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
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
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)
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
A0A0U1LSP0
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
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 astins from the plant Aster tataricus
metabolism
Pelliciarosea asterica
-
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
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 inner loop is a structural determinant of the lyase and mutase activities of PAM
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
-
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
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PAM_TAXCA
698
0
76532
Swiss-Prot
Secretory Pathway (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
secondary structural analysis of the simulated PAM systems at the resting state, wild-type and mutant enzymes, overview
additional information
analysis of enzyme PAM three-dimensional structures with a bound (R)-beta-phenylalanine analogue and with bound trans-cinnamic acid, and of cofactor MIO-less enzyme mutant structures, overview
additional information
-
analysis of enzyme PAM three-dimensional structures with a bound (R)-beta-phenylalanine analogue and with bound trans-cinnamic acid, and of cofactor MIO-less enzyme mutant structures, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.38 A resolution, space group C2. A (E)-cinnamate molecule is bound in the active site, lying above the 4-methylidene-1H-imidazol-5(4H)-one cofactor and under a loop region that includes residues 80-97, which define the top of the active site. The (E)-cinnamate molecule lies about 3.4 A above the methylidene carbon of the 4-methylidene-1H-imidazol-5(4H)-one moiety. The carboxylate of the cinnamate makes a salt bridge interaction with a strongly conserved residue R325, which serves to position the product in the active site. The plane of the aromatic ring of the cinnamate is displaced about 20° from the perpendicular relative to the pi-bond plane of the propenoate carboncarbon double bond. The aromatic ring is bound relatively loosely in the active site, making only one direct hydrophobic interaction with residue L104
purified recombinant wild-type PAM in complex with (R)-beta-phenylalanine or with L-beta-Phe analogue (S)-3-amino-2,2-difluoro-phenylpropanoic acid, enzyme mutant Y80A complexed with (S)-3-amino-2,2-difluoro-phenylpropanoic acid, and MIO-less enzyme mutants N231A and Y322A, crystallization from 0.2-0.5 mM TCEP, pH 7.0, with or without 2.0-20 mM ligand, X-ray diffraction structure determination and analysis at 1.85-2.20 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F455N
-
the enzyme shows reduced phenylalanine aminomutase activity and increased phenylalanine ammonia-lyase activity compared to the wild type enzyme
G191A
the mutant shows strongly reduced specific activity compared to the wild type enzyme
G204A
the mutant shows reduced specific activity compared to the wild type enzyme
G307A
the mutant shows reduced specific activity compared to the wild type enzyme
G307A/K340R/K537R
the mutant shows strongly decreased specific activity compared to the wild type enzyme
G32A
the mutant shows slightly reduced specific activity compared to the wild type enzyme
G32A/K114R/K340R
the mutant shows slightly increased specific activity compared to the wild type enzyme
G32A/K114R/K402R
the mutant shows decreased specific activity compared to the wild type enzyme
G32A/K114R/K537R
the mutant shows slightly increased specific activity compared to the wild type enzyme
G32A/K340R/K537R
the mutant shows increased specific activity compared to the wild type enzyme
G407A
the mutant shows slightly reduced specific activity compared to the wild type enzyme
K114R
the mutant shows 1.45fold increased catalytic efficiency and 2.96fold improved half-life at 50°C over those of the wild type enzyme
K114R/G32A
the mutant shows decreased specific activity compared to the wild type enzyme
K114R/G370A
the mutant shows strongly decreased specific activity compared to the wild type enzyme
K114R/K340R/K402R
the mutant shows slightly decreased specific activity compared to the wild type enzyme
K114R/K340R/K537R
the mutant shows decreased specific activity compared to the wild type enzyme
K299R
the mutant shows reduced specific activity compared to the wild type enzyme
K33R
the mutant shows strongly reduced specific activity compared to the wild type enzyme
K340R
the mutant shows 3fold increased catalytic efficiency and 2.12fold improved half-life at 50°C over those of the wild type enzyme. The conversion rate of L-phenylalanine to L-beta-phenylalanine is improved by 17% compared to that of the wild type enzyme
K340R/G32A
the mutant shows decreased specific activity compared to the wild type enzyme
K340R/G370A
the mutant shows strongly decreased specific activity compared to the wild type enzyme
K340R/K114R
the mutant shows strongly decreased specific activity compared to the wild type enzyme
K402R
the mutant shows increased specific activity compared to the wild type enzyme
K501R
the mutant shows slightly reduced specific activity compared to the wild type enzyme
K521R
the mutant shows slightly reduced specific activity compared to the wild type enzyme
K537R
the mutant shows strongly increased specific activity compared to the wild type enzyme
K537R/G307A
the mutant shows decreased specific activity compared to the wild type enzyme
K537R/G32A
the mutant shows strongly decreased specific activity compared to the wild type enzyme
K537R/G407A
the mutant shows strongly decreased specific activity compared to the wild type enzyme
K537R/K114R
the mutant shows decreased specific activity compared to the wild type enzyme
K537R/K340R
the mutant shows decreased specific activity compared to the wild type enzyme
S195A
the mutant shows reduced specific activity compared to the wild type enzyme
S206A
the mutant shows slightly reduced specific activity compared to the wild type enzyme
S211A
the mutant shows reduced specific activity compared to the wild type enzyme
S289A
the mutant shows slightly reduced specific activity compared to the wild type enzyme
S30A
the mutant shows reduced specific activity compared to the wild type enzyme
S36A
the mutant shows reduced specific activity compared to the wild type enzyme
S403A
the mutant shows slightly reduced specific activity compared to the wild type enzyme
S539A
the mutant shows slightly reduced specific activity compared to the wild type enzyme
S65A
the mutant shows reduced specific activity compared to the wild type enzyme
S69A
the mutant shows reduced specific activity compared to the wild type enzyme
S72A
the mutant shows reduced specific activity compared to the wild type enzyme
S98A
the mutant shows reduced specific activity compared to the wild type enzyme
L104A
1.5-fold increase in kcat and a decrease in KM values for 3'-methyl-alpha-phenylalanine and styryl-alpha-alanine substrates
A77T/I79S/C89T/L97G
site-directed mutagenesis, the mutant shows an altered structure compared to wild-type enzyme with reduced beta-ladder and 3_10-helix contents
I431V
the mutant shows reduced catalytic efficiencies with L-phenylalanine/L-beta-phenylalanine and increased catalytic efficiencies with L-tyrosine/L-beta-tyrosine compared to the wild type enzyme
L104S
the mutant shows reduced catalytic efficiencies with L-phenylalanine/L-beta-phenylalanine compared to the wild type enzyme and is inactive with L-tyrosine
L108E
site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme
L108E/N458F
site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme
L108S
the mutant shows reduced catalytic efficiencies with L-phenylalanine/L-beta-phenylalanine and L-beta-tyrosine compared to the wild type enzyme and is inactive with L-tyrosine
L179S
the mutant shows no activity with L-phenylalanine and no activity with L-beta-phenylalanine as well as 8% activity with L-tyrosine and no activity with L-beta-tyrosine compared to the wild type enzyme
L179T
the mutant shows no activity with L-phenylalanine and 14% activity with L-beta-phenylalanine as well as no activity with L-tyrosine and 4% activity with L-beta-tyrosine compared to the wild type enzyme
L97G
site-directed mutagenesis, the mutant shows an altered structure compared to wild-type enzyme, the mutant has a significant increase in 310-helix and beta-ladder, compared to wild-type, with the highest coil percent among the PAM variants and improved activity. The mutant shows reduced temperature stability and optimum for PAM activity, in contrast to PAL activity
L97G/A77T/C89T
site-directed mutagenesis, the mutant shows an altered structure compared to wild-type enzyme with reduced beta-ladder and 3_10-helix contents
L97G/C89T
site-directed mutagenesis, the mutant shows an altered structure compared to wild-type enzyme, the mutant has a significant increase in 310-helix and beta-ladder compared to wild-type. The mutant shows reduced temperature stability and optimum for PAM activity, in contrast to PAL activity
N231A
site-directed mutagenesis, a cofactor MIO-less, catalytically inactive mutant
N458A
the mutant shows 6% activity with L-phenylalanine and L-beta-phenylalanine as well as no activity with L-tyrosine and L-beta-tyrosine compared to the wild type enzyme
N458C
the mutant shows 20% activity with L-phenylalanine and 27% activity with L-beta-phenylalanine as well as no activity with L-tyrosine and 0.4% activity with L-beta-tyrosine compared to the wild type enzyme
N458F
site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme
N458L
site-directed mutagenesis, the mutant shows reduced activity with trans-cinnamate compared to wild-type enzyme
Q459C
the mutant shows 10% activity with L-phenylalanine and no activity with L-beta-phenylalanine as well as 38% activity with L-tyrosine and no activity with L-beta-tyrosine compared to the wild type enzyme
Q459H
the mutant shows no activity with L-phenylalanine, L-beta-phenylalanine, L-tyrosine and L-beta-tyrosine
Q459L
the mutant shows no activity with L-phenylalanine and 9% activity with L-beta-phenylalanine as well as no activity with L-tyrosine and L-beta-tyrosine compared to the wild type enzyme
Y322A
site-directed mutagenesis, a cofactor MIO-less, catalytically inactive mutant
additional information
mutation of the inner loop region, that closes the active site of PAM, within PAM (PAM residues 77-97) in a stepwise approach. Almost all of the single loop mutations trigger a lyase phenotype in PAM. Experimental and computational evidence suggest that the induced lyase features result from inner loop mobility enhancements, which are possibly caused by a 310-helix cluster, flanking alpha-helices, and hydrophobic interactions. The application of wild-type PAM for the synthesis of beta-amino acids is hindered by low reaction rates and the mixture of alpha-Phe and beta-Phe generated from the asymmetric synthetic route. Molecular dynamic simulations
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 9
after incubating at pH 8.0-9.0 for 2 h, more than 60% of activity remains
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
after incubation at 50°C for 30 min, less than 50% of the enzymatic activity remains
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ratnayake, N.D.; Wanninayake, U.; Geiger, J.H.; Walker, K.D.
Stereochemistry and mechanism of a microbial phenylalanine aminomutase
J. Am. Chem. Soc.
133
8531-8533
2011
Pantoea agglomerans
brenda
Feng, L.; Wanninayake, U.; Strom, S.; Geiger, J.; Walker, K.
Mechanistic, mutational, and structural evaluation of a taxus phenylalanine aminomutase
Biochemistry
50
2919-2930
2011
Taxus canadensis (Q6GZ04), Taxus canadensis
brenda
Heberling, M.; Masman, M.; Bartsch, S.; Wybenga, G.; Dijkstra, B.; Marrink, S.; Janssen, D.
Ironing out their differences Dissecting the structural determinants of a phenylalanine aminomutase and ammonia lyase
ACS Chem. Biol.
10
989-997
2015
Taxus chinensis (Q68G84), Taxus canadensis (Q6GZ04)
-
brenda
Parmeggiani, F
; Weise, N.J.; Ahmed, S.T.; Turner, N.J. Synthetic and therapeutic applications of ammonia-lyases and aminomutases
Chem. Rev.
118
73-118
2018
Taxus chinensis (Q68G84), Talaromyces islandicus (A0A0U1LSP0), Aster tataricus, Pelliciarosea asterica
brenda
Zhu, L.; Ge, F.; Li, W.; Song, P.; Tang, H.; Tao, Y.; Liu, Y.; Du, G.
One step synthesis of unnatural beta-arylalanines using mutant phenylalanine aminomutase from Taxus chinensis with high beta-regioselectivity
Enzyme Microb. Technol.
114
22-28
2018
Taxus chinensis (Q68G83), Taxus chinensis
brenda
Zhou, L.; Wang, Y.; Liu, H.; Han, L.; Zhang, W.; Cui, W.; Liu, Z.; Zhou, Z.
Surface engineering of a Pantoea agglomerans-derived phenylalanine aminomutase for the improvement of (S)-beta-phenylalanine biosynthesis
Biochem. Biophys. Res. Commun.
518
204-211
2019
Pantoea agglomerans (Q84FL5)
brenda
Peng, F.; Aliyu, H.; Delavault, A.; Engel, U.; Rudat, J.
Synthesis of (S)-and (R)-beta-tyrosine by redesigned phenylalanine aminomutase
Catalysts
12
397
2022
Taxus chinensis (Q68G84)
-
brenda
Zhu, L.; Yang, J.; Feng, G.; Ge, F.; Li, W.; Song, P.; Tao, Y.; Zhou, Z.
Investigation into isomerization reaction of phenylalanine aminomutase from Pantoea agglomerans
Enzyme Microb. Technol.
132
109428
2020
Pantoea agglomerans
brenda
Feng, G.; Xu, W.; Song, P.; Li, W.; Tao, Y.; Ge, F.; Zhu, L.
Characterization of recombinant phenylalanine aminomutase from Taxus chinensis and its application for synthesis of R-beta-arylalanine
Sh. Kexue/Food Sci.
42
82-87
2021
Taxus chinensis
-
brenda
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