Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Varga, A.; Banoczi, G.; Nagy, B.; Bencze, L.; Tosa, M.; Gellert, A.; Irimie, F.; Retey, J.; Poppe, L.; Paizs, C.
    Influence of the aromatic moiety in alpha- and beta-arylalanines on their biotransformation with phenylalanine 2,3-aminomutase from Pantoea agglomerans (2016), RSC Adv., 6, 56412-56420 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.3.11 recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS Pantoea agglomerans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.4.3.11 NH4+ changing the (NH4)2CO3 concentration in the range of 50-1000 mM at pH 8.0 significantly influences the product compositions Pantoea agglomerans

Organism

EC Number Organism UniProt Comment Textmining
5.4.3.11 Pantoea agglomerans Q84FL5 i.e. Enterobacter agglomerans or Erwinia herbicola
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.3.11 recombinant N-terminally His10-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, dialysis, and ultrafiltration Pantoea agglomerans

Reaction

EC Number Reaction Comment Organism Reaction ID
5.4.3.11 L-phenylalanine = D-beta-phenylalanine the proposed mechanism of action of PaPAM: starting from either direction with the cooperation of two catalytically essential tyrosine residues (Tyr1 and Tyr2) and the MIO prosthetic group, N-MIO intermediates of alpha- or beta-phenylalanine are formed which interconvert by a alpha - beta migration of the amino group involving a postulated (E)-cinnamate intermediate. PaPAM-catalysed kinetic resolutions starting from racemic alpha-arylalanines or racemic beta-arylalanines result in the opposite enantiomers as products vs. unreacted enantiomers. Mechanism, overview. Formation of significant amounts of (E)-arylacrylates is observed with many substrates indicating substantial lyase-activity of enzyme PaPAM Pantoea agglomerans
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.3.11 D-phenylalanine
-
 Pantoea agglomerans D-beta-phenylalanine
-
 ?
5.4.3.11 additional information the enzyme performs enantiomer-selective isomerization of various racemic alpha- and beta-arylalanines, both alpha- and beta-arylalanines are accepted as substrates when the aryl moiety is relatively small, like phenyl, 2-, 3-, 4-fluorophenyl or thiophen-2-yl. While 2-substituted alpha-phenylalanines bearing bulky electron withdrawing substituents do not react, the corresponding substituted beta-aryl analogues are converted rapidly. Conversion of 3- and 4-substituted alpha-arylalanines happens smoothly, while conversion of the corresponding beta-arylalanines is poor or non-existent. The high enantiomeric excess (ee) values of the products indicate excellent enantiomer selectivity and stereospecificity of the isomerization except for (S)-2-nitro-a-phenylalanine (ee 92%) from the beta-isomer. Computational modelling reveals that one of the main factors controlling biocatalytic activity is the energy difference between the covalent regioisomeric enzyme-substrate complexes. Formation of significant amounts of (E)-arylacrylates is observed with many substrates indicating substantial lyase-activity of enzyme PaPAM. Differences of conversions of the PaPAM-catalysed isomerizations from alpha- and beta-arylalanines racemates, substrate categories and relative energy differences of the regioisomeric N-MIO intermediates, substrate specificity and reaction products, overview Pantoea agglomerans ?
-
 ?
5.4.3.11 rac-2-chloro-phenylalanine
-
 Pantoea agglomerans 2-chloro-D-beta-phenylalanine + 2-chloro-L-beta-phenylalanine
-
 ?
5.4.3.11 rac-2-fluoro-phenylalanine
-
 Pantoea agglomerans 2-fluoro-D-beta-phenylalanine + 2-fluoro-L-beta-phenylalanine
-
 ?
5.4.3.11 rac-2-nitro-phenylalanine
-
 Pantoea agglomerans 2-nitro-D-beta-phenylalanine + 2-nitro-L-beta-phenylalanine
-
 ?
5.4.3.11 rac-3-chloro-phenylalanine
-
 Pantoea agglomerans 3-chloro-D-beta-phenylalanine + 3-chloro-L-beta-phenylalanine
-
 ?
5.4.3.11 rac-3-fluoro-phenylalanine
-
 Pantoea agglomerans 3-fluoro-D-beta-phenylalanine + 3-fluoro-L-beta-phenylalanine
-
 ?
5.4.3.11 rac-3-nitro-phenylalanine
-
 Pantoea agglomerans 3-nitro-D-beta-phenylalanine + 3-nitro-L-beta-phenylalanine
-
 ?
5.4.3.11 rac-4-bromo-phenylalanine
-
 Pantoea agglomerans 4-bromo-D-beta-phenylalanine + 4-bromo-L-beta-phenylalanine
-
 ?
5.4.3.11 rac-4-chloro-phenylalanine
-
 Pantoea agglomerans 4-chloro-D-beta-phenylalanine + 4-chloro-L-beta-phenylalanine
-
 ?
5.4.3.11 rac-4-fluoro-phenylalanine
-
 Pantoea agglomerans 4-fluoro-D-beta-phenylalanine + 4-fluoro-L-beta-phenylalanine
-
 ?
5.4.3.11 rac-4-nitro-phenylalanine
-
 Pantoea agglomerans 4-nitro-D-beta-phenylalanine + 4-nitro-L-beta-phenylalanine
-
 ?
5.4.3.11 rac-thiophen-2-ylalanine
-
 Pantoea agglomerans D-beta-thiophen-2-ylalanine + L-beta-thiophen-2-ylalanine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.4.3.11 admH
-
 Pantoea agglomerans
5.4.3.11 PaPAM
-
 Pantoea agglomerans
5.4.3.11 phenylalanine 2,3-aminomutase
-
 Pantoea agglomerans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.4.3.11 22
-
 assay at room temperature Pantoea agglomerans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4.3.11 7 9 alteration of pH of the buffer solution in the range of pH 7-9 (at 100 mM (NH4)2CO3) is indifferent to enzymatic conversion Pantoea agglomerans

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.3.11 4-methylidene-1H-imidazol-5(4H)-one MIO, prosthetic group, dependent on Pantoea agglomerans

General Information

EC Number General Information Comment Organism
5.4.3.11 additional information molecular modelling of the covalent enzyme-substrate N-MIO complexes in PaPAM Pantoea agglomerans