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Literature summary extracted from

  • Varga, A.; Filip, A.; Bencze, L.; Satorhelyi, P.; Bell, E.; Vertessy, B.; Poppe, L.; Paizs, C.
    Expression and purification of recombinant phenylalanine 2,3-aminomutase from Pantoea agglomerans (2016), Stud. Univ. Babes-Bolyai Chem., 61, 7-19 .
No PubMed abstract available

Application

EC Number Application Comment Organism
5.4.3.11 drug development phenylalanine ammonia-lyases and 2,3-aminomutases are emerging as important enzymatic systems as potential target for treating diseases such as phenylketonuria and cancer Pantoea agglomerans
5.4.3.11 synthesis the enzyme is an attractive alternative enzymatic route to obtain enantiomerically pure alpha- and beta-amino acids, via green synthetic routes to chiral amines Pantoea agglomerans

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.3.11 a 1639 bps long synthetic gene, recombinant overexpression of N-terminally His10-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS, real-time PCR enzyme expression analysis, method evaluation, optimization, and upscaling to high level protein expression. 37°C is the best temperature for maximum protein production. Subcloning in Escherichia coli strain XL-1 Blue Pantoea agglomerans

General Stability

EC Number General Stability Organism
5.4.3.11 no stability increase of the enzyme upon substrate binding Pantoea agglomerans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.3.11 D-alpha-phenylalanine Pantoea agglomerans (S)-alpha-phenylalanine D-beta-phenylalanine
-
 ?
5.4.3.11 additional information Pantoea agglomerans in nature, phenylalanine 2,3-aminonutase from Pantoea agglomerans is an (S)-selective enzyme, transforming the (S)-alpha-phenylalanine in (S)-beta-phenylalanine ?
-
 ?

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.3.11 D-alpha-phenylalanine (S)-alpha-phenylalanine Pantoea agglomerans D-beta-phenylalanine
-
 ?
5.4.3.11 additional information in nature, phenylalanine 2,3-aminonutase from Pantoea agglomerans is an (S)-selective enzyme, transforming the (S)-alpha-phenylalanine in (S)-beta-phenylalanine Pantoea agglomerans ?
-
 ?
5.4.3.11 additional information PaPAM converts (S)-alpha-amino acids to (S)-beta-amino acids Pantoea agglomerans ?
-
 ?
5.4.3.11 rac-alpha-phenylalanine
-
 Pantoea agglomerans D-beta-phenylalanine
-
 ?

Subunits

EC Number Subunits Comment Organism
5.4.3.11 ? x * 72000, recombinant His-tagged enzyme, SDS-PAGE Pantoea agglomerans

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 25
-
 assay at Pantoea agglomerans

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.4.3.11 73 74 melting temperature of purifed recombinant enzyme in presence or absence of the enzyme Pantoea agglomerans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4.3.11 8
-
-
 Pantoea agglomerans

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.3.11 4-methylidene-1H-imidazol-5(4H)-one MIO, a protein-derived cofactor, which is generated autocatalytically from three active site residues, Ala-Ser-Gly (Thr-Ser-Gly in PaPAM), forming a MIO signature motif Pantoea agglomerans

General Information

EC Number General Information Comment Organism
5.4.3.11 evolution phenylalanine 2,3-mutases, PAMs, belong to the class I lyase-like family that includes tyrosine 2,3-aminomutases (TAMs), tyrosine ammonia-lyases (TALs), and histidine ammonia-lyases (HALs). All these enzymes rely on a protein-derived cofactor, 4-methylideneimidazol-5-one (MIO), which is generated autocatalytically from three active site residues, Ala-Ser-Gly (Thr-Ser-Gly in PaPAM), forming a MIO signature motif Pantoea agglomerans