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Literature summary for 5.4.3.11 extracted from

  • Zhu, L.; Tao, Y.; Ge, F.; Li, W.; Liu, Y.; Du, G.
    Production and characterization of phenylalanine aminomutase from Streptomyces maritimus and synthesis of beta-arylalanine (2017), Chem. J. Chin. Univ., 38, 206-211 .
No PubMed abstract available
Search for more literature for 5.4.3.11

Application

Application Comment Organism
synthesis the enzyme can be used for synthesis of beta-arylalanines with different groups at the benzene ring, 93% yield of 2-nitro-beta-phenylalanine. Potential prospectin application for the enzyme Streptomyces maritimus

Cloned(Commentary)

Cloned (Comment) Organism
gene pam, functional recombinant expression from plasmid pET28a in Escherichia coli strain BL21 Streptomyces maritimus

Protein Variants

Protein Variants Comment Organism
additional information evaluation of recombinant enzyme production in Escherichia coli strain BL21 and synthesis of beta-arylalanines. Maximal enzyme activity of 2.5 U/mg at pH 9.0, 30°C. Synthesis of beta-arylalanines with different groups at the benzene ring, 93% yield of 2-nitro-beta-phenylalanine Streptomyces maritimus

Organism

Organism UniProt Comment Textmining
Streptomyces maritimus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the recombinant enzyme displays a broad substrate spectrum Streptomyces maritimus ?
-
 ?

Synonyms

Synonyms Comment Organism
phenylalanine aminomutase
-
 Streptomyces maritimus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60 70 recombinant enzyme, 3 h, completely stable at Streptomyces maritimus

pH Stability

pH Stability pH Stability Maximum Comment Organism
9 11 recombinant enzyme, 24 h, about 98% activity remaining Streptomyces maritimus