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Literature summary 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

Application

EC Number Application Comment Organism
5.4.3.11 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
5.4.3.11 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

EC Number Organism UniProt Comment Textmining
5.4.3.11 Streptomyces maritimus
-
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
5.4.3.11 phenylalanine aminomutase
-
Streptomyces maritimus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.4.3.11 60 70 recombinant enzyme, 3 h, completely stable at Streptomyces maritimus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
5.4.3.11 9 11 recombinant enzyme, 24 h, about 98% activity remaining Streptomyces maritimus