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Literature summary extracted from

  • Yamada, M.; Kurahashi, K.
    Adenosine triphosphate and pyrophosphate dependent phenylalanine racemase of Bacillus brevis Nagano (1968), J. Biochem., 63, 59-69.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.1.1.11 2-mercaptoethanol stimulates 2-2.5fold at 0.05 M Brevibacillus brevis
5.1.1.11 diphosphate absolute requirement. Optimal concentration: 0.2-2 mM Brevibacillus brevis
5.1.1.11 dithiothreitol stimulates 2-2.5fold at 0.05 M. Inhibition at higher concentrations Brevibacillus brevis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.1.11 Mg2+ Mn2+ or Mg2+ required, up to 0.5 mM. Inhibitory at higher concentrations Brevibacillus brevis
5.1.1.11 Mn2+ Mn2+ or Mg2+ required, up to 0.5 mM Brevibacillus brevis

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.11 Brevibacillus brevis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.11
-
 Brevibacillus brevis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.11 ATP + L-Phe + H2O equilibrium ratio of L-Phe to D-Phe is 3:7 Brevibacillus brevis AMP + diphosphate + D-Phe
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.1.11 8.2 8.5
-
 Brevibacillus brevis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.1.1.11 7.2 8.6 7.2: about 25% of maximal activity, 8.6: about 85% of maximal activity Brevibacillus brevis