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Literature summary for 5.1.1.11 extracted from

  • Yamada, M.; Kurahashi, K.
    Further purification and properties of adenosine triphosphate-dependent phenylalanine racemase of Bacillus brevis NAGANO (1969), J. Biochem., 66, 529-540.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol the velocity of the D-Phe formation from the L-isomer is markedly affected by the concentration of DTT, whereas that of L-Phe formation from the D-isomer is less affected Brevibacillus brevis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
L-Phe
-
Brevibacillus brevis
0.15
-
ATP
-
Brevibacillus brevis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
95000
-
x * 95000, SDS-PAGE Brevibacillus brevis
100000
-
sucrose density gradient centrifugation Brevibacillus brevis

Organism

Organism UniProt Comment Textmining
Brevibacillus brevis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Brevibacillus brevis

Reaction

Reaction Comment Organism Reaction ID
ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine the amino group of Phe is essential for its binding to the aminoacyl adenylate reaction center. The carbonyl group is not at all or only weakly bound. The benzene ring of Phe which determines substrate recognition also seems to be of minor importance for substrate binding Brevibacillus brevis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Brevibacillus brevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Phe + H2O
-
Brevibacillus brevis AMP + diphosphate + D-Phe
-
?
additional information the enzyme catalyzes Phe racemization and activation. Catalyzes ATP-AMP exchange reaction, L-Phe dependent ATP-AMP exchange reaction Brevibacillus brevis ?
-
?

Subunits

Subunits Comment Organism
? x * 95000, SDS-PAGE Brevibacillus brevis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Brevibacillus brevis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
formation of L-isomer from D-Phe Brevibacillus brevis
8.2 8.5 formation of D-isomer from L-Phe Brevibacillus brevis

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
the velocity of the D-Phe formation from the L-isomer is markedly affected by the concentration of DTT, whereas that of L-Phe formation from the D-isomer is less affected Brevibacillus brevis