Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.1.1.1 extracted from

  • Kurokawa, Y.; Watanabe, A.; Yoshimura, T.; Esaki, N.; Soda, K.
    Transamination as a side-reaction catalyzed by alanine racemase of Bacillus stearothermophilus (1998), J. Biochem., 124, 1163-1169.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
K39A mutant enzyme is inactive as a catalyst for racemization as well as transamination Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Ala the enzyme catalyzes transamination as a side function.The pyridoxal form of the enzyme is converted to the pyridoxamine form by incubation with its natural substrate, D-alanine or L-alanine, under acidic conditions: the enzyme loses its racemase activity concomitantly. The pyridoxamine form of the enzyme returns to the pyridoxal form by incubation with pyruvate at alkaline pH Geobacillus stearothermophilus D-Ala
-
r
additional information the epsilon-amino group of Lys39 participates in both racemization and transamination when catalyzed by the wild-type enzyme Geobacillus stearothermophilus ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.5
-
racemization from D-Ala to L-Ala Geobacillus stearothermophilus
10
-
racemization from L-Ala to D-Ala Geobacillus stearothermophilus

pH Range

pH Minimum pH Maximum Comment Organism
8.5 11 pH 8.5: about 55% of maximal activity, pH 11.0: about 65% of maximal activity, racemization from L-Ala to D-Ala Geobacillus stearothermophilus
9 11 pH 9: about 50% of maximal activity, pH 11.0: about 35% of maximal activity, racemization from D-Ala to L-Ala Geobacillus stearothermophilus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate the pyridoxal form of the enzyme is converted to the pyridoxamine form by incubation with its natural substrate, D-alanine or L-alanine, under acidic conditions: the enzyme loses its racemase activity concomitantly. The pyridoxamine form of the enzyme returns to the pyridoxal form by incubation with pyruvate at alkaline pH Geobacillus stearothermophilus