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Literature summary for 5.1.1.1 extracted from

  • Toyama, H.; Tanizawa, K.; Wakayama, M.; Lee, Q.L.; Yoshimura, T.; Esaki, N.; Soda, K.
    Limited proteolysis of thermostable alanine racemase of Bacillus stearothermophilus (1991), Agric. Biol. Chem., 55, 2881-2882.
No PubMed abstract available

Protein Variants

Protein Variants Comment Organism
additional information mutant gene which tandemly encodes the two polypeptides of the enzyme subunit, fragment 1 and fragment 2, cleaved at the position corresponding to the predicted hinge region. The mutant fragmentary alanine racemase is active at about 40% of the activity of the wild type enzyme Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Ala
-
Geobacillus stearothermophilus D-Ala
-
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