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Literature summary extracted from

  • Toyama, H.; Esaki, N.; Yoshimura, T.; Tanizawa, K.; Soda, K.
    Thermostable alanine racemase of Bacillus stearothermophilus: subunit dissociation and unfolding (1991), J. Biochem., 110, 279-283.
    View publication on PubMed

General Stability

EC Number General Stability Organism
5.1.1.1 in 0.6 M to 1.5 M guanidine hydrochloride the dimeric enzyme is dissociated into a monomeric form, which is catalytically inactive Geobacillus stearothermophilus

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.1 Geobacillus stearothermophilus
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
5.1.1.1 enzyme denatured in 6 M guanidine hydrochloride is renatured either by dialysis or dilution to reduce the guanidine hydrochloride concentration Geobacillus stearothermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.1 L-Ala
-
Geobacillus stearothermophilus D-Ala
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
5.1.1.1 pyridoxal 5'-phosphate the monomeric inactive enzyme appears to bind the cofactor pyridoxal 5'-phosphate by a non-covalent linkage, although the native dimeric enzyme binds the cofactor through an aldimine Schiff base linkage Geobacillus stearothermophilus