Literature summary for 5.1.1.1 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.

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General Stability

General Stability	Organism
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

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
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)

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

Cofactor

Cofactor	Comment	Organism	Structure
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

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Release 2023.1 (January 2023)