Literature summary for 5.1.1.1 extracted from

Watanabe, A.; Yoshimura, T.; Mikami, B.; Hayashi, H.; Kagamiyama, H.; Esaki, N.
Reaction mechanism of alanine racemase from Bacillus stearothermophilus: X-ray crystallographic studies of the enzyme bound with N-(5'-phosphopyridoxyl)alanine (2002), J. Biol. Chem., 277, 19166-19172.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging-drop vapor diffusion method. Crystal structure of the enzyme bound with reaction intermediate analogs, N-(5'-phosphopyridoxyl)-L-alanine and N-(5'-phosphopyridoxyl)-D-alanine, determined at 2.0 A resolution with the crystallographic R factor of 17.2 for PLP-L-Ala and 16.9 for PLP-D-Ala complexes	Geobacillus stearothermophilus

Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-Ala	Tyr265 and Lys39 are the catalytic bases removing alpha-hydrogen from L- and D-alanine	Geobacillus stearothermophilus	D-Ala	-	r

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Release 2023.1 (January 2023)