Literature summary for 5.1.99.5 extracted from

Martinez-Rodriguez, S.; Andujar-Sanchez, M.; Neira, J.L.; Clemente-Jimenez, J.M.; Jara-Perez, V.; Rodriguez-Vico, F.; Las Heras-Vazquez, F.J.
Site-directed mutagenesis indicates an important role of cysteines 76 and 181 in the catalysis of hydantoin racemase from Sinorhizobium meliloti (2006), Protein Sci., 15, 2729-2738.

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Protein Variants

Protein Variants	Comment	Organism
C181A	no residual activity. The secondary and the tertiary structure of the mutant is not significantly affected. Residue Cys181 is responsible for L-isomer recognition and racemization. Binding thermodynamic parameters of different substrates, thermodynamic parameters of the guanidinium hydrochloride-induced denaturation	Sinorhizobium meliloti
C76A	no residual activity. The secondary and the tertiary structure of the mutant is not significantly affected. Residue Cys76 is responsible for recognition and proton retrieval of D-isomers. Binding thermodynamic parameters of different substrates, thermodynamic parameters of the guanidinium hydrochloride-induced denaturation	Sinorhizobium meliloti

Organism

Organism	UniProt	Comment	Textmining
Sinorhizobium meliloti	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
D-5-monosubstituted hydantoin = L-5-monosubstituted hydantoin	two-base mechanism for the racemization of 5-monosubstituted hydantoins	Sinorhizobium meliloti	a

Renatured (Commentary)

Renatured (Comment)	Organism
thermodynamic parameters of the guanidinium hydrochloride-induced denaturation of wild-type and mutants C76A, C181A	Sinorhizobium meliloti

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-5-methylthioethylhydantoin	-	Sinorhizobium meliloti	D-5-methylthioethylhydantoin	-	r
L-ethylhydantoin	-	Sinorhizobium meliloti	D-ethylhydantoin	-	r
L-isopropylhydantoin	-	Sinorhizobium meliloti	D-isopropylhydantoin	-	r

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Release 2023.1 (January 2023)