Literature summary for 3.5.2.2 extracted from

Cheon, Y.H.; Park, H.S.; Kim, J.H.; Kim, Y.; Kim, H.S.
Manipulation of the active site loops of D-hydantoinase, a (beta/alpha)8-barrel protein, for modulation of the substrate specificity (2004), Biochemistry, 43, 7413-7420.

Search for more literature for 3.5.2.2

Protein Variants

Protein Variants	Comment	Organism
F159A	turnover number for hydantoin is 10% of that of the wild-type enzyme, Km-value for hydantoin is 4.6fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 6.1fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.4fold higher than that of the wild-type enzyme. Specificity of the mutant enzyme towards aromatic substrate hydroxyphenylhydantoin is enhanced by 200fold compared with that of the wild-type enzyme	Geobacillus stearothermophilus
F159I	turnover number for hydantoin is 61% of that of the wild-type enzyme, Km-value for hydantoin is 1.9fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 2.6fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.5fold lower than that of the wild-type enzyme	Geobacillus stearothermophilus
F159L	turnover number for hydantoin 64% of the turnover number of the wild-type enzyme, Km-value for hydantoin is 90% of the value of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 61% of that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 2.5fold lower than that of the wild-type enzyme	Geobacillus stearothermophilus
F159S	turnover number for hydantoin is 4.7% of that of the wild-type enzyme, Km-value for hydantoin is 4fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 15.5fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 5fold higher than that of the wild-type enzyme	Geobacillus stearothermophilus
F159V	turnover number for hydantoin is 22% of that of the wild-type enzyme, Km-value for hydantoin is 1.6fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 2.8fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.5fold lower than that of the wild-type enzyme	Geobacillus stearothermophilus
L65F/F159A F159A	turnover number for hydantoin is 10.9% of that of the wild-type enzyme, Km-value for hydantoin is 4.8fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 11fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 2.4fold higher than that of the wild-type enzyme. Specificity of the mutant enzyme towards aromatic substrate hydroxyphenylhydantoin is enhanced by 200fold compared with that of the wild-type enzyme	Geobacillus stearothermophilus
M63F/L65V F159A	turnover number for hydantoin is 9.5% of that of the wild-type enzyme, Km-value for hydantoin is 2.6fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 10fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 4.4fold higher than that of the wild-type enzyme. Specificity of the mutant enzyme towards aromatic substrate hydroxyphenylhydantoin is enhanced by 200fold compared with that of the wild-type enzyme	Geobacillus stearothermophilus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
2.2	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, mutant enzyme F159L	Geobacillus stearothermophilus
3.5	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, mutant enzyme F159I	Geobacillus stearothermophilus
3.6	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, mutant enzyme F159V	Geobacillus stearothermophilus
5.4	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, wild-type enzyme	Geobacillus stearothermophilus
7.4	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, mutant enzyme F159A	Geobacillus stearothermophilus
8	9	hydantoin	pH 8.0, 37°C, mutant enzyme F159L	Geobacillus stearothermophilus
13	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, mutant enzyme L65F/F159A	Geobacillus stearothermophilus
24	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, mutant enzyme M63F/L65V	Geobacillus stearothermophilus
27	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, mutant enzyme F159S	Geobacillus stearothermophilus
98	-	hydantoin	pH 8.0, 37°C, wild-type enzyme	Geobacillus stearothermophilus
160	-	hydantoin	pH 8.0, 37°C, mutant enzyme F159V	Geobacillus stearothermophilus
190	-	hydantoin	pH 8.0, 37°C, mutant enzyme F159I	Geobacillus stearothermophilus
260	-	hydantoin	pH 8.0, 37°C, mutant enzyme M63F/L65V	Geobacillus stearothermophilus
400	-	hydantoin	pH 8.0, 37°C, mutant enzyme F159S	Geobacillus stearothermophilus
450	-	hydantoin	pH 8.0, 37°C, mutant enzyme F159A	Geobacillus stearothermophilus
470	-	hydantoin	pH 8.0, 37°C, mutant enzyme L65F/F159A	Geobacillus stearothermophilus

Organism

Organism	UniProt	Comment	Textmining
Geobacillus stearothermophilus	-	SD1	-
Geobacillus stearothermophilus SD1	-	SD1	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
DL-hydroxymethylhydantoin + H2O	-	Geobacillus stearothermophilus	?	-	?
DL-hydroxymethylhydantoin + H2O	-	Geobacillus stearothermophilus SD1	?	-	?
DL-hydroxyphenylhydantoin + H2O	-	Geobacillus stearothermophilus	N-carbamoyl-D-hydroxyphenylglycine	-	?
DL-hydroxyphenylhydantoin + H2O	-	Geobacillus stearothermophilus SD1	N-carbamoyl-D-hydroxyphenylglycine	-	?
DL-phenylhydantoin + H2O	-	Geobacillus stearothermophilus	N-carbamoyl-D-phenylglycine	-	?
DL-phenylhydantoin + H2O	-	Geobacillus stearothermophilus SD1	N-carbamoyl-D-phenylglycine	-	?
hydantoin + H2O	-	Geobacillus stearothermophilus	hydantoic acid	-	?
hydantoin + H2O	-	Geobacillus stearothermophilus SD1	hydantoic acid	-	?

Synonyms

Synonyms	Comment	Organism
D-hydantoinase	-	Geobacillus stearothermophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
11	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, mutant enzyme F159L	Geobacillus stearothermophilus
18	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, wild-type enzyme	Geobacillus stearothermophilus
21	-	hydantoin	pH 8.0, 37°C, mutant enzyme F159S	Geobacillus stearothermophilus
42	-	hydantoin	pH 8.0, 37°C, mutant enzyme M63F/L65V	Geobacillus stearothermophilus
45	-	hydantoin	pH 8.0, 37°C, mutant enzyme F159A	Geobacillus stearothermophilus
46	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, mutant enzyme F159I	Geobacillus stearothermophilus
48	-	hydantoin	pH 8.0, 37°C, mutant enzyme L65F/F159A	Geobacillus stearothermophilus
50	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, mutant enzyme F159V	Geobacillus stearothermophilus
97	-	hydantoin	pH 8.0, 37°C, mutant enzyme F159V	Geobacillus stearothermophilus
110	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, mutant enzyme F159A	Geobacillus stearothermophilus
180	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, mutant enzyme M63F/L65V	Geobacillus stearothermophilus
200	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, mutant enzyme L65F/F159A	Geobacillus stearothermophilus
270	-	hydantoin	pH 8.0, 37°C, mutant enzyme F159I	Geobacillus stearothermophilus
280	-	hydantoin	pH 8.0, 37°C, mutant enzyme F159L	Geobacillus stearothermophilus
280	-	DL-hydroxyphenylhydantoin	pH 8.0, 37°C, mutant enzyme F159S	Geobacillus stearothermophilus
440	-	hydantoin	pH 8.0, 37°C, wild-type enzyme	Geobacillus stearothermophilus

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Release 2023.1 (January 2023)