Literature summary for 3.3.2.10 extracted from

Hopmann, K.H.; Himo, F.
Insights into the reaction mechanism of soluble epoxide hydrolase from theoretical active site mutants (2006), J. Phys. Chem. B, 110, 21299-21310.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
wild-type and mutants Y381F, Y465F, Y381F/Y465F. The two active site tyrosine residues act in concert to lower the activation barrier for the alkylation step	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
Y381F	crystallization data, optimized transition state distances. Stronger preference for attack at the benzylic position than mutant Y465F	Homo sapiens
Y381F/Y465F	crystallization data, optimized transition state distances	Homo sapiens
Y465F	crystallization data, optimized transition state distances. Stronger preference for attack at the terminal position than mutant Y381F	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P34913	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(1S,2S)-beta-methylstyrene oxide + H2O	enzyme attacks almost exclusively at the benzylic position	Homo sapiens	?	-	?
(S)-styrene oxide + H2O	preferred attack at the benzylic position	Homo sapiens	1-phenylethane-1,2-diol	-	?

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Release 2023.1 (January 2023)