Mutation of Tyr-383 in leukotriene A4 hydrolase: effects on enzyme activities.
Andberg
M
M
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Wetterholm
A
A
Haeggström
J Z
JZ
D000818:Animals; D001665:Binding Sites; D003001:Cloning, Molecular; D004851:Epoxide Hydrolases / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli; D007700:Kinetics; D051379:Mice; D016297:Mutagenesis, Site-Directed; D010447:Peptide Hydrolases / Q000378:metabolism; D017354:Point Mutation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D014443:Tyrosine
D011994:Recombinant Proteins; D014443:Tyrosine; D004851:Epoxide Hydrolases; D010447:Peptide Hydrolases; C043134:leukotriene A4 hydrolase