Studies on the active site of leukotriene A4 hydrolase.
Wetterholm
A
A
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Mueller
M J
MJ
Blomster
M
M
Samuelsson
B
B
Haeggström
J Z
JZ
D001665:Binding Sites; D002384:Catalysis; D003931:Diacetyl / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004851:Epoxide Hydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018698:Glutamic Acid / Q000502:physiology; D006801:Humans; D007093:Imidazoles / Q000494:pharmacology; D017572:Leukotriene A4 / Q000378:metabolism; D008741:Methyl Methanesulfonate / Q000494:pharmacology; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D010446:Peptide Fragments / Q000494:pharmacology; D010658:Phenylglyoxal / Q000494:pharmacology
D004791:Enzyme Inhibitors; D007093:Imidazoles; D017572:Leukotriene A4; D010446:Peptide Fragments; D018698:Glutamic Acid; D008741:Methyl Methanesulfonate; D004851:Epoxide Hydrolases; D003931:Diacetyl; D010658:Phenylglyoxal; C043134:leukotriene A4 hydrolase; C012160:N-acetylimidazole