Molecular cloning and amino acid sequence of leukotriene A4 hydrolase.
A cDNA clone corresponding to leukotriene A4 hydrolase was isolated from a human lung lambda gt11 expression library by immunoscreening with a polyclonal antiserum. Several additional clones from human lung and placenta cDNA lambda g11 libraries were obtained by plaque hybridization with the 32P-labeled lung cDNA clone. One of these clones has an insert of 1910 base pairs that contains the complete protein-coding region. From the deduced primary structure, leukotriene A4 hydrolase is a 610 amino and protein with a calculated molecular weight of 69,140. No apparent homologies with microsomal epoxide hydrolases were found. RNA blot analysis indicated substantial amounts of a discrete mRNA of approximately equal to 2250 nucleotides in lung tissue and leukocytes.
Funk
C D
CD
Department of Physiological Chemistry, Karolinska Institutet, Stockholm, Sweden.
Rådmark
O
O
Fu
J Y
JY
Matsumoto
T
T
Jörnvall
H
H
Shimizu
T
T
Samuelsson
B
B
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004262:DNA Restriction Enzymes; D004851:Epoxide Hydrolases / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics; D005260:Female; D005796:Genes; D006801:Humans; D008168:Lung / Q000201:enzymology; D008969:Molecular Sequence Data; D010920:Placenta / Q000201:enzymology
D004262:DNA Restriction Enzymes; D004851:Epoxide Hydrolases; C043134:leukotriene A4 hydrolase