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J. Biol. Chem., Vol. 267, Issue 2, 789-793, Jan, 1992
K Ohashi, KH Ruan, RJ Kulmacz, KK Wu and LH Wang
Polymerase chain reaction techniques have been used to isolate a cDNA clone
containing the entire protein coding region of thromboxane A2 synthase (EC
5.3.99.5) from a human lung cDNA library. The cDNA clone hybridizes with a
single 2.1-kilobase mRNA species in phorbol ester- induced human
erythroleukemia and monocytic leukemia cell lines. A second cDNA, differing
only by an insert of 163 base pairs near the 3'- end of the translated
region, was also found to be present in the same library. The proteins
predicted from both nucleic acid sequences include the three polypeptide
sequences determined from amino acid sequencing of the purified human
platelet enzyme, five potential sites for N-glycosylation, and a
hydrophobic region that may serve to anchor the synthase in the endoplasmic
reticulum membrane. The longer predicted protein, designated thromboxane
synthase-I, contains 534 amino acids, with a Mr of 60,684, whereas the
shorter protein, designated thromboxane synthase-II, contains 460 amino
acids and has a Mr of 52,408. Although thromboxane synthase-II lacks the
conserved cysteine that serves as the proximal heme ligand in the other
cytochromes, significant sequence similarities exist among thromboxane
synthase-I and -II and several P450s, particularly those in family 3. The
overall amino acid identity is considerably less than 40%, making it likely
that thromboxane synthase represents a previously undefined family of
cytochrome P450.
Primary structure of human thromboxane synthase determined from the cDNA sequence
Department of Internal Medicine, University of Texas Health Science Center, Houston 77030.
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