[HTML][HTML] Spatial requirements for 15-(R)-hydroxy-5Z, 8Z, 11Z, 13E-eicosatetraenoic acid synthesis within the cyclooxygenase active site of murine COX-2: why …
SW Rowlinson, BC Crews, DC Goodwin… - Journal of Biological …, 2000 - ASBMB
The two isoforms of cyclooxygenase, COX-1 and COX-2, are acetylated by aspirin at Ser-
530 and Ser-516, respectively, in the cyclooxygenase active site. Acetylated COX-2 is
essentially a lipoxygenase, making 15-(R)-hydroxyeicosatetraenoic acid (15-HETE) and 11-
(R)-hydroxyeicosatetraenoic acid (11-HETE), whereas acetylated COX-1 is unable to
oxidize arachidonic acid to any products. Because the COX isoforms are structurally similar
and share approximately 60% amino acid identity, we postulated that differences within the …
530 and Ser-516, respectively, in the cyclooxygenase active site. Acetylated COX-2 is
essentially a lipoxygenase, making 15-(R)-hydroxyeicosatetraenoic acid (15-HETE) and 11-
(R)-hydroxyeicosatetraenoic acid (11-HETE), whereas acetylated COX-1 is unable to
oxidize arachidonic acid to any products. Because the COX isoforms are structurally similar
and share approximately 60% amino acid identity, we postulated that differences within the …