PGG2, 11R-HPETE and 15R/S-HPETE are formed from different conformers of arachidonic acid in the prostaglandin endoperoxide H synthase-1 cyclooxygenase site.
PGG2, 11R-HPETE and 15R/S-HPETE are formed from different conformers of arachidonic acid in the prostaglandin endoperoxide H synthase-1 cyclooxygenase site.
复制标题
PGG2、11R-HPETE 和 15R/S-HPETE 由前列腺素内过氧化物 H 合成酶 1 环加氧酶位点中花生四烯酸的不同构象异构体形成。
DOI：
10.1007/978-1-4615-0193-0_11
复制
发表时间：
2002
影响因子：
--
通讯作者：
Smith,WilliamL
中科院分区：
文献类型：
--
作者：
Thuresson,ElizabethD;Lakkides,KarenM;Smith,WilliamL
Prostaglandin endoperoxide H synthases-1 and -2 (PGHS-1 and -2) catalyze the committed step in the formation of prostanoids (prostaglandins, thromboxane A2 (l-6). PGHSs catalyze two separate reactions: a cyclooxygenase reaction in which arachidonate is converted to prostaglandin G2 (PGG2) and a peroxidase reaction in which PGG2undergoes a two-electron reduction to PGH2. The cyclooxygenase reaction begins with a rate-limiting abstraction of the 13-proS hydrogen from arachidonate to yield an arachidonyl radical (7,8). This is followed by sequential oxygen additions at C-11 and C-15 to yield the prostaglandin endoperoxide PGG2. PGHSs exhibit some lipoxygenase activity producing small amounts of 11-hydroperoxy-5Z,8Z,12E,14Z-eicosatetraenoic acid (11-HPETE) and 15-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoic acid (15-HPETE) from arachidonic acid (9, 10). Aspirin-acetylated PGHS-2, which has no cyclooxygenase activity, synthesizes 15R-HPETE (10,11). Studies comparing native and aspirinacetylated PGHS-2 have raised the possibility that arachidonate can bind in distinct orientations in the PGHS-2 active site to produce either PGG2, 1 l R-HPETE or 15RHPETE (10). Here we develop the concept that arachidonate can be bound in the cyclooxygenase active site of ovine (o)PGHS-1 in at least three different, catalytically competent arrangements that lead to PGG2, 11R-HPETE, and 15R/S-HPETE, respectively, and that these three arrangements of arachidonate occur subsequent to its entry into the cyclooxygenase active site.
登录
查看更多内容
前列腺素内过氧化物合酶和细胞色素 P450 单加氧酶对 5,8,11-二十碳三烯酸的氧化：主要代谢物形成的结构和机制。
影响因子：
3.9
作者：
E. Oliw;L. Hörnsten;H. Sprecher;M. Hamberg
通讯作者：
M. Hamberg
DOI：
10.1016/s0021-9258(17)36820-5
发表时间：
1994-05
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
M. Lecomte;O. Laneuville;Chuan Ji;D L DeWitt;William L. Smith
通讯作者：
M. Lecomte;O. Laneuville;Chuan Ji;D L DeWitt;William L. Smith
影响因子：
13.5
作者：
SMITH, WL;MARNETT, LJ;DEWITT, DL
通讯作者：
DEWITT, DL
非甾体抗炎药对人前列腺素内过氧化物 H 合酶-1 和 -2 的差异抑制。
DOI：
--
发表时间：
1994
期刊：
The Journal of pharmacology and experimental therapeutics
影响因子：
--
作者：
Laneuville,O;Breuer,DK;Dewitt,DL;Hla,T;Funk,CD;Smith,WL
通讯作者：
Smith,WL
DOI：
--
发表时间：
1992
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Shimokawa,T;Smith,WL
通讯作者：
Smith,WL