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1 c acid] and its subsequent transformation to LTA4 5-LOX is thought to receive arachidonic acid from t
2 3 as critical for acid and base catalysis of LTA4 and reduced glutathione, respectively.
3 rted by cyclooxygenases into leukotriene A4 (LTA4) and subsequently into the chemotaxin LTB4, which h
4 ximately 40% (P<0.05) to a similar extent as LTA4 ( approximately 50%, P<0.05) but was not converted
5  such as arachidonic acid or the leukotriene LTA4, are further processed by endothelial enzymes via t
6                                   The enzyme-LTA4 complex structures and dynamic domain movements pro
7 y of S36E increased linearly with increasing LTA4 concentrations during the steady-state kinetics ana
8 ic pocket that accommodates the omega-end of LTA4, distant from the aminopeptidase active site, thus
9 el, which accommodates the aliphatic tale of LTA4 during EH reaction.
10 sulting structural alterations indicate that LTA4 entrance into the active site is a dynamic process
11 ants in the leukotriene pathway (ALOX5AP and LTA4) have emerged as susceptibility factors for myocard
12                                              LTA4 hydrolase (EC 3.3.2.6) is a dual-function enzyme th
13 h enantiomers as substrates, and recombinant LTA4 hydrolase (LTA4H) converted chiral 5S(6)-epoxide-co
14 on the expression and subsequent activity of LTA4 hydrolase and LTC4 synthase, respectively.
15 acterize the proximal promoters of the human LTA4 hydrolase and SPARC genes, each within 1 day.
16 hibit proinflammatory mediator production by LTA4 hydrolase and to block arachidonate conversion by h
17 his unusual enzyme, we have cloned the mouse LTA4 hydrolase cDNA.
18 ts of Pro-Gly-Pro, it could be inferred that LTA4 hydrolase cleaves at the N terminus of the palindro
19                                              LTA4 hydrolase differs from other proteins required for
20                A 1.62-A crystal structure of LTA4 hydrolase in a dual complex with ARM1 and the Pro-G
21 Here, we determined the crystal structure of LTA4 hydrolase in complex with a Pro-Gly-Pro analog at 1
22          Thus the widespread distribution of LTA4 hydrolase in various cell types in the tissues sugg
23  plausible that the widespread occurrence of LTA4 hydrolase in various tissues may correspond more wi
24 g and analysis of genomic sequences of mouse LTA4 hydrolase indicated that it is a single-copy gene s
25               ARM1 represents a new class of LTA4 hydrolase inhibitor that holds promise for improved
26          In situ hybridization revealed that LTA4 hydrolase is localized in the crypt cells of the sm
27            Using these animals, we show that LTA4 hydrolase is required for the production of LTB4 in
28                                              LTA4 hydrolase is widely expressed, with the highest lev
29 l LTC4 synthase KO or mice transplanted with LTA4 hydrolase-deficient bone marrow.
30                                 Furthermore, LTA4 hydrolase-deficient mice are resistant to platelet-
31  To address this question, we have generated LTA4 hydrolase-deficient mice.
32 s an endogenous aminopeptidase substrate for LTA4 hydrolase.
33 vivo role for the aminopeptidase activity of LTA4 hydrolase.
34 as an aminopeptidase than its function as an LTA4 hydrolase.
35  no apparent effect of the glucocorticoid on LTA4-hydrolase-immunoreactive protein levels or specific
36      Coexpression of FLAP partially restored LTA4 hydrolysis product formation by 5-LOX-Y181A.
37 oximately 60-70% 5-LOX-wt levels) but not of LTA4 hydrolysis products.
38 at levels comparable to 5-LOX-wt but reduced LTA4 hydrolysis products.
39  of approximately 0.5 muM) and conversion of LTA4 into LTB4 by purified LTA4H with a Ki of 2.3 muM.
40 rts the highly unstable epoxide intermediate LTA4 into LTB4, a potent leukocyte activating agent, whi
41 Hence, ARM1 selectively blocks conversion of LTA4 into LTB4, although sparing the enzyme's anti-infla
42               In certain inflammatory cells, LTA4 is converted into the cysteinyl leukotriene (cysLT)
43                                Leukotrienes (LTA4, LTB4, LTC4, LTD4, and LTE4) are inflammatory lipid
44                  Co-application of LTB4 with LTA4, LTC4, LTD4, or LTE4 suppressed LTB4-induced activa
45 n crystal structures of LTA4H complexed with LTA4, providing the structural underpinnings of the enzy
46 oxide hydrolase activity (i.e. conversion of LTA4 to LTB4).
47 ential for the conversion of leukotriene A4 (LTA4) to leukotriene B4 (LTB4) and also possesses an ami
48 ticipate in cLT production by conjugation of LTA4 with glutathione to produce LTC4.
49 (LTC4) synthase catalyzes the conjugation of LTA4 with reduced GSH to form LTC4, the parent of the re
50  catalyzes the conjugation of the fatty acid LTA4 with the tripeptide GSH to produce LTC4, the parent

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