LEUKOTRIENE A4 HYDROLASE (HUMAN RECOMBINANT)
LEUKOTRIENE A4 HYDROLASE (HUMAN RECOMBINANT)结构式
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常用名 | LEUKOTRIENE A4 HYDROLASE (HUMAN RECOMBINANT) | 英文名 | LEUKOTRIENE A4 HYDROLASE (HUMAN RECOMBINANT) |
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| CAS号 | 90119-07-6 | 分子量 | N/A | |
| 密度 | N/A | 沸点 | N/A | |
| 分子式 | N/A | 熔点 | N/A | |
| MSDS | N/A | 闪点 | N/A |
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Binding to and Inhibition of Insulin-Regulated Aminopeptidase by Macrocyclic Disulfides Enhances Spine Density.
Mol. Pharmacol. 89 , 413-24, (2016) Angiotensin IV (Ang IV) and related peptide analogs, as well as nonpeptide inhibitors of insulin-regulated aminopeptidase (IRAP), have previously been shown to enhance memory and cognition in animal models. Furthermore, the endogenous IRAP substrates oxytocin... |
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Leukotriene A(4) hydrolase inhibition attenuates allergic airway inflammation and hyperresponsiveness.
Am. J. Respir. Crit. Care Med. 181 , 899-907, (2010) Allergic asthma is characterized by reversible airway obstruction, lung inflammation, and airway hyperresponsiveness (AHR). Previous studies using leukotriene B(4) (LTB(4)) receptor 1-deficient mice and adoptive transfer experiments have suggested that LTB(4)... |
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Role of leukotriene A4 hydrolase aminopeptidase in the pathogenesis of emphysema.
J. Immunol. 192(11) , 5059-68, (2014) The leukotriene A4 hydrolase (LTA4H) is a bifunctional enzyme with epoxy hydrolase and aminopeptidase activities. We hypothesize that the LTA4H aminopeptidase activity alleviates neutrophilic inflammation, which contributes to cigarette smoke (CS)-induced emp... |
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Molecular cloning of a cDNA coding for human leukotriene A4 hydrolase. Complete primary structure of an enzyme involved in eicosanoid synthesis.
J. Biol. Chem. 262(29) , 13873-6, (1987) We have isolated a near full-length cDNA encoding human leukotriene A4 hydrolase, which synthesizes a potent chemotactic and spasmogenic compound, leukotriene B4. A human spleen cDNA library was screened with a 48-mer oligonucleotide probe, synthesized accord... |
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Leukotriene A4 hydrolase in the human lung. Inactivation of the enzyme with leukotriene A4 isomers.
J. Biol. Chem. 262(21) , 10200-5, (1987) Leukotriene A4 hydrolase from the human lung was purified to apparent homogeneity. The molecular weight (68,000-71,000), the amino acid composition, and the N-terminal amino acid sequence were similar to those of the human neutrophil enzyme but different from... |
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Leukotriene A4. Enzymatic conversion into 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid by mouse liver cytosolic epoxide hydrolase.
J. Biol. Chem. 261(14) , 6332-7, (1986) Mouse liver homogenates transformed leukotriene A4 into a 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid. This novel enzymatic metabolite of leukotriene A4 was characterized by physical means including ultraviolet spectroscopy, high performance liquid chromato... |
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Epoxide hydrolases: their roles and interactions with lipid metabolism.
Prog. Lipid Res. 44(1) , 1-51, (2005) The epoxide hydrolases (EHs) are enzymes present in all living organisms, which transform epoxide containing lipids by the addition of water. In plants and animals, many of these lipid substrates have potent biologically activities, such as host defenses, con... |
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Purification and characterisation of leukotriene A4 hydrolase from rat neutrophils.
Biochim. Biophys. Acta 840(1) , 43-50, (1985) Leukotriene A4 hydrolase was rapidly and extensively purified from rat neutrophils using anion exchange and gel filtration high-pressure liquid chromatography. The enzyme which converts the allylic epoxide leukotriene A4 to the 5,12-dihydroxyeicosatetraenoic ... |
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Epoxide hydrolases: biochemistry and molecular biology.
Chem. Biol. Interact. 129(1-2) , 41-59, (2000) Epoxides are organic three-membered oxygen compounds that arise from oxidative metabolism of endogenous, as well as xenobiotic compounds via chemical and enzymatic oxidation processes, including the cytochrome P450 monooxygenase system. The resultant epoxides... |
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The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity.
J. Biol. Chem. 269(15) , 11269-73, (1994) Leukotriene-A4 hydrolase (EC 3.3.2.6) cleaved the NH2-terminal amino acid from several tripeptides, typified by arginyl-glycyl-aspartic acid, arginyl-glycyl-glycine, and arginyl-histidyl-phenylalanine, with catalytic efficiencies (kcat/Km) > or = 1 x 10(6) M-... |