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L5170

Sigma-Aldrich

Leukotriene A4 Hydrolase human

recombinant, expressed in E. coli

Synonym(s):

LTA-4 hydrolase, LTA4, LTA4H

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

description

contains C-terminal his-tag

Assay

≥90% (SDS-PAGE)

mol wt

~69 kDa

NCBI accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... LTA4H(4048)

Application

Leukotriene A4 Hydrolase human (LTA4H) is a drug target for anti-inflammation, and for cancer prevention and therapy. It is also suitable for screening inhibitors of Leukotriene B4 synthesis. LTA4H is used to study allergic asthma and airway hyperresponsiveness .

Biochem/physiol Actions

Leukotriene A4 Hydrolase human (LTA4H) is a bifunctional zinc metalloenzyme that converts LTA4 into Leukotriene B4, and also demonstrates aminopeptidase activity. Leukotriene B4 is a lipid chemoattractant that plays critical roles in inflammaton, immune responses, host defenses against infections, and lipid homeostasis. Inhibition of LTA4H in a mouse model decreases LTB4 in the airways and attenuates airway inflammation and airway hyperreactivity through modulation of T cell and dendritic cell function .

Physical form

Supplied as a solution in 100mM Tris, pH 8.0, containing 20% glycerol and 100mM potassium chloride.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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J Haeggström et al.
The Journal of biological chemistry, 261(14), 6332-6337 (1986-05-15)
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 chromatography, and gas chromatography-mass spectrometry. After subcellular fractionation, the enzymatic activity was
John W Newman et al.
Progress in lipid research, 44(1), 1-51 (2005-03-08)
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, control of
L Orning et al.
The Journal of biological chemistry, 269(15), 11269-11273 (1994-04-15)
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-1 s-1. This exceeds by 10-fold the kcat/Km for its lipid
A J Fretland et al.
Chemico-biological interactions, 129(1-2), 41-59 (2001-01-13)
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 are typically unstable in aqueous environments and
N Ohishi et al.
The Journal of biological chemistry, 262(21), 10200-10205 (1987-07-25)
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 those of

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