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3.3.2.6: leukotriene-A4 hydrolase

This is an abbreviated version!
For detailed information about leukotriene-A4 hydrolase, go to the full flat file.

Word Map on EC 3.3.2.6

Reaction

leukotriene A4
+
H2O
=
leukotriene B4

Synonyms

EH, epoxide hydrolase, hydrolase, leukotriene A4, leukotriene A(4) hydrolase, leukotriene A4 hydrolase, leukotriene A4 hydrolase/aminopeptidase, leukotriene hydrolase A4, leukotriene-A4 hydrolase, leukotriene-A4-hydrolase, LT A4 hydrolase, LTA-4 hydrolase, LTA4 hydrolase, LTA4-h, LTA4H, More

ECTree

     3 Hydrolases
         3.3 Acting on ether bonds
             3.3.2 Ether hydrolases
                3.3.2.6 leukotriene-A4 hydrolase

Crystallization

Crystallization on EC 3.3.2.6 - leukotriene-A4 hydrolase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure determination
crystal structure of enzyme complexed with bestatin
crystal structure of enzyme in complex with captopril, thioamine or hydroxamic acid
-
enzyme in complex with inhibitors SAHA or M344, X-ray diffraction structure determination and analysis
in complex with inhibitor N-[3(R)-[(hydroxyamino)carbonyl]-2-benzyl-1-oxopropyl]-L-alanine, to 1.9 A resolution, space group P212121. The inhibitor binds along the sequence signature for M1 aminopeptidases, GXMEN. It exhibits bidentate chelation of the catalytic zinc and binds to LTA4H's enzymatically essential carboxylate recognition site. The inhibitor binds in an extended beta-sheet conformation between the zinc ion and Arg563. The carboxyl moiety forms two hydrogen bonds with Arg563, and the hydroxamate moiety chelates the zinc ion in a bidentate fashion
liquid-liquid diffusion method, with 28% (w/v) polyethylene glycol, 100 mM imidazole pH 7.2, and 5 mM YbCl3
molecular docking studies with inhibitors. Position and size of substituted groups plays a key role in the binding conformation of the compounds. Compounds without branches, and p-substituted compounds tend to bind LTA4H in the channel, forming a hydrogen bond between the pyrrolidine nitrogen atom and Gly269 main-chain oxygen atom. o- or m-Substituted compounds can stay at the entrance part of the pocket in a reversed orientation with three hydrogen bonds, the nitrogen atom to Gln136, the oxygen atom connected to alkyl group to His295, and the oxygen atom connected to bibenzyl to Gly268 main-chain nitrogen atom
-
mutant E296Q in complex with N-(4-oxo-4-pyrrolidinyl-butanoyl)-L-proline, liquid/liquid diffusion method, using 22-30% (w/v) PEG 8000, 100 mM NaAc, 100 mM imidazole buffer (pH 6.5-7.0), and 5 mM YbCl3
mutant enzyme E296Q in complex with inhibitors RB3040 and RB3041, and substrate, liquid-liquid diffusion method, using 28% (w/v) polyethylene glycol, 50 mM Na acetate, 100 mM imidazole (pH 6.8), and 5 mM YbCl3
the structure of LTA4H in complex with the competitive inhibitor is determined
-
wild-type enzyme and mutant D375N
wild-type enzyme and mutant E271Q
-
enzyme in complex with inhibitors SAHA or M344, X-ray diffraction structure determination and analysis
sitting drop vapor diffusion method, using 100 mM Bis-Tris pH 6.5, 20%(w/v) PEG 3350