[E296Q]LTA4H in complex with Arg-Ala-Arg substrate

Structure-based dissection of the active site chemistry of leukotriene a4 hydrolase: implications for m1 aminopeptidases and inhibitor design.

Assay for rapid analysis of the tri-peptidase activity of LTA4 hydrolase.

Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates.

Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms.

Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375.

Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation.

LTA-4 hydrolase,Leukotriene A(4) hydrolase,Tripeptide aminopeptidase LTA4H

HHHHHHPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDLTIEKVVINGQEVKYA
LGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKL
TYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEF
SETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHQISHSWTGNLVTNKTWDHF
WLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLE
QLLGGPEIFLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQR
WITAKEDDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIPLA
LKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAMLVGKDLKVD

TRI-PEPTIDE WAS CO-CRYSTALLIZED WITH [E296Q]LTA4H BY LIQUID-LIQUID DIFFUSION IN MELTING-POINT CAPILLARIES. A TRIS-BUFFERED (10 mM, PH 7.5) SOLUTION OF PROTEIN AND TRIPEPTIDE, MOLAR RATIO 1:10 (~70 MICROM PROTEIN), WAS LAYERED ON THE PRECIPITATE SOLUTION CONTAINING 28% (WEIGHT/VOLUME) POLYETHYLENE GLYCOL (MW 8000), 50 mM NA ACETATE, 100 mM IMIDAZOLE, PH 6.8, AND 5 MM YBCL3. CRYSTALS WERE ADDITIONALLY SOAKED IN SOLUTIONS WITH INCREASED TRI-PEPTIDE CONCENTRATION PRIOR TO DATA COLLECTION, liquid-liquid diffusion, temperature 298K

Same enzyme complexed with inhibitor RB3041

TRANSITION STATE, ANALOGUE PEPTIDE, HYDROLYSIS, ALTERNATIVE SPLICING, CYTOPLASM, HYDROLASE, LEUKOTRIENE BIOSYNTHESIS, METAL-BINDING, METALLOPROTEASE, MULTIFUNCTIONAL ENZYME, PROTEASE, ZINC, TRIPEPTIDE SUBSTRATE

PEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDLTIEKVVINGQEVKYALGERQS
YKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEV
SVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESM
LKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGH
TVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGP
EIFLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQRWITAKE
DDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIPLALKMATE
QGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAMLVGKDLKVD