Leukotriene A-4 hydrolase (LTA-4 hydrolase) (EC 3.3.2.6) (Leukotriene A(4) hydrolase) (Tripeptide aminopeptidase LTA4H) (EC 3.4.11.4)
1_MPEIV 6_ DTCSL 11_ ASPAS 16_ VCRTK 21_ HLHLR 26_ CSVDF 31_ TRRTL 36_ TGTAA 41_ LTVQS 46_ QEDNL 51_ RSLVL 56_ DTKDL 61_ TIEKV 66_ VINGQ 71_ EVKYA 76_ LGERQ 81_ SYKGS 86_ PMEIS 91_ LPIAL 96_ SKNQE 101_ IVIEI 106_ SFETS 111_ PKSSA 116_ LQWLT 121_ PEQTS 126_ GKEHP 131_ YLFSQ 136_ CQAIH 141_ CRAIL 146_ PCQDT 151_ PSVKL 156_ TYTAE 161_ VSVPK 166_ ELVAL 171_ MSAIR 176_ DGETP 181_ DPEDP 186_ SRKIY 191_ KFIQK 196_ VPIPC 201_ YLIAL 206_ VVGAL 211_ ESRQI 216_ GPRTL 221_ VWSEK 226_ EQVEK 231_ SAYEF 236_ SETES 241_ MLKIA 246_ EDLGG 251_ PYVWG 256_ QYDLL 261_ VLPPS 266_ FPYGG 271_ MENPC 276_ LTFVT 281_ PTLLA 286_ GDKSL 291_ SNVIA 296_ HEISH 301_ SWTGN 306_ LVTNK 311_ TWDHF 316_ WLNEG 321_ HTVYL 326_ ERHIC 331_ GRLFG 336_ EKFRH 341_ FNALG 346_ GWGEL 351_ QNSVK 356_ TFGET 361_ HPFTK 366_ LVVDL 371_ TDIDP 376_ DVAYS 381_ SVPYE 386_ KGFAL 391_ LFYLE 396_ QLLGG 401_ PEIFL 406_ GFLKA 411_ YVEKF 416_ SYKSI 421_ TTDDW 426_ KDFLY 431_ SYFKD 436_ KVDVL 441_ NQVDW 446_ NAWLY 451_ SPGLP 456_ PIKPN 461_ YDMTL 466_ TNACI 471_ ALSQR 476_ WITAK 481_ EDDLN 486_ SFNAT 491_ DLKDL 496_ SSHQL 501_ NEFLA 506_ QTLQR 511_ APLPL 516_ GHIKR 521_ MQEVY 526_ NFNAI 531_ NNSEI 536_ RFRWL 541_ RLCIQ 546_ SKWED 551_ AIPLA 556_ LKMAT 561_ EQGRM 566_ KFTRP 571_ LFKDL 576_ AAFDK 581_ SHDQA 586_ VRTYQ 591_ EHKAS 596_ MHPVT 601_ AMLVG 606_KDLKV
1: Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities. Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the pro-inflammatory mediator leukotriene B4 (LTB4) (PubMed:11917124, PubMed:12207002, PubMed:15078870, PubMed:18804029, PubMed:1897988, PubMed:1975494, PubMed:2244921). Also has aminopeptidase activity, with high affinity for N-terminal arginines of various synthetic tripeptides (PubMed:18804029, PubMed:20813919). In addition to its pro-inflammatory EH activity, may also counteract inflammation by its aminopeptidase activity, which inactivates by cleavage another neutrophil attractant, the tripeptide Pro-Gly-Pro (PGP), a bioactive fragment of collagen generated by the action of matrix metalloproteinase-9 (MMP9) and prolylendopeptidase (PREPL) (PubMed:20813919, PubMed:24591641). Involved also in the biosynthesis of resolvin E1 and 18S-resolvin E1 from eicosapentaenoic acid, two lipid mediators that show potent anti-inflammatory and pro-resolving actions (PubMed:21206090)