Glutathione hydrolase 5 proenzyme (EC 3.4.19.13) (Gamma-glutamyl transpeptidase-related enzyme) (GGT-rel) (Gamma-glutamyltransferase 5) (GGT 5) (EC 2.3.2.2) (Gamma-glutamyltransferase-like activity 1) (Gamma-glutamyltranspeptidase 5) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) [Cleaved into: Glutathione hydrolase 5 heavy chain; Glutathione hydrolase 5 light chain]
1_MARGY 6_ GATVS 11_ LVLLG 16_ LGLAL 21_ AVIVL 26_ AVVLS 31_ RHQAP 36_ CGPQA 41_ FAHAA 46_ VAADS 51_ KVCSD 56_ IGRAI 61_ LQQQG 66_ SPVDA 71_ TIAAL 76_ VCTSV 81_ VNPQS 86_ MGLGG 91_ GVIFT 96_ IYNVT 101_ TGKVE 106_ VINAR 111_ ETVPA 116_ SHAPS 121_ LLDQC 126_ AQALP 131_ LGTGA 136_ QWIGV 141_ PGELR 146_ GYAEA 151_ HRRHG 156_ RLPWA 161_ QLFQP 166_ TIALL 171_ RGGHV 176_ VAPVL 181_ SRFLH 186_ NSILR 191_ PSLQA 196_ STLRQ 201_ LFFNG 206_ TEPLR 211_ PQDPL 216_ PWPAL 221_ ATTLE 226_ TVATE 231_ GVEVF 236_ YTGRL 241_ GQMLV 246_ EDIAK 251_ EGSQL 256_ TLQDL 261_ AKFQP 266_ EVVDA 271_ LEVPL 276_ GDYTL 281_ YSPPP 286_ PAGGA 291_ ILSFI 296_ LNVLR 301_ GFNFS 306_ TESMA 311_ RPEGR 316_ VNVYH 321_ HLVET 326_ LKFAK 331_ GQRWR 336_ LGDPR 341_ SHPKL 346_ QNASR 351_ DLLGE 356_ TLAQL 361_ IRQQI 366_ DGRGD 371_ HQLSH 376_ YSLAE 381_ AWGHG 386_ TGTSH 391_ VSVLG 396_ EDGSA 401_ VAATS 406_ TINTP 411_ FGAMV 416_ YSPRT 421_ GIILN 426_ NELLD 431_ LCERC 436_ PRGSG 441_ TTPSP 446_ VSGDR 451_ VGGAP 456_ GRCWP 461_ PVPGE 466_ RSPSS 471_ MVPSI 476_ LINKA 481_ QGSKL 486_ VIGGA 491_ GGELI 496_ ISAVA 501_ QAIMS 506_ KLWLG 511_ FDLRA 516_ AIAAP 521_ ILHVN 526_ SKGCV 531_ EYEPN 536_ FSQEV 541_ QRGLQ 546_ DRGQN 551_ QTQRP 556_ FFLNV 561_ VQAVS 566_ QEGAC 571_ VYAVS 576_ DLRKS 581_GEAAG
1: Cleaves the gamma-glutamyl bond of extracellular glutathione tripeptide (gamma-Glu-Cys-Gly) and certain glutathione conjugates (PubMed:1676842, PubMed:21447318). Hydrolyzes glutathione releasing L-Glu and Cys-Gly dipeptide which is further metabolized to maintain extracellular cysteine levels but also to provide cysteine necessary for intracellular glutathione synthesis (PubMed:1676842, PubMed:21447318). Among glutathione-S-conjugates metabolizes leukotriene C4 (LTC4) and S-geranylgeranyl-glutathione (GGG), but is inactive toward gamma-glutamyl leucine. Converts extracellular LTC4 to LTD4 during acute inflammatory response. Acts as a negative regulator of GGG bioactivity. GGT5 (via GGG catabolism) and ABCC1 (via extracellular transport) establish GGG gradients within lymphoid tissues to position P2RY8-positive lymphocytes at germinal centers in lymphoid follicles and restrict their chemotactic transmigration from blood vessels to bone marrow parenchyma (By similarity). The transpeptidation reaction, i.e. the transfer of gamma-glutamyl moiety to an acceptor molecule to yield a new gamma-glutamyl compound requires high concentration of dipeptide acceptor and is considered nonphysiological (PubMed:21447318, PubMed:29667297)