Glutathione hydrolase 1 proenzyme (EC 3.4.19.13) (Gamma-glutamyltransferase 1) (Gamma-glutamyltranspeptidase 1) (GGT 1) (EC 2.3.2.2) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) (CD antigen CD224) [Cleaved into: Glutathione hydrolase 1 heavy chain; Glutathione hydrolase 1 light chain]
1_MKKKL 6_ VVLGL 11_ LAVVL 16_ VLVIV 21_ GLCLW 26_ LPSAS 31_ KEPDN 36_ HVYTR 41_ AAVAA 46_ DAKQC 51_ SKIGR 56_ DALRD 61_ GGSAV 66_ DAAIA 71_ ALLCV 76_ GLMNA 81_ HSMGI 86_ GGGLF 91_ LTIYN 96_ STTRK 101_ AEVIN 106_ AREVA 111_ PRLAF 116_ ATMFN 121_ SSEQS 126_ QKGGL 131_ SVAVP 136_ GEIRG 141_ YELAH 146_ QRHGR 151_ LPWAR 156_ LFQPS 161_ IQLAR 166_ QGFPV 171_ GKGLA 176_ AALEN 181_ KRTVI 186_ EQQPV 191_ LCEVF 196_ CRDRK 201_ VLREG 206_ ERLTL 211_ PQLAD 216_ TYETL 221_ AIEGA 226_ QAFYN 231_ GSLTA 236_ QIVKD 241_ IQAAG 246_ GIVTA 251_ EDLNN 256_ YRAEL 261_ IEHPL 266_ NISLG 271_ DVVLY 276_ MPSAP 281_ LSGPV 286_ LALIL 291_ NILKG 296_ YNFSR 301_ ESVES 306_ PEQKG 311_ LTYHR 316_ IVEAF 321_ RFAYA 326_ KRTLL 331_ GDPKF 336_ VDVTE 341_ VVRNM 346_ TSEFF 351_ AAQLR 356_ AQISD 361_ DTTHP 366_ ISYYK 371_ PEFYT 376_ PDDGG 381_ TAHLS 386_ VVAED 391_ GSAVS 396_ ATSTI 401_ NLYFG 406_ SKVRS 411_ PVSGI 416_ LFNNE 421_ MDDFS 426_ SPSIT 431_ NEFGV 436_ PPSPA 441_ NFIQP 446_ GKQPL 451_ SSMCP 456_ TIMVG 461_ QDGQV 466_ RMVVG 471_ AAGGT 476_ QITTA 481_ TALAI 486_ IYNLW 491_ FGYDV 496_ KRAVE 501_ EPRLH 506_ NQLLP 511_ NVTTV 516_ ERNID 521_ QAVTA 526_ ALETR 531_ HHHTQ 536_ IASTF 541_ IAVVQ 546_ AIVRT 551_ AGGWA 556_ AASDS 561_RKGGE
1: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates (such as maresin conjugate (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate, MCTR1) and other gamma-glutamyl compounds (such as leukotriene C4, LTC4) (PubMed:17924658, PubMed:21447318, PubMed:27791009). The metabolism of glutathione by GGT1 releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases (PubMed:27791009). In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound (PubMed:17924658, PubMed:21447318, PubMed:7673200, PubMed:7759490, PubMed:8095045, PubMed:8827453). Contributes to cysteine homeostasis, glutathione homeostasis and in the conversion of the leukotriene LTC4 to LTD4
2: Seems to be catalytically inactive