Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Pro-Thr-Val-Thr-Gly-Cys-S-S-Cys-Gly + NADPH + H+ = Pro-Thr-Val-Thr-Gly-Cys + Cys-Gly + NADP+
-
glutathione + acceptor = cysteinylglycine + 5-L-glutamyl-acceptor
-
glutathione + leukotriene D = cysteinylglycine + leukotriene C
-
hypoglycin A + GSH = hypoglycin B + cysteinylglycine
-
glutathione disulfide + glycylglycine = L-Cys-Gly + 5-L-glutamyl-glycylglycine
-
GSH + glycylglycine = L-Cys-Gly + 5-L-glutamyl-glycylglycine
-
GSSG + glycylglycine = L-Cys-Gly + 5-L-glutamyl-glycylglycine
-
gamma-L-glutamyl-L-cysteinyl-glycine + glycylglycine = L-cysteinyl-glycine + 5-L-glutamyl-glycylglycine
-
glutathione + 1-aminocyclopropane-1-carboxylic acid = L-cysteinylglycine + 5-L-glutamyl-1-aminocyclopropane-1-carboxylic acid
-
glutathione + amino acid = L-cysteinylglycine + 5-L-glutamyl-amino acid
-
glutathione + an amino acid = L-cysteinylglycine + 5-L-glutamyl-amino acid
-
glutathione + an amino acid = L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
glutathione + daunomycin = L-cysteinylglycine + 5-L-glutamyl-daunomycin
-
glutathione + glutathione = L-cysteinylglycine + 5-glutamyl-glutathione
-
glutathione + Gly-Gly = L-cysteinylglycine + 5-L-glutamyl-Gly-Gly
-
glutathione + H2O = L-cysteinylglycine + L-glutamate
-
glutathione + L-cysteinylglycine = L-cysteinylglycine + glutathione
-
Gly-L-Cys-Gly + H2O = Gly + L-Cys-Gly
-
S-2,4-dinitrophenyl-L-Cys-Gly + H2O = 2,4-dinitrophenol + L-Cys-Gly
-
S-4-nitrobenzyl-L-Cys-Gly + H2O = 4-nitrobenzyl alcohol + L-Cys-Gly
-
glutathione + H2O = L-cysteinylglycine + L-glutamate
-
reduced glutathione + H2O = L-cysteinylglycine + L-glutamate
-
N-(4-oxoglutaryl)-L-cysteinylglycine + H2O = 2-oxoglutarate + L-cysteinylglycine
-
gamma-Glu-Cys-Gly = L-glutamate + Cys-Gly
-
glutathione = L-cysteinylglycine + 5-oxo-L-proline
-
glutathione = 5-oxoproline + L-Cys-Gly
-
ATP + L-cysteine + glycine = ADP + phosphate + L-cysteinyl-glycine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Characterization of the peptide substrate specificity of glutathionylspermidine synthetase from Crithidia fasciculata
1997
De Craecker, S.; Verbruggen, C.; Rajan, P.; Smith, K.; Haemers, A.; Fairlamb, A.H.
Mol. Biochem. Parasitol.
84
25-32
DDT dehydrochlorinase. II. Substrate and cofactor specificity
1959
Lipke, H.; Kearns, C.W.
J. Biol. Chem.
234
2129-2132
Glutathione-degrading enzymes of microvillus membranes
1982
Kozak, E.M.; Tate, S.S.
J. Biol. Chem.
257
6322-6327
Purification and some properties of gamma-glutamyl transpeptidase from azo dye-induced hepatoma
1974
Taniguchi, N.
J. Biochem.
75
473-480
Kinetic studies of sheep kidney gamma-glutamyl transpeptidase
1976
Karkowsky, A.M.; Bergamini, M.V.W.; Orlowski, M.
J. Biol. Chem.
251
4736-4743
gamma-Glutamyl transpeptidase of sheep-kidney cortex. Isolation, catalytic properties and dissociation into two polypeptide chains
1976
Zelazo, P.; Orlowski, M.
Eur. J. Biochem.
61
147-155
gamma-Glutamyl transpeptidase, a leukotriene metabolizing enzyme
1982
Bernström, K.; Orning, L.; Hammarström, S.
Methods Enzymol.
86
38-45
gamma-Glutamyl transpeptidase: kinetics and mechanism
1985
Allison, D.
Methods Enzymol.
113
419-437
gamma-Glutamyl transpeptidase from kidney
1985
Tate, S.S.; Meister, A.
Methods Enzymol.
113
400-419
gamma-Glutamyl transpeptidase-dependent mutagenicity and cytotoxicity of gamma-glutamyl derivatives: a model for biochemical targeting of chemotherapeutic agents
1998
Keren, R.; Stark, A.A.
Environ. Mol. Mutagen.
32
377-386
Purified gamma-glutamyl transpeptidases from tomato exhibit high affinity for glutathione and glutathione S-conjugates
2000
Martin, M.N.; Slovin, J.P.
Plant Physiol.
122
1417-1426
Role for recombinant gamma-glutamyltransferase from Treponema denticola in glutathione metabolism
2003
Chu, L.; Xu, X.; Dong, Z.; Cappelli, D.; Ebersole, J.L.
Infect. Immun.
71
335-342
gamma-Glutamyl transpeptidase in the yeast Saccharomyces cerevisiae and its role in the vacuolar transport and metabolism of glutathione
2001
Mehdi, K.; Thierie, J.; Penninckx, M.J.
Biochem. J.
359
631-637
gamma-Glutamyl transpeptidase in transgenic tobacco plants. Cellular localization, processing, and biochemical properties
2002
Storozhenko, S.; Belles-Boix, E.; Babiychuk, E.; Herouart, D.; Davey, M.W.; Slooten, L.; Van Montagu, M.; Inze, D.; Kushnir, S.
Plant Physiol.
128
1109-1119
New role for leucyl aminopeptidase in glutathione turnover
2004
Cappiello, M.; Lazzarotti, A.; Buono, F.; Scaloni, A.; D'ambrosio, C.; Amodeo, P.; Mendez, B.L.; Pelosi, P.; Del Corso, A.; Mura, U.
Biochem. J.
378
35-44
Identification of cytosolic leucyl aminopeptidase (EC 3.4.11.1) as the major cysteinylglycine-hydrolysing activity in rat liver
2003
Jösch, C.; Klotz, L.O.; Sies, H.
Biol. Chem.
384
213-218
Purification and characterization of aminopeptidase B from Escherichia coli K-12
2001
Suzuki, H.; Kamatani, S.; Kumagai, H.
Biosci. Biotechnol. Biochem.
65
1549-1558
Specificity of the wound-induced leucine aminopeptidase (LAP-A) of tomato. Activity on dipeptide and tripeptide substrates
2000
Gu, Y.Q.; Walling, L.L.
Eur. J. Biochem.
267
1178-1187
Oxidative inactivation of brain ecto-5'-nucleotidase by thiols/Fe2+ system
2000
Liu, X.W.; Sok, D.E.
Neurochem. Res.
25
1475-1484
Metal ion substitution in the catalytic site greatly affects the binding of sulfhydryl-containing compounds to leucyl aminopeptidase
2006
Cappiello, M.; Alterio, V.; Amodeo, P.; Del Corso, A.; Scaloni, A.; Pedone, C.; Moschini, R.; De Donatis, G.M.; De Simone, G.; Mura, U.
Biochemistry
45
3226-3234
-
Leucyl aminopeptidase PepA
2004
Colloms, S.D.
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds)
1
905-910
-
Membrane alanyl aminopeptidase
2004
Turner, A.J.
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
289-294
Purification and properties of soluble and bound gamma-glutamyltransferases from radish cotyledon
2006
Nakano, Y.; Okawa, S.; Yamauchi, T.; Koizumi, Y.; Sekiya, J.
Biosci. Biotechnol. Biochem.
70
369-376
Purification and characterization of dipeptidase hydrolyzing L-cysteinylglycine from radish cotyledon
2007
Kumada, H.O.; Koizumi, Y.; Sekiya, J.
Biosci. Biotechnol. Biochem.
71
3102-3104
Colorimetric assay of aminopeptidase N activity based on inhibition of the disassembly of gold nano-composites conjugated with a thermo-responsive copolymer
2009
Uehara, N.; Fujita, M.; Shimizu, T.
Anal. Sci.
25
267-273
A 52-kDa leucyl aminopeptidase from Treponema denticola is a cysteinylglycinase that mediates the second step of glutathione metabolism
2008
Chu, L.; Lai, Y.; Xu, X.; Eddy, S.; Yang, S.; Song, L.; Kolodrubetz, D.
J. Biol. Chem.
283
19351-19358
Hydrolysis of S-aryl-cysteinylglycine conjugates catalyzed by porcine kidney cortex membrane dipeptidase
2012
Poon, J.C.; Josephy, P.D.
Xenobiotica
42
1178-1186
Brush border membrane hydrolysis of S-benzyl-cysteine-p-nitroanilide, and activity of aminopeptidase M
1980
Rankin, B.B.; McIntyre, T.M.; Curthoys, N.P.
Biochem. Biophys. Res. Commun.
96
991-996
Chromatographic purification of cysteinyl-glycinase
1957
Semenza, G.
Biochim. Biophys. Acta
24
401-413
Identification of cytosolic leucyl aminopeptidase (EC 3.4.11.1) as the major cysteinylglycine-hydrolysing activity in rat liver
2003
Joesch, C.; Klotz, L.; Sies, H.
Biol. Chem.
384
213-218