EC                 Enzyme                                 

gamma-glutamyl hydrolase;
folate conjugase;
lysosomal gamma-glutamyl carboxypeptidase;
gamma-Glu-X carboxypeptidase;
pteroyl-poly-gamma-glutamate hydrolase;
carboxypeptidase G;
folic acid conjugase;
poly(gamma-glutamic acid) endohydrolase;
polyglutamate hydrolase;
poly(glutamic acid) hydrolase II;
pteroylpoly-gamma-glutamyl hydrolase
Acting on peptide bonds (peptidases);
Omega peptidases
BRITE hierarchy
Hydrolysis of a gamma-glutamyl bond
(other) R04242
A lysosomal or secreted, thiol-dependent peptidase, most active at acidic pH. Commonly studied with folylpoly-gamma-glutamate as substrate, with which the initial cleavage may release glutamate or poly-gamma-glutamate of two or more residues, according to the species of origin of the enzyme. Final products are pteroyl-alpha-glutamate (folic acid) and free glutamate. Highly specific for the gamma-glutamyl bond, but not for the C-terminal amino acid (leaving group). Action on gamma-glutamyl bonds is independent of an N-terminal pteroyl moiety, but it is not known whether an N-terminal gamma-Glu residue can be hydrolysed. Type example of peptidase family C26.
EC created 1972 as EC, transferred 1978 to EC, transferred 1992 to EC, modified 1997
ec00790  Folate biosynthesis
K01307  gamma-glutamyl hydrolase
HSA: 8836(GGH)
PTR: 464204(GGH)
PPS: 100969380(GGH)
GGO: 101150735(GGH)
PON: 100435664(GGH)
NLE: 100595851(GGH)
MCC: 700747(GGH)
MCF: 102126049(GGH)
CSAB: 103236874(GGH)
RRO: 104660106(GGH)
RBB: 108543162(GGH)
CJC: 100415059(GGH)
SBQ: 101047923(GGH)
MMU: 14590(Ggh)
RNO: 25455(Ggh)
CGE: 100751581(Ggh)
NGI: 103737737(Ggh)
HGL: 101724155(Ggh)
CCAN: 109698223(Ggh)
OCU: 100350070(GGH)
TUP: 102485618(GGH)
CFA: 100856436(GGH)
AML: 100482891(GGH)
UMR: 103677471(GGH)
ORO: 101373905(GGH)
FCA: 101100943(GGH)
PTG: 102970330(GGH)
AJU: 106988829(GGH)
BTA: 525303(GGH)
BOM: 102276825(GGH)
BIU: 109568566(GGH)
PHD: 102343185(GGH)
CHX: 102190334(GGH)
OAS: 101118706(GGH)
SSC: 100154232(GGH)
CFR: 102507789(GGH)
CDK: 105094475(GGH)
BACU: 103016741(GGH)
LVE: 103090393(GGH)
OOR: 101273875(GGH)
ECB: 100052567(GGH)
EPZ: 103553263(GGH)
EAI: 106834311(GGH)
MYB: 102240048(GGH)
MYD: 102768461(GGH)
HAI: 109375951(GGH)
PALE: 102886790(GGH)
LAV: 100671079(GGH)
TMU: 101347582
MDO: 100029624(GGH)
SHR: 100922531(GGH)
OAA: 100082379(GGH)
GGA: 421144(GGH)
MGP: 100540892(GGH)
CJO: 107310260(GGH)
APLA: 101790897(GGH)
ACYG: 106039060(GGH)
TGU: 100220150(GGH)
GFR: 102038404(GGH)
FAB: 101814012(GGH)
PHI: 102105349(GGH)
PMAJ: 107200637(GGH)
CCW: 104692925(GGH)
FPG: 101919182(GGH)
FCH: 102055448(GGH)
CLV: 102087830(GGH)
EGZ: 104122047(GGH)
AAM: 106494371(GGH)
ASN: 102387582(GGH)
AMJ: 102558989(GGH)
PSS: 102460960(GGH)
CPIC: 101933582 101939707(GGH)
ACS: 100563793(ggh)
PVT: 110088990(GGH)
PBI: 103066894(GGH)
GJA: 107110867(GGH)
XLA: 444589(ggh.L) 496099(ggh.2.L)
XTR: 100490929 594986(ggh)
NPR: 108796604(GGH) 108800416
DRE: 406624(ggh) 563836(zgc:171566)
IPU: 108265017 108267579(GGH) 108281015(Ggh)
TRU: 101066803(ggh) 101071237
LCM: 102357327
CMK: 103179122 103180721(ggh)
SPU: 582718
APLC: 110980374
DME: Dmel_CG32155(l(3)72Dp)
DSI: Dsimw501_GD14608(Dsim_GD14608)
AAG: 5573776
BIM: 100742651
BTER: 100651812
SOC: 105196643
AEC: 105148388
ACEP: 105627444
PBAR: 105430931
PGC: 109851946
NVI: 100117051
TCA: 659635
DPA: 109537699
BMOR: 101736547
PMAC: 106708714
PXY: 105393491
FCD: 110848151
CRG: 105317584
LAK: 106166411
ATH: AT1G78660(GGH1) AT1G78670(GGH3) AT1G78680(GGH2)
THJ: 104813997
CPAP: 110812565
TCC: 18594335
DZI: 111276559
GMX: 100796947 547881(GH)
ADU: 107459833
AIP: 107613260
LJA: Lj0g3v0178769.1(Lj0g3v0178769.1) Lj0g3v0338049.1(Lj0g3v0338049.1)
PPER: 18779010
PMUM: 103325967
PAVI: 110757564
ZJU: 107403905
CMO: 103501819
CMAX: 111480987
CMOS: 111446777
CPEP: 111789236
RCU: 8288177
JCU: 105636017
HBR: 110650012
JRE: 109011928
VVI: 100262251
SLY: 100191133(GGH1) 100191134(GGH3) 100191135(GGH2)
INI: 109188447(DR15) 109188449
SIND: 105176926
OEU: 111370840
HAN: 110912906
DCR: 108220262
BVG: 104891329
OSA: 4339329
DOSA: Os05t0517500-01(Os05g0517500)
OBR: 102700528
BDI: 100828890
ATS: 109747252(LOC109747252)
ZMA: 100274493(cl4945_1)
SITA: 101782252
PDA: 103708964
EGU: 105047475
MUS: 103989604
DCT: 110094990
AOF: 109848496
ATR: 18426350
DDI: DDB_G0286535(gghA) DDB_G0289365(gghB)
DFA: DFA_01284 DFA_11781(gghA)
SMIN: v1.2.013270.t1(symbB.v1.2.013270.t1) v1.2.013687.t1(symbB.v1.2.013687.t1) v1.2.023128.t1(symbB.v1.2.023128.t1) v1.2.024246.t1(symbB.v1.2.024246.t1)
 » show all
McGuire, J.J. and Coward, J.K.
Pteroylpolyglutamates: biosynthesis, degradation and function.
In: Blakley, R.L. and Benkovic, S.J. (Eds.), Folates and Pterins, John Wiley and Sons, New York, 1984, p. 135-191.
2  [PMID:8343522]
Wang Y, Nimec Z, Ryan TJ, Dias JA, Galivan J.
The properties of the secreted gamma-glutamyl hydrolases from H35 hepatoma cells.
Biochim. Biophys. Acta. 1164 (1993) 227-35.
3  [PMID:7565632]
Yao R, Rhee MS, Galivan J.
Effects of gamma-glutamyl hydrolase on folyl and antifolylpolyglutamates in cultured H35 hepatoma cells.
Mol. Pharmacol. 48 (1995) 505-11.
4  [PMID:8816764]
Yao R, Schneider E, Ryan TJ, Galivan J.
Human gamma-glutamyl hydrolase: cloning and characterization of the enzyme expressed in vitro.
Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 10134-8.
5  [PMID:8621474]
Yao R, Nimec Z, Ryan TJ, Galivan J.
Identification, cloning, and sequencing of a cDNA coding for rat gamma-glutamyl hydrolase.
J. Biol. Chem. 271 (1996) 8525-8.
Other DBs
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IUBMB Enzyme Nomenclature:
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BRENDA, the Enzyme Database:
CAS: 9074-87-7

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