| Entry |
|
|---|
| Name |
gamma-glutamyl hydrolase;
conjugase;
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 |
|---|
| Class |
Hydrolases;
Acting on peptide bonds (peptidases);
Omega peptidases
 |
|---|
| Reaction(IUBMB) |
Hydrolysis of a gamma-glutamyl bond |
|---|
| Reaction(KEGG) |
(other) R04242
 |
|---|
| Comment |
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. |
|---|
| Pathway |
PATH: ec00790 Folate biosynthesis |
|---|
| Orthology |
KO: K01307 gamma-glutamyl hydrolase |
|---|
| Genes |
HSA: 8836(GGH)
PTR: 464204(GGH)
MCC: 700747(GGH)
MMU: 14590(Ggh)
RNO: 25455(Ggh)
CFA: 477896(GGH)
BTA: 525303(GGH)
SSC: 100154232
ECB: 100052567
MDO: 100029624
OAA: 100082379
GGA: 421144(GGH)
TGU: 100220150
XLA: 444589
XTR: 594986(ggh)
DRE: 406624(ggh)
BFO: BRAFLDRAFT_275351 BRAFLDRAFT_275357
SPU: 582718
DME: Dmel_CG32155
DPO: Dpse_GA16720
DAN: Dana_GF24165
DER: Dere_GG15966
DSE: Dsec_GM25600
DSI: Dsim_GD14608
DYA: Dyak_GE19534 Dyak_GE23118
DGR: Dgri_GH15860
DMO: Dmoj_GI12643
AGA: AgaP_AGAP006670
AAG: AaeL_AAEL000271
CQU: CpipJ_CPIJ006930
AME: 551312
NVI: 100117051
TCA: 659635
API: 100167343
NVE: NEMVE_v1g182128 NEMVE_v1g246653
HMG: 100207447 100215242
TAD: TRIADDRAFT_34071
ATH: AT1G78670(ATGGH3) AT1G78680(ATGGH2)
POP: POPTR_1095675 POPTR_1117997
RCU: RCOM_0106060
VVI: 100262251(GSVIVT00027851001)
OSA: 4339329(Os05g0517500)
SBI: SORBI_09g025690(SORBIDRAFT_09g025690)
ZMA: 100274493(cl4945_1)
PPP: PHYPADRAFT_165556 PHYPADRAFT_234686
CRE: CHLREDRAFT_187002(GGH2)
DDI: DDBDRAFT_0187001 DDBDRAFT_0188389
TET: TTHERM_00030360 TTHERM_00130000 TTHERM_00321670 TTHERM_00449200
TTHERM_00819530 TTHERM_01027470 TTHERM_01156850
PTM: GSPATT00002255001 GSPATT00035342001 GSPATT00037241001
PTI: PHATR_13333
 |
|---|
| Structures |
PDB: 1L9X |
|---|
Reference
Authors
Title
Journal
|
1
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. |
|---|
Reference
Authors
Title
Journal
Organism
|
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.
Homo sapiens [GN:hsa], Rattus norvegicus [GN:rno], Bos taurus
[GN:bta], Gallus gallus [GN:gga] |
|---|
Reference
Authors
Title
Journal
Organism
|
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.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
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.
Homo sapiens [GN:hsa] |
|---|
Reference
Authors
Title
Journal
Organism
|
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.
Rattus norvegicus [GN:rno] |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 3.4.19.9
IUBMB Enzyme Nomenclature: 3.4.19.9
ExPASy - ENZYME nomenclature database: 3.4.19.9
BRENDA, the Enzyme Database: 3.4.19.9
CAS: 9074-87-7 |
|---|
