KEGG   ENZYME: 3.4.19.9Help
Entry
EC 3.4.19.9                 Enzyme                                 

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
BRITE hierarchy
Reaction(IUBMB)
Hydrolysis of a gamma-glutamyl bond
Reaction(KEGG)
(other) R04242
Show
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.
History
EC 3.4.19.9 created 1972 as EC 3.4.12.10, transferred 1978 to EC 3.4.22.12, transferred 1992 to EC 3.4.19.9, modified 1997
Pathway
Folate biosynthesis
Orthology
K01307  
gamma-glutamyl hydrolase
Genes
HSA: 
8836(GGH)
PTR: 
464204(GGH)
PPS: 
GGO: 
PON: 
MCC: 
700747(GGH)
MCF: 
MMU: 
14590(Ggh)
RNO: 
25455(Ggh)
CGE: 
HGL: 
TUP: 
CFA: 
AML: 
FCA: 
PTG: 
BTA: 
525303(GGH)
BOM: 
PHD: 
CHX: 
OAS: 
SSC: 
CFR: 
BACU: 
LVE: 
ECB: 
MYB: 
MYD: 
PALE: 
MDO: 
SHR: 
OAA: 
GGA: 
421144(GGH)
MGP: 
TGU: 
FAB: 
PHI: 
APLA: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
ACS: 
PBI: 
XLA: 
444589(ggh)
XTR: 
594986(ggh)
DRE: 
406624(ggh) 563836(im:7151442)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
CMK: 
BFO: 
SPU: 
DME: 
Dmel_CG32155(l(3)72Dp)
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
AT1G78660(GGH1) AT1G78670(GGH3) AT1G78680(GGH2)
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
MTR: 
CAM: 
FVE: 
PPER: 
PMUM: 
MDM: 
CSV: 
CMO: 
RCU: 
POP: 
VVI: 
SLY: 
100191133(GGH1) 100191134(GGH3) 100191135(GGH2)
SOT: 
OSA: 
DOSA: 
Os05t0517500-01(Os05g0517500)
OBR: 
BDI: 
SBI: 
SORBI_09g025670(SORBIDRAFT_09g025670) SORBI_09g025680(SORBIDRAFT_09g025680) SORBI_09g025690(SORBIDRAFT_09g025690)
ZMA: 
100274493(cl4945_1)
SITA: 
ATR: 
s00170p00050820(AMTR_s00170p00050820)
SMO: 
PPP: 
CRE: 
VCN: 
MIS: 
CSL: 
CVR: 
MBR: 
DDI: 
DPP: 
DFA: 
ACAN: 
TET: 
PTM: 
PTI: 
PIF: 
EHX: 
GTT: 
NGR: 
 » show all
Taxonomy
Reference
1
  Authors
McGuire, J.J. and Coward, J.K.
  Title
Pteroylpolyglutamates: biosynthesis, degradation and function.
  Journal
In: Blakley, R.L. and Benkovic, S.J. (Eds.), Folates and Pterins, John Wiley and Sons, New York, 1984, p. 135-191.
Reference
2  [PMID:8343522]
  Authors
Wang Y, Nimec Z, Ryan TJ, Dias JA, Galivan J.
  Title
The properties of the secreted gamma-glutamyl hydrolases from H35 hepatoma cells.
  Journal
Biochim. Biophys. Acta. 1164 (1993) 227-35.
  Sequence
[rno:25455]
Reference
3  [PMID:7565632]
  Authors
Yao R, Rhee MS, Galivan J.
  Title
Effects of gamma-glutamyl hydrolase on folyl and antifolylpolyglutamates in cultured H35 hepatoma cells.
  Journal
Mol. Pharmacol. 48 (1995) 505-11.
Reference
4  [PMID:8816764]
  Authors
Yao R, Schneider E, Ryan TJ, Galivan J.
  Title
Human gamma-glutamyl hydrolase: cloning and characterization of the enzyme expressed in vitro.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 10134-8.
  Sequence
[hsa:8836]
Reference
5  [PMID:8621474]
  Authors
Yao R, Nimec Z, Ryan TJ, Galivan J.
  Title
Identification, cloning, and sequencing of a cDNA coding for rat gamma-glutamyl hydrolase.
  Journal
J. Biol. Chem. 271 (1996) 8525-8.
  Sequence
[rno:25455]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9074-87-7

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