KEGG   ENZYME: 3.4.17.21Help
Entry
EC 3.4.17.21                Enzyme                                 

Name
glutamate carboxypeptidase II;
N-acetylated-gamma-linked-acidic dipeptidase (NAALADase);
folate hydrolase;
prostate-specific membrane antigen;
pteroylpoly-gamma-glutamate carboxypeptidase;
microsomal gamma-glutamyl carboxypeptidase;
pteroylpolyglutamate hydrolase;
folylpolyglutamate hydrolase;
pteroylpoly-gamma-glutamate hydrolase;
pteroylpolygammaglutamyl hydrolase;
pteroylpolyglutamate hydrolase;
pteroylpolyglutamic acid hydrolase;
PSM antigen;
acetylaspartylglutamate dipeptidase;
NAALA dipeptidase;
rat NAAG peptidase;
mGCP;
membrane glutamate carboxypeptidase;
N-acetylated-alpha-linked-amino dipeptidase;
prostrate-specific membrane antigen;
N-Acetylated alpha-linked acidic dipeptidase;
PSMA
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metallocarboxypeptidases
BRITE hierarchy
Reaction(IUBMB)
Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates
Comment
A metallo-carboxypeptidase that is predominantly expressed as a membrane-bound enzyme of 94-100 kDa , but also exists in a soluble form. Hydrolyses alpha-peptide bonds in Ac-Asp-Glu, Asp-Glu, and Glu-Glu, but also gamma-glutamyl bonds in gamma-Glu-Glu, and folylpoly-gamma-glutamates. With folylpoly-gamma-glutamates, shows processive carboxypeptidase activity to produce pteroylmonoglutamate [4]. Does not hydrolyse Ac-beta-Asp-Glu. Known inhibitors: quisqualic acid, Ac-beta-Asp-Glu, and 2-phosphonomethyl-pentanedioate. In peptidase family M28 of Vibrio leucyl aminopeptidase. The release of C-terminal glutamate from folylpoly-gamma-glutamates is also catalysed by EC 3.4.17.11 (glutamate carboxypeptidase) and EC 3.4.19.9 (gamma-Glu-X carboxypeptidase).
History
EC 3.4.17.21 created 1997, modified 2000 (EC 3.4.13.8 created 1972 and EC 3.4.19.8 created 1992, incorporated 2000)
Orthology
K01301  
glutamate carboxypeptidase II
K14592  
folate hydrolase 1
Genes
HSA: 
10003(NAALAD2) 10004(NAALADL1) 2346(FOLH1)
PTR: 
451185(FOLH1) 451309(NAALADL1) 451475 451478(NAALAD2)
PPS: 
100970655(NAALAD2) 100970744(NAALADL1)
GGO: 
101133710(NAALADL1) 101147888(FOLH1)
PON: 
100445995(NAALADL1) 100453848(FOLH1) 100460916(NAALAD2)
MCC: 
694180(NAALAD2) 707714(FOLH1) 717018(NAALADL1)
MCF: 
MMU: 
381204(Naaladl1) 53320(Folh1) 72560(Naalad2)
RNO: 
300384(Naalad2) 83568(Naaladl1) 85309(Folh1)
CGE: 
HGL: 
101702083(Naaladl1) 101722660(Naalad2) 101725016(Folh1)
TUP: 
102475075(NAALADL1) 102487205(FOLH1B) 102488479(NAALAD2)
CFA: 
476775(FOLH1) 483751(NAALADL1) 485139(NAALAD2)
AML: 
100469236(NAALAD2) 100470423(NAALADL1) 100472805
FCA: 
101082777(NAALADL1) 101089389(NAALAD2) 101089641
BTA: 
505865(FOLH1) 506692(NAALADL1) 536439(NAALAD2)
BOM: 
102265480(NAALAD2) 102272952(FOLH1B) 102286181(NAALADL1)
PHD: 
102315808(NAALADL1) 102320530(NAALAD2)
CHX: 
102177776(NAALAD2) 102186842(NAALADL1) 102190665(FOLH1B)
SSC: 
100515250(NAALADL1) 102164324(NAALAD2) 397677(FOLH1)
CFR: 
102510657(FOLH1B)
ECB: 
100050187(NAALAD2) 100056368(NAALADL1) 100060132(FOLH1B)
MYB: 
102246530(NAALADL1) 102258767 102262061(NAALAD2)
MDO: 
100009990 100013563(NAALAD2) 100030670(NAALADL1)
SHR: 
100913549(NAALADL1) 100918727 100927408(NAALAD2)
OAA: 
GGA: 
419010(NAALAD2) 419011(FOLH1)
MGP: 
TGU: 
FAB: 
101814982(FOLH1) 101815312(NAALAD2)
PHI: 
102105283(FOLH1B) 102106596(NAALAD2)
APLA: 
FPG: 
FCH: 
102054726(NAALAD2) 102058819(FOLH1B)
CLV: 
102094196(NAALAD2) 102095234(FOLH1B)
ASN: 
PSS: 
102455710(FOLH1B)
ACS: 
XLA: 
100037180 734632(naalad2)
XTR: 
100485577(folh1) 100487005 594947(naalad2)
DRE: 
100000223(naaladl1) 393247(naalad2)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
BFO: 
CIN: 
SPU: 
ISC: 
CBR: 
LOA: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
ALY: 
GMX: 
CAM: 
FVE: 
CSV: 
RCU: 
VVI: 
SLY: 
OSA: 
DOSA: 
Os01t0740500-00(Os01g0740500) Os01t0743300-01(Os01g0743300) Os03t0790600-01(Os03g0790600)
BDI: 
SBI: 
SORBI_01g005710(SORBIDRAFT_01g005710) SORBI_03g034150(SORBIDRAFT_03g034150) SORBI_03g034260(SORBIDRAFT_03g034260)
ZMA: 
SITA: 
SMO: 
PPP: 
CME: 
KLA: 
PPA: 
VPO: 
DHA: 
PIC: 
LEL: 
CAL: 
CDU: 
YLI: 
PAN: 
FGR: 
SSL: 
BFU: 
ANI: 
NFI: 
AFM: 
AOR: 
AOR_1_1728154(AO090003000972)
ANG: 
ANI_1_512164(An18g03980)
AFV: 
ACT: 
PCS: 
CIM: 
CPW: 
URE: 
PNO: 
TML: 
MPR: 
MGL: 
ACAN: 
PIF: 
GTT: 
RHA: 
SEN: 
ABA: 
ACA: 
ACM: 
TSA: 
SUS: 
CTM: 
GAU: 
RMR: 
CPI: 
SHG: 
CMR: 
DFE: 
SLI: 
RSI: 
RBI: 
MRS: 
 » show all
Taxonomy
Reference
1  [PMID:9123729]
  Authors
Heston WD.
  Title
Characterization and glutamyl preferring carboxypeptidase function of prostate specific membrane antigen: a novel folate hydrolase.
  Journal
Urology. 49 (1997) 104-12.
  Organism
Homo sapiens [GN:hsa]
Reference
2  [PMID:9187245]
  Authors
Rawlings ND, Barrett AJ.
  Title
Structure of membrane glutamate carboxypeptidase.
  Journal
Biochim. Biophys. Acta. 1339 (1997) 247-52.
  Organism
Homo sapiens [GN:hsa]
  Sequence
[hsa:2346]
Reference
3  [PMID:9685395]
  Authors
Halsted CH, Ling EH, Luthi-Carter R, Villanueva JA, Gardner JM, Coyle JT.
  Title
Folylpoly-gamma-glutamate carboxypeptidase from pig jejunum. Molecular characterization and relation to glutamate carboxypeptidase II.
  Journal
J. Biol. Chem. 273 (1998) 20417-24.
  Organism
Sus scofa [GN:ssc]
  Sequence
[ssc:397677]
Reference
4  [PMID:9501243]
  Authors
Luthi-Carter R, Berger UV, Barczak AK, Enna M, Coyle JT.
  Title
Isolation and expression of a rat brain cDNA encoding glutamate carboxypeptidase II.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 3215-20.
  Organism
Rattus norvegicus [GN:rno]
  Sequence
[rno:85309]
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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