KEGG   ENZYME: 3.5.1.26Help
Entry
EC 3.5.1.26                 Enzyme                                 
Name N4-(beta-N-acetylglucosaminyl)-L-asparaginase;
aspartylglucosylamine deaspartylase;
aspartylglucosylaminase;
aspartylglucosaminidase;
aspartylglycosylamine amidohydrolase;
N-aspartyl-beta-glucosaminidase;
glucosylamidase;
beta-aspartylglucosylamine amidohydrolase;
4-N-(beta-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
Class Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy
Sysname N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
Reaction(IUBMB) N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O =
N-acetyl-beta-D-glucosaminylamine + L-aspartate [RN:R03421]
Reaction(KEGG) R03421
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Substrate N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine [CPD:C04540];
H2O [CPD:C00001]
Product N-acetyl-beta-D-glucosaminylamine [CPD:C01239];
L-aspartate [CPD:C00049]
Comment Acts only on asparagine-oligosaccharides containing one amino acid,
i.e., the asparagine has free alpha-amino and alpha-carboxyl groups
[cf. EC 3.5.1.52, peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine
amidase]
Pathway PATH: ec00511  Other glycan degradation
Orthology KO: K01444  N4-(beta-N-acetylglucosaminyl)-L-asparaginase
Genes HSA: 175(AGA)
PTR: 461616(AGA)
MCC: 699740(AGA)
MMU: 11593(Aga)
RNO: 290923(Aga)
CFA: 475638(AGA)
BTA: 511345(AGA)
SSC: 100152203
ECB: 100060636
MDO: 100017534
OAA: 100087946
GGA: 422558(AGA)
TGU: 100231883
XLA: 496249
DRE: 566517(aga)
BFO: BRAFLDRAFT_117129 BRAFLDRAFT_86031
CIN: 100177598 100184715
SPU: 593612
DME: Dmel_CG10474 Dmel_CG1827 Dmel_CG4372
DPO: Dpse_GA14866 Dpse_GA18140
DAN: Dana_GF11609 Dana_GF12478 Dana_GF12480
DER: Dere_GG20738 Dere_GG24090
DPE: Dper_GL17147 Dper_GL17509
DSE: Dsec_GM15681 Dsec_GM21137
DSI: Dsim_GD10667 Dsim_GD25160 Dsim_GD25331
DYA: Dyak_GE12034 Dyak_GE13669 Dyak_GE19290
DGR: Dgri_GH22932
DMO: Dmoj_GI18418
AGA: AgaP_AGAP012301
AAG: AaeL_AAEL009406
CQU: CpipJ_CPIJ012618
AME: 411392
NVI: 100119424
TCA: 663067
API: 100164194
ISC: IscW_ISCW001950
CEL: R04B3.2(glycosylasparaginase)
CBR: CBG02104
BMY: Bm1_03250
SMM: Smp_173480
NVE: NEMVE_v1g122819 NEMVE_v1g157905 NEMVE_v1g79749
HMG: 100205957
TAD: TRIADDRAFT_24893
ATH: AT5G61540
POP: POPTR_730562
RCU: RCOM_1501020
VVI: 100242161(GSVIVT00030825001)
OSA: 4336581(Os04g0549300)
ZMA: 100280081
PPP: PHYPADRAFT_125543
NCR: NCU09718
PAN: PODANSg1289
MGR: MGG_03346
FGR: FG02189.1
XCC: XCC2914(aspG)
XCB: XC_1195
XCA: xccb100_1239(aspG)
XCV: XCV3222
XAC: XAC3092(aspG)
XOO: XOO1760(aspG)
XOM: XOO_1660
XOP: PXO_01618
SML: Smlt2173
SMT: Smal_1767
CCR: CC_2359
CCS: CCNA_02444
CDF: CD0139
RMR: Rmar_1344
DFE: Dfer_2594
CPI: Cpin_6563
GFO: GFO_0141
FJO: Fjoh_2037
RBI: RB2501_03780
Taxonomy
Structures PDB: 1APY  1APZ  1AYY  1P4K  1P4V  2GAC  2GAW  2GL9  9GAA  9GAC  
     9GAF  
Reference
  Authors
  Title

  Journal
  Organism
 1  [PMID:5010303]
Kono M, Yamashina I.
Purification and properties of 4-L-aspartylglycosylamine
amidohydrolase from hog kidney.
Biochim. Biophys. Acta. 258 (1972) 600-17.
Sus scofa [GN:ssc]
Reference
  Authors
  Title
  Journal
  Organism
 2  [PMID:6061403]
Mahadevan S, Tappel AL.
Beta-aspartylglucosylamine amido hydrolase of rat liver and kidney.
J. Biol. Chem. 242 (1967) 4568-76.
Rattus norvegicus [GN:rno]
Reference
  Authors
  Title

  Journal
  Organism
 3  [PMID:5778645]
Tarentino AL, Maley F.
The purification and properties of a beta-aspartyl
N-acetylglucosylamine amidohydrolase from hen oviduct.
Arch. Biochem. Biophys. 130 (1969) 295-303.
Gallus gallus [GN:gga]
Other DBs ExplorEnz - The Enzyme Database: 3.5.1.26
IUBMB Enzyme Nomenclature: 3.5.1.26
ExPASy - ENZYME nomenclature database: 3.5.1.26
BRENDA, the Enzyme Database: 3.5.1.26
CAS: 9075-24-5
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