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Basic Ligand Information
Roles as Enzyme Ligand
Enzyme Kinetic Parameters
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Ligand N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine

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Basic Ligand Information

Molecular Structure

Picture of N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine (click for magnification)

Molecular Formula

BRENDA Name

InChIKey

C₁₂H₂₁N₃O₈

N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine

YTTRPBWEMMPYSW-HRRFRDKFSA-N

Synonyms:

1,2-dideoxy-1-[L-beta-aspartamido]-2-acetamido-beta-D-glucopyranose, 1-beta-aspartyl-N-acetyl-D-glucosaminylamine, 1-L-beta-aspartamido-(2-acetamido)-1,2-dideoxy-beta-D-glucose, 2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-beta-D-glucose, 2-acetamido-1-N-(4-L-aspartyl)-2-deoxy-beta-D-glycopyranosylamine, AsnGlcNAc, GlcNAc-Asn, GlcNAcAsn, N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine, N4-(acetyl-beta-D-glucosaminyl)asparagine, N4-(beta-N-acetylglucosaminyl)-L-asparagine

Pathway Source

Pathways

MetaCyc

L-asparagine degradation III (mammalian)

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.26

N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine + H2O = ?

654334

3.5.1.26

N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = 2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate

209057, 209058, 209059, 209060, 209061, 209062, 209063, 209050, 209054, 209049, 209048, 209051, 209047

3.5.1.26

N4-(beta-N-acetylglucosaminyl)-L-asparagine + H2O = 2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate

681417

3.5.1.26

N4-(beta-N-acetylglucosaminyl)-L-asparagine + H2O = N-acetyl-D-glucosaminylamine + L-aspartate

753573, 755339

3.5.1.26

4 entries

Substrate in Enzyme-catalyzed Reactions (10 results)

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EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.2.1.96

GlcNAc-Asn + Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAc = Manalpha(1-6)(Manalpha(1-3))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-Asn

700895

3.2.1.96

GlcNAcAsn + H2O = N-acetyl-D-glucosamine + L-asparagine

1,2-dideoxy-1-[L-beta-aspartamido]-2-acetamido-beta-D-glucopyranose + H2O = ?

171767

3.5.1.26

2-acetamido-1-beta-(L-aspartamido)-1,2-dideoxy-beta-D-glucose + H2O = 2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate

209055, 209056, 209067, 209066, 209068, 209065, 209064

3.5.1.26

N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine + H2O = 2-acetamido-2-deoxy-beta-D-glucopyranosylamine + L-asparagine

654334

3.5.1.26

N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine + H2O = ?

654334

3.5.1.26

N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = 2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate

209057, 209058, 209059, 209060, 209061, 209062, 209063, 712919, 209050, 209054, 209049, 209048, 209051, 209047

3.5.1.26

N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate

681417, 657367, 656376, 654537

3.5.1.26

N4-(beta-N-acetylglucosaminyl)-L-asparagine + H2O = 2-acetamido-1-amino-1,2-dideoxy-beta-D-glucose + L-aspartate

681417

3.5.1.26

N4-(beta-N-acetylglucosaminyl)-L-asparagine + H2O = N-acetyl-D-glucosaminylamine + L-aspartate

753573, 755339, 712162

3.5.1.26

7 entries

Product in Enzyme-catalyzed Reactions (8 results)

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EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.2.1.96

Asn(GlcNAc)2-(Man)5 + H2O = AsnGlcNAc + Man5(GlcNAc)

0, 171700, 171686

3.2.1.96

Asn(GlcNAc)2-(Man)6 + H2O = AsnGlcNAc + (GlcNAc)1-(Man)6

0, 171698, 171686

3.2.1.96

Asn(GlcNAc)2-(Man)6(GlcNAc)2 + H2O = AsnGlcNAc + (GlcNAC)1-(Man)6(GlcNAc)2

171698, 171686

3.2.1.96

(Man)3(GlcNAc)2Asn + H2O = (Man)3GlcNAc + GlcNAc-Asn

3.2.1.96

(Man)5(GlcNAc)2Asn + H2O = (Man)5GlcNAc + GlcNAc-Asn

3.2.1.96

(Man)6(GlcNAc)2Asn + H2O = (Man)6GlcNAc + GlcNAc-Asn

0, 171707

3.2.1.96

asialo-N-acetyl-lactosaminic-type glycoasparagine + H2O = GlcNAc-Asn + ?

171712

3.2.1.96

Manalpha1->6(Manalpha1->3)Manalpha1->6(Manalpha1->2Manalpha1->3)Manbeta1->4GlcNAcbeta1->4GlcNAcAsn + H2O = Manalpha1->6(Manalpha1->3)Manalpha1->6(Manalpha1->2Manalpha1->3)Manbeta1->4GlcNAcbeta1 + GlcNAcAsn

171687, 0

3.2.1.96

8 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (7 results)

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EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.5.1.26

0.00015

mutant enzyme T152C

681417

3.5.1.26

0.00015

mutant with T152C

681417

3.5.1.26

0.08

mutant T203I, pH 7.5, 37°C

755339

3.5.1.26

5.93

mutant T99K, pH 7.5, 37°C

755339

3.5.1.26

14.18

recombinant wild-type enzyme, pH 7.5, 37°C

native enzyme

wild type enzyme

K_M Value (17 results)

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EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

0.05

0.059

0.09

0.09

recombinant wild-type enzyme, pH 7.5, 37°C

0.11

0.116

0.16

at 37°C and pH 7.7, pH- and temperature dependend

209063

3.5.1.26

0.166

mutant T203I, pH 7.5, 37°C

0.208

0.26

mutant T99K, pH 7.5, 37°C

755339

3.5.1.26

0.4

for amidase-3

209068

3.5.1.26

0.538

at pH 7.5 and 37°C

712919

3.5.1.26

0.64

amidase-1 and amidase-2, value depending on enzyme concentration

0.88

1.25

2.5

References & Links

Literature References (38)

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Show Reference (38 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

171686

26849

endo-beta-N-Acetylglucosaminidase from Streptomyces plicatus

1978

Tarentino, A.L.; Trimble, R.B.; Maley, F.

Methods Enzymol.

50C

574-580

171687

26848

endo-beta-N-Acetylglucosaminidases CI and CII from Clostridium perfringens

1978

Kobata, A.

Methods Enzymol.

567-574

171698

4204552

Purification and properties of an endo-beta-N-acetylglucosaminidase from Streptomyces griseus

1974

Tarentino, A.L.; Maley, F.

J. Biol. Chem.

249

811-817

171700

4152561

endo-beta-N-Acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae

1974

Koide, N.; Muramatsu, T.

J. Biol. Chem.

249

4897-4904

171707

914800

Partial purification and characterization of an engo-beta-N-acetylglucosaminidase from fig extract

1977

Ogata-Arakawa, M.; Muramatsu, T.; Kobata, A.

J. Biochem.

611-614

171712

7378051

Demonstration and cytosolic location of an endo-N-acetyl-beta-D-glucosaminidase activity towards an asialo-N-acetyl-lactosaminic-type substrate in rat liver

1980

Pierce, R.J.; Spik, G.; Montreuil, J.

Biochem. J.

185

261-264

171767

_ber Glykosylamidasen aus Limnaea stagnalis L.

1970

Kaverzneva, E.D.; Tschuchrova, A.I.; Kisseleva, V.V.

Liebigs Ann. Chem.

738

130-135

209047

9257709

Recombinant human glycosylasparaginase catalyzes hydrolysis of L-asparagine

1997

Noronkoski, T.; Stoineva, I.B.; Petkov, D.D.; Mononen, I.

FEBS Lett.

412

149-152

209048

9737998

Activation and oligomerization of aspartylglucosaminidase

1998

Saarela, J.; Laine, M.; Tikkanen, R.; Oinonen, C.; Jalanko, A.; Rouvinen, J.; Peltonen, L.

J. Biol. Chem.

273

25320-25328

209049

10531509

Purification and crystallization of precursors and autoprocessed enzymes of Flavobacterium glycosylasparaginase: an N-terminal nucleophile hydrolase

1999

Cui, T.; Liao, P.H.; Guan, C.; Guo, H.C.

Acta Crystallogr. Sect. D

1961-1964

209050

8877373

Purification, biochemistry and molecular cloning of an insect glycosylasparaginase from Spodoptera frugiperda

1996

Liu, Y.; Dunn, G.S.; Aronson, N.N.

Glycobiology

527-536

209051

8670796

Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: implications for catalytic mechanism and autocatalytic activation

1996

Tikkanen, R.; Riikonen, A.; Oinonen, C.; Rouvinen, J.; Peltonen, L.

EMBO J.

2954-2960

209054

8250923

The first demonstration of a prokaryotic glycosylasparaginase

1993

Tarentino, A.L.; Plummer, T.H.

Biochem. Biophys. Res. Commun.

197

179-186

209055

Human aspartylglucosaminidase

1992

Enomaa, N.; Heiskanen, T.; Halila, R.; Sormunen, R.; Seppälä, R.; Vihinen, M.; Peltonen, L.

Biochem. J.

286

613-618

209056

1281977

Purification and structure of human liver aspartylglucosaminidase

1992

Rip, J.W.; Coulter-Mackie, M.B.; Rupar, C.A.; Gordon, B.A.

Biochem. J.

288

1005-1010

209057

1554372

Comparison of liver glycosylasparaginases from six vertebrates

1992

Tollersrud, O.K.; Aronson, N.

Biochem. J.

282

891-897

209058

1859849

Glycoasparaginase in human urine

1991

Kaartinen, V.

Biochim. Biophys. Acta

1097

28-30

209059

2005122

Glycosasparaginase from human leukocytes

1991

Kaartinen, V.; Williams, J.C.; Tomich, J.; Yates, J.R.; Hood, L.E.; Mononen, I.

J. Biol. Chem.

266

5860-5869

209060

2039475

Human leucocyte aspartylglucosaminidase

1991

Halila, R.; Baumann, M.; Ikonen, E.; Enomaa, N.; Peltonen, L.

Biochem. J.

276

251-256

209061

6885799

Purification and properties of human hepatic aspartylglucosaminidase

1983

McGovern, M.M.; Aula, P.; Desnick, R.J.

J. Biol. Chem.

258

10743-10747

209062

666738

Effect of different compounds on 1-aspartamido-beta-N-acetylglucosamine amidohydrolase from human liver

1978

Dugal, B.

Biochem. J.

171

799-802

209063

21658

Purification and some properties of 1-aspartamido-beta-N-acetylglucosamine amidohydrolase from human liver

1977

Dugal, B.; Stromme, J.

Biochem. J.

165

497-502

209064

869921

Measurement of 1-aspartamido-beta-N-acetylglucosamine amidohydrolase activity in human tissues

1977

Dugal, B.

Biochem. J.

163

9-14

209065

5778645

The purification and properties of a beta-aspartyl N-acetylglucosylamine amidohydrolase from hen oviduct

1969

Tarentino, A.I.; Maley, F.

Arch. Biochem. Biophys.

130

295-303

209066

6061403

beta-Aspartylglucosylamine amido hydrolase of rat liver and kidney

1967

Mahadevan, S.; Tappel, A.L.

J. Biol. Chem.

242

4568-4578

209067

4724304

Specificity studies of 4-L-aspartylglycosylamine amido hydrolase

1973

Tanaka, M.; Kohno, M.; Yamashina, I.

J. Biochem.

1285-1289

209068

5010303

Purification and properties of 4-L-aspartylglycosylamine amidohydrolase from hog kidney

1972

Kohno, M.; Yamashina, I.

Biochim. Biophys. Acta

258

600-617

654334

11437347

Glycosylasparaginase activity requires the alpha-carboxyl group, but not the alpha-amino group, on N(4)-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine

2001

Risley, J.M.; Huang, D.H.; Kaylor, J.J.; Malik, J.J.; Xia, Y.Q.; York, W.M.

Arch. Biochem. Biophys.

391

165-170

654537

14616088

Autoproteolytic activation of human aspartylglucosaminidase

2004

Saarela, J.; Oinonen, C.; Jalanko, A.; Rouvinen, J.; Peltonen, L.

Biochem. J.

378

363-371

656376

11697047

Glycosylasparaginase inhibition studies: competitive inhibitors, transition state mimics, noncompetitive inhibitors

2001

Risley, J.M.; Huang, D.H.; Kaylor, J.J.; Malik, J.J.; Xia, Y.Q.

J. Enzyme Inhib.

269-274

657367

12906830

A dual role for an aspartic acid in glycosylasparaginase autoproteolysis

2003

Qian, X.; Guan, C.; Guo, H.C.

Structure

997-1003

681417

17157318

Crystallographic snapshot of a productive glycosylasparaginase-substrate complex

2007

Wang, Y.; Guo, H.C.

J. Mol. Biol.

366

82-92

700895

19252736

Structural basis and catalytic mechanism for the dual functional endo-beta-N-acetylglucosaminidase A

2009

Yin, J.; Li, L.; Shaw, N.; Li, Y.; Song, J.K.; Zhang, W.; Xia, C.; Zhang, R.; Joachimiak, A.; Zhang, H.C.; Wang, L.X.; Liu, Z.J.; Wang, P.

PLoS ONE

e4658

712162

20036741

Molecular and biochemical analysis of an aspartylglucosaminidase from the venom of the parasitoid wasp Asobara tabida (Hymenoptera: Braconidae)

2010

Vinchon, S.; Moreau, S.J.; Drezen, J.M.; Prevost, G.; Cherqui, A.

Insect Biochem. Mol. Biol.

38-48

712919

19158835

Depletion of L-asparagine supply and apoptosis of leukemia cells induced by human glycosylasparaginase

2009

Kelo, E.; Noronkoski, T.; Mononen, I.

Leukemia

1167-1171

732602

24362939

Endo-beta-N-acetylglucosaminidase catalysed glycosylation: tolerance of enzymes to structural variation of the glycosyl amino acid acceptor

2014

Tomabechi, Y.; Squire, M.A.; Fairbanks, A.J.

Org. Biomol. Chem.

942-955

753573

29993127

Biochemical and structural insights into an allelic variant causing the lysosomal storage disorder - aspartylglucosaminuria

2018

Pande, S.; Bizilj, W.; Guo, H.C.

FEBS Lett.

592

2550-2561

755339

30901125

The T99K variant of glycosylasparaginase shows a new structural mechanism of the genetic disease aspartylglucosaminuria

2019

Pande, S.; Guo, H.C.

Protein Sci.

1013-1023

Links to other databases for N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine

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PubChem

Ligand N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine

Basic Ligand Information

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

Substrate in Enzyme-catalyzed Reactions (10 results)

Product in Enzyme-catalyzed Reactions (8 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (7 results)

KM Value (17 results)

References & Links

Literature References (38)

Links to other databases for N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine

k_cat Value (Turnover Number) (7 results)

K_M Value (17 results)