print visible entries

print all entries

Ligand N-carbobenzoxy-L-aspartic acid

Basic Ligand Information

Molecular Structure

close all tables

open all tables

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (17 results)

top print hide

Show Substrate (17 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.17.B1

benzyloxycarbonyl-Asp + H2O = ?

651211, 651034

-

3.4.17.B1

benzyloxycarbonyl-Asp + H2O = L-aspartate + benzyloxycarbonate

719687

-

3.4.17.B1

2 entries

3.4.21.63

N-Cbz-L-Asp + sec-butanol = N-Cbz-L-Asp-sec-butyl ester

650680

-

3.4.24.27

benzyloxycarbonyl-Asp + Phe-methylester = benzyloxycarbonyl-Asp-Phe methyl ester + H2O

31133, 31134

3qh1, 3D-view

3.4.24.27

benzyloxycarbonyl-Asp + Phe-methylester = benzyloxycarbonyl-Asp-Phe methyl ester + H2O

31133, 31134

3qh5, 3D-view

3.4.24.27

benzyloxycarbonyl-Asp + Phe-methylester = benzyloxycarbonyl-Asp-Phe methyl ester + H2O

31133, 31134

5wr2, 3D-view

3.4.24.27

benzyloxycarbonyl-Asp + Phe-methylester = benzyloxycarbonyl-Asp-Phe methyl ester + H2O

31133, 31134

5wr3, 3D-view

3.4.24.27

benzyloxycarbonyl-Asp + Phe-methylester = benzyloxycarbonyl-Asp-Phe methyl ester + H2O

31133, 31134

5wr5, 3D-view

3.4.24.27

benzyloxycarbonyl-Asp + Phe-methylester = benzyloxycarbonyl-Asp-Phe methyl ester + H2O

31133, 31134

5wr6, 3D-view

3.4.24.27

carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester = carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester

732993

3qh1, 3D-view

3.4.24.27

carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester = carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester

732993

3qh5, 3D-view

3.4.24.27

carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester = carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester

732993

5wr2, 3D-view

3.4.24.27

carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester = carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester

732993

5wr3, 3D-view

3.4.24.27

carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester = carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester

732993

5wr5, 3D-view

3.4.24.27

carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester = carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester

732993

5wr6, 3D-view

3.4.24.27

12 entries

3.5.1.15

N-carbobenzoxy-L-aspartate + H2O = ?

209005

-

3.5.1.64

Nalpha-benzyloxycarbonyl-L-Asp + H2O = benzyl alcohol + CO2 + L-Asp

172071

-

Product in Enzyme-catalyzed Reactions (21 results)

top print hide

Show Product (21 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.17.6

benzyloxycarbonyl-Asp-Ala + H2O = benzyloxycarbonyl-Asp + Ala

81311

-

3.4.21.19

benzyloxycarbonyl-Asp methyl ester + H2O = benzyloxycarbonyl-Asp + methanol

650308

-

3.4.22.7

N-alpha-benzyloxycarbonyl-L-Asp-4-nitrophenyl ester + H2O = N-alpha-benzyloxycarbonyl-L-Asp + 4-nitrophenol

0

-

3.4.24.27

N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester + H2O = N-benzyloxycarbonyl-L-Asp + L-Phe-methyl ester

0

3qh1, 3D-view

3.4.24.27

N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester + H2O = N-benzyloxycarbonyl-L-Asp + L-Phe-methyl ester

0

3qh5, 3D-view

3.4.24.27

N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester + H2O = N-benzyloxycarbonyl-L-Asp + L-Phe-methyl ester

0

5wr2, 3D-view

3.4.24.27

N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester + H2O = N-benzyloxycarbonyl-L-Asp + L-Phe-methyl ester

0

5wr3, 3D-view

3.4.24.27

N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester + H2O = N-benzyloxycarbonyl-L-Asp + L-Phe-methyl ester

0

5wr5, 3D-view

3.4.24.27

N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester + H2O = N-benzyloxycarbonyl-L-Asp + L-Phe-methyl ester

0

5wr6, 3D-view

3.4.24.27

N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O = N-carbobenzoxy-L-Asp + L-Phe-methyl ester

0

3qh1, 3D-view

3.4.24.27

N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O = N-carbobenzoxy-L-Asp + L-Phe-methyl ester

0

3qh5, 3D-view

3.4.24.27

N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O = N-carbobenzoxy-L-Asp + L-Phe-methyl ester

0

5wr2, 3D-view

3.4.24.27

N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O = N-carbobenzoxy-L-Asp + L-Phe-methyl ester

0

5wr3, 3D-view

3.4.24.27

N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O = N-carbobenzoxy-L-Asp + L-Phe-methyl ester

0

5wr5, 3D-view

3.4.24.27

N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O = N-carbobenzoxy-L-Asp + L-Phe-methyl ester

0

5wr6, 3D-view

3.4.24.27

N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O = N-carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester

0

3qh1, 3D-view

3.4.24.27

N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O = N-carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester

0

3qh5, 3D-view

3.4.24.27

N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O = N-carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester

0

5wr2, 3D-view

3.4.24.27

N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O = N-carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester

0

5wr3, 3D-view

3.4.24.27

N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O = N-carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester

0

5wr5, 3D-view

3.4.24.27

N-carbobenzoxy-L-Asp-L-Phe-methyl ester + H2O = N-carbobenzoxy-L-aspartic acid + L-phenylalanine methyl ester

0

5wr6, 3D-view

3.4.24.27

18 entries

Inhibitor in Enzyme-catalyzed Reactions (11 results)

top print hide

Show Inhibitors (11 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.17

-

756178

-

2.3.1.17

-

756178

-

2.3.1.17

2 entries

3.4.17.11

hydrolysis of 4-amino-N10-methylpteroylglutamic acid

647244

-

3.4.24.27

substrate inhibition

732993

3qh1, 3D-view

3.4.24.27

substrate inhibition

732993

3qh5, 3D-view

3.4.24.27

substrate inhibition

732993

5wr2, 3D-view

3.4.24.27

substrate inhibition

732993

5wr3, 3D-view

3.4.24.27

substrate inhibition

732993

5wr5, 3D-view

3.4.24.27

substrate inhibition

732993

5wr6, 3D-view

3.4.24.27

6 entries

3.5.1.134

-

755035

-

6.3.5.4

weak

1713

-

3D Structure of Enzyme-Ligand-Complex (PDB) (84 results)

top print hide

Show 3D Structure of Enzyme-Ligand-Complex (PDB) (84 entries)

EC NUMBER

ENZYME 3D STRUCTURE

3.4.24.27

3qh1, 3D-view

3.4.24.27

3qh5, 3D-view

3.4.24.27

5wr2, 3D-view

3.4.24.27

5wr3, 3D-view

3.4.24.27

5wr5, 3D-view

3.4.24.27

5wr6, 3D-view

3.4.24.27

3qh1, 3D-view

3.4.24.27

3qh5, 3D-view

3.4.24.27

5wr2, 3D-view

3.4.24.27

5wr3, 3D-view

3.4.24.27

5wr5, 3D-view

3.4.24.27

5wr6, 3D-view

3.4.24.27

3qh1, 3D-view

3.4.24.27

3qh5, 3D-view

3.4.24.27

5wr2, 3D-view

3.4.24.27

5wr3, 3D-view

3.4.24.27

5wr5, 3D-view

3.4.24.27

5wr6, 3D-view

3.4.24.27

3qh1, 3D-view

3.4.24.27

3qh5, 3D-view

3.4.24.27

5wr2, 3D-view

3.4.24.27

5wr3, 3D-view

3.4.24.27

5wr5, 3D-view

3.4.24.27

5wr6, 3D-view

3.4.24.27

3qh1, 3D-view

3.4.24.27

3qh5, 3D-view

3.4.24.27

5wr2, 3D-view

3.4.24.27

5wr3, 3D-view

3.4.24.27

5wr5, 3D-view

3.4.24.27

5wr6, 3D-view

3.4.24.27

3qh1, 3D-view

3.4.24.27

3qh5, 3D-view

3.4.24.27

5wr2, 3D-view

3.4.24.27

5wr3, 3D-view

3.4.24.27

5wr5, 3D-view

3.4.24.27

5wr6, 3D-view

3.4.24.27

3qh1, 3D-view

3.4.24.27

3qh5, 3D-view

3.4.24.27

5wr2, 3D-view

3.4.24.27

5wr3, 3D-view

3.4.24.27

5wr5, 3D-view

3.4.24.27

5wr6, 3D-view

3.4.24.27

3qh1, 3D-view

3.4.24.27

3qh5, 3D-view

3.4.24.27

5wr2, 3D-view

3.4.24.27

5wr3, 3D-view

3.4.24.27

5wr5, 3D-view

3.4.24.27

5wr6, 3D-view

3.4.24.27

3qh1, 3D-view

3.4.24.27

3qh5, 3D-view

3.4.24.27

5wr2, 3D-view

3.4.24.27

5wr3, 3D-view

3.4.24.27

5wr5, 3D-view

3.4.24.27

5wr6, 3D-view

3.4.24.27

3qh1, 3D-view

3.4.24.27

3qh5, 3D-view

3.4.24.27

5wr2, 3D-view

3.4.24.27

5wr3, 3D-view

3.4.24.27

5wr5, 3D-view

3.4.24.27

5wr6, 3D-view

3.4.24.27

3qh1, 3D-view

3.4.24.27

3qh5, 3D-view

3.4.24.27

5wr2, 3D-view

3.4.24.27

5wr3, 3D-view

3.4.24.27

5wr5, 3D-view

3.4.24.27

5wr6, 3D-view

3.4.24.27

3qh1, 3D-view

3.4.24.27

3qh5, 3D-view

3.4.24.27

5wr2, 3D-view

3.4.24.27

5wr3, 3D-view

3.4.24.27

5wr5, 3D-view

3.4.24.27

5wr6, 3D-view

3.4.24.27

3qh1, 3D-view

3.4.24.27

3qh5, 3D-view

3.4.24.27

5wr2, 3D-view

3.4.24.27

5wr3, 3D-view

3.4.24.27

5wr5, 3D-view

3.4.24.27

5wr6, 3D-view

3.4.24.27

3qh1, 3D-view

3.4.24.27

3qh5, 3D-view

3.4.24.27

5wr2, 3D-view

3.4.24.27

5wr3, 3D-view

3.4.24.27

5wr5, 3D-view

3.4.24.27

5wr6, 3D-view

3.4.24.27

84 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (8 results)

top print hide

Show Turnover Number (8 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.4.17.B1

6

-

pH 6.5, 60°C

651034

3.4.24.27

0.3

-

mutant enzyme F114A, at pH 7.5, at 25°C

711866

3.4.24.27

1.3

-

wild type enzyme, at pH 7.5, at 25°C

711866

3.4.24.27

2.1

-

mutant enzyme D150A, at pH 7.5, at 25°C

711866

3.4.24.27

2.3

-

mutant enzyme N227H, at pH 7.5, at 25°C

711866

3.4.24.27

2.5

-

mutant enzyme D150E, at pH 7.5, at 25°C

711866

3.4.24.27

3.2

-

mutant enzyme D150W, at pH 7.5, at 25°C

711866

3.4.24.27

4.9

-

mutant enzyme I168A, at pH 7.5, at 25°C

711866

3.4.24.27

7 entries

K_M Value (9 results)

top print hide

Show KM Value (9 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.4.17.B1

0.22

-

pH 6.5, 60°C

651034

3.4.24.27

2.8

-

pH 5.0 or pH 6.0

31134

3.4.24.27

49

-

mutant enzyme F114A, at pH 7.5, at 25°C

711866

3.4.24.27

54

-

mutant enzyme D150W, at pH 7.5, at 25°C

711866

3.4.24.27

57

-

mutant enzyme D150A, at pH 7.5, at 25°C

711866

3.4.24.27

60

-

mutant enzyme D150E, at pH 7.5, at 25°C

711866

3.4.24.27

62

-

wild type enzyme, at pH 7.5, at 25°C

711866

3.4.24.27

70

-

mutant enzyme N227H, at pH 7.5, at 25°C

711866

3.4.24.27

105

-

mutant enzyme I168A, at pH 7.5, at 25°C

711866

3.4.24.27

8 entries

K_i Value (2 results)

top print hide

Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.1.17

0.017

-

pH 7.4, temperature not specified in the publication

756178

2.3.1.17

0.017

-

pH 7.4, temperature not specified in the publication

756178

2.3.1.17

2 entries

References & Links

Literature References (16)

top print hide

Show Reference (16 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1713

5076775

Glutamine-dependent asparagine synthetase from leukemia cells. Chloride dependence mechanism of action and inhibition

1972

Horowitz, B.; Meister, A.

J. Biol. Chem.

247

6708-6719

31133

-

The effect of inhibitors on thermolysin-catalyzed peptide bond synthesis

1986

Durrant, I.; Beynon, R.J.; Rodgers, P.B.

Biochem. Soc. Trans.

14

143

31134

3792308

Kinetics and equilibrium of enzymatic synthesis of peptides in aqueous/organic biphasic systems. Thermolysin-catalyzed synthesis of N-(benzyloxycarbonyl)-L-aspartyl-L-phenylalanine methyl ester [published erratum appears in Eur J Biochem 1987 Sep 15;167(3):601]

1986

Nakanishi, K.; Kimura, Y.; Matsuno, R.

Eur. J. Biochem.

161

541-549

81311

5806587

Bacterial peptidases. 3. An enzyme specific for N-acyl linkages to alanine

1969

Levy, C.C.; Goldman, P.

J. Biol. Chem.

244

4467-4472

172071

-

A novel enzyme, Nalpha-benzyloxycarbonyl amino acid urethane hydrolase IV

1985

Matsumura, E.; Shin, T.; Murao, S.; Sakaguchi, M.; Kawano, T.

Agric. Biol. Chem.

49

3643-3645

209005

1987315

Purification, characterization, and localization of aspartoacylase from bovine brain

1991

Kaul, R.; Casanova, J.; Johnson, A.B.; Tang, P.; Matalon, R.

J. Neurochem.

56

129-135

647244

5129727

Purification and properties of carboxypeptidase G 1

1971

McCullough, J.L.; Chabner, B.A.; Bertino, J.R.

J. Biol. Chem.

246

7207-7213

650308

11004534

Engineering of substrate mimetics as novel-type substrates for glutamic acid-specific endopeptidases: design, synthesis, and application

2000

Wehofsky, N.; Wissmann, J.D.; Alisch, M.; Bordusa, F.

Biochim. Biophys. Acta

1479

114-122

650680

-

Enzymes catalyzed esterification of N-protcted amino acids with secondary alcohol

1997

Shih, I.L.; Chiu, L.C.; Lai, C.T.; Liaw, W.C.; Tai, D.F.

Biotechnol. Lett.

19

857-859

651034

1597179

Purification and characterization of a thermostable carboxypeptidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus

1992

Colombo, S.; D'Auria, S.; Fusi, P.; Zecca, L.; Raia, C.A.; Tortora, P.

Eur. J. Biochem.

206

349-357

651211

-

Intracellular proteases from the extremely thermophilic archaebacterium Sulfolobus solfataricus

1991

Fusi, P.; Villa, M.; Burlini, N.; Tortora, P.; Guerritore, A.

Experientia

47

1057-1060

711866

-

Synthesis of N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester catalyzed by thermolysin variants with improved activity

2010

Kusano, M.; Yasukawa, K.; Inouye, K.

Enzyme Microb. Technol.

46

320-325

719687

7559343

Molecular cloning, nucleotide sequence, and expression of a carboxypeptidase-encoding gene from the archaebacterium Sulfolobus solfataricus

1995

Colombo, S.; Toietta, G.; Zecca, L.; Vanoni, M.; Tortora, P.

J. Bacteriol.

177

:5561-5566

732993

24944748

Synthesis of aspartame by thermolysin: an x-ray structural study

2014

Birrane, G.; Bhyravbhatla, B.; Navia, M.

ACS Med. Chem. Lett.

5

706-710

755035

-

N-carbobenzyloxy-D-aspartic acid as a competitive inhibitor of indole-3-acetyl-L-aspartic acid hydrolase of Enterobacter agglomerans

2002

Chou, J.; Mulbry, W.; Cohen, J.

Plant Growth Regul.

37

241-248

756178

28007430

Design and optimization of aspartate N-acetyltransferase inhibitors for the potential treatment of Canavan disease

2017

Thangavelu, B.; Mutthamsetty, V.; Wang, Q.; Viola, R.E.

Bioorg. Med. Chem.

25

870-885

Links to other databases for N-carbobenzoxy-L-aspartic acid

top print hide

Show Links (1 entry)

ChEBI

PubChem

-