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Basic Ligand Information
Roles as Enzyme Ligand
Enzyme Kinetic Parameters
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Ligand N-carbobenzoxy-L-Asp-L-Phe methyl ester

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Basic Ligand Information

Molecular Structure

Picture of N-carbobenzoxy-L-Asp-L-Phe methyl ester (click for magnification)

Molecular Formula

BRENDA Name

InChIKey

C₂₂H₂₄N₂O₇

N-carbobenzoxy-L-Asp-L-Phe methyl ester

YSCNREZXFSZAQO-ROUUACIJSA-N

Synonyms:

Benzyloxycarbonyl-Asp-Phe methyl ester, carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester, N-benzyloxycarbonyl-L-Asp-L-Phe-methyl ester, N-carbobenzoxy-L-Asp-L-Phe-methyl ester, N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester, N-carbobenzyloxy-L-Asp-L-Phe methyl ester, Nalpha-benzyloxycarbonyl-L-aspartyl-L-phenylalanine methyl ester

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.24.27

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

711393

Substrate in Enzyme-catalyzed Reactions (8 results)

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EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.24.27

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

717396

3.4.24.27

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

683276, 683182, 683614, 683615, 684019, 712532, 733524

3.4.24.27

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

668003, 711393

3.4.24.27

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

670784, 669153

3.4.24.27

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

711866

3.4.24.27

N-carbobenzoxy-L-aspartyl-L-phenylalanine methyl ester + H2O = ?

734109

3.4.24.27

N-carbobenzyloxy-L-Asp-L-Phe methyl ester + H2O = ?

668246

3.4.24.27

Nalpha-benzyloxycarbonyl-L-aspartyl-L-phenylalanine methyl ester + H2O = ?

651789

3.4.24.27

8 entries

Product in Enzyme-catalyzed Reactions (2 results)

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EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.24.27

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

31133, 31134

3.4.24.27

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

3.4.24.27

2 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (45 results)

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EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.4.24.27

1.3

pH 7.5, 25°C, recombinant mutant Q225A

683614

3.4.24.27

1.5

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

711866

3.4.24.27

1.6

pH 7.5, 25°C, recombinant mutant Q225V

683614

3.4.24.27

3.3

mutant enzyme S53D/L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

3.3

pH 7.0, 25°C, recombinant mutant G8C/N60C/S65P

683182

3.4.24.27

3.3

pH 7.5, 25°C, recombinant mutant Q225D

683614

3.4.24.27

3.4

pH 7.0, 25°C, recombinant wild-type enzyme

683182

3.4.24.27

3.6

pH 7.5, 25°C, recombinant mutant Q225R

683614

3.4.24.27

3.7

pH 7.5, 25°C, recombinant mutant Q128K

683614

3.4.24.27

3.8

pH 7.5, 25°C, recombinant enzyme

670784

3.4.24.27

3.8

pH 7.5, 25°C, recombinant mutant Q128A

683614

3.4.24.27

3.8

pH 7.5, 25°C, recombinant wild-type enzyme

683276

3.4.24.27

4.3

pH 7.5, 25°C, native enzyme

670784

3.4.24.27

4.3

pH 7.5, 25°C, native wild-type enzyme

683276

3.4.24.27

4.3

pH 7.5, 25°C, recombinant mutants Q128E and Q225E

683614

3.4.24.27

4.7

pH 7.5, 25°C, recombinant wild-type enzyme and mutant Q225K

683614

3.4.24.27

4.8

recombinant mutant G117R, pH 7.5, 25°C

717396

3.4.24.27

5.4

mutant enzyme G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

5.4

purified recombinant mutant N116T, pH 7.5, 25°C

734109

3.4.24.27

5.9

wild type enzyme, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

6.3

mutant enzyme L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

6.4

mutant enzyme S53D/L155A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

6.7

pH 7.0, 25°C, recombinant mutant L144S

683182

3.4.24.27

6.7

purified recombinant mutant N116A, pH 7.5, 25°C

734109

3.4.24.27

pH 7.0, 25°C, recombinant mutant G8C/N60C/S65P/L144S

683182

3.4.24.27

7.1

purified recombinant mutant N116Q, pH 7.5, 25°C

734109

3.4.24.27

7.4

mutant enzyme S53D/G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

7.7

mutant enzyme I168A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

7.7

purified recombinant wild-type enzyme, pH 7.5, 25°C

734109

3.4.24.27

7.9

recombinant wild-type enzyme, pH 7.5, 25°C

717396

3.4.24.27

8.4

recombinant mutant G117K, pH 7.5, 25°C

717396

3.4.24.27

8.7

mutant enzyme L155A, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

9.4

mutant enzyme L144S, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

9.5

wild type enzyme, at pH 7.5, at 25°C

711866

3.4.24.27

10.5

recombinant mutant G117E, pH 7.5, 25°C

717396

3.4.24.27

purified recombinant mutant N116D, pH 7.5, 25°C

734109

3.4.24.27

12.3

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

711866

3.4.24.27

15.5

mutant enzyme D150E/I168A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

15.6

mutant enzyme L144S/D150E/S53D, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

16.5

mutant enzyme D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

mutant enzyme L144S/D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

17.1

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

711866

3.4.24.27

20.5

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

711866

3.4.24.27

24.4

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

711866

3.4.24.27

49.4

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

711866

3.4.24.27

45 entries

K_M Value (49 results)

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Show KM Value (49 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.4.24.27

0.033

pH 5.5

31134

3.4.24.27

0.059

pH 6.0

31134

3.4.24.27

0.06

pH 7.0, 25°C, recombinant mutant L144S

683182

3.4.24.27

0.076

pH 5.0

31134

3.4.24.27

0.1

pH 7.0, 25°C, recombinant mutant G8C/N60C/S65P/L144S

683182

3.4.24.27

0.16

mutant enzyme L144S/D150E/S53D, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

0.17

mutant enzyme L144S/D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

0.18

mutant enzyme D150E/I168A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

0.18

pH 7.0, 25°C, recombinant mutant G8C/N60C/S65P

683182

3.4.24.27

0.19

mutant enzyme L144S, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

0.24

pH 7.5, 25°C, recombinant mutant Q225V

683614

3.4.24.27

0.28

pH 7.5, 25°C, recombinant mutant Q128A

683614

3.4.24.27

0.29

pH 7.5, 25°C, recombinant mutant Q225A

683614

3.4.24.27

0.3

pH 7.5, 25°C, recombinant mutants Q128K and Q225R

683614

3.4.24.27

0.33

pH 7.0, 25°C, recombinant wild-type enzyme

683182

3.4.24.27

0.33

pH 7.5, 25°C, recombinant mutant Q128E

683614

3.4.24.27

0.34

pH 7.5, 25°C, recombinant mutant Q225D

683614

3.4.24.27

0.38

purified recombinant mutant N116Q, pH 7.5, 25°C

734109

3.4.24.27

0.39

pH 7.5, 25°C, recombinant mutant Q225K

683614

3.4.24.27

0.39

purified recombinant wild-type enzyme, pH 7.5, 25°C

734109

3.4.24.27

0.4

pH 7.5, 25°C, recombinant enzyme

670784

3.4.24.27

0.4

pH 7.5, 25°C, recombinant wild-type enzyme

683276

3.4.24.27

0.41

purified recombinant mutant N116A, pH 7.5, 25°C

734109

3.4.24.27

0.42

recombinant wild-type enzyme, pH 7.5, 25°C

717396

3.4.24.27

0.44

recombinant mutant G117E, pH 7.5, 25°C

717396

3.4.24.27

0.45

pH 7.5, 25°C, recombinant wild-type enzyme

683614

3.4.24.27

0.46

mutant enzyme I168A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

0.48

purified recombinant mutant N116D, pH 7.5, 25°C

734109

3.4.24.27

0.49

purified recombinant mutant N116T, pH 7.5, 25°C

734109

3.4.24.27

0.5

recombinant mutant G117R, pH 7.5, 25°C

717396

3.4.24.27

0.5

mutant enzyme D150E, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

0.52

pH 7.5, 25°C, native enzyme

670784

3.4.24.27

0.52

pH 7.5, 25°C, native wild-type enzyme

683276

3.4.24.27

0.54

mutant enzyme G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

0.55

mutant enzyme S53D/L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

0.57

recombinant mutant G117K, pH 7.5, 25°C

717396

3.4.24.27

0.63

pH 7.5, 25°C, recombinant mutant Q225E

683614

3.4.24.27

0.63

wild type enzyme, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

0.69

mutant enzyme S53D/L155A, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

0.7

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

711866

3.4.24.27

0.8

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

711866

3.4.24.27

0.83

mutant enzyme L155A/G8C/N60C/S65P, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

0.94

mutant enzyme S53D/G8C/N60C/S65P, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

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

711866

3.4.24.27

wild type enzyme, at pH 7.5, at 25°C

711866

3.4.24.27

1.29

mutant enzyme L155A, in the absence of 4 M NaCl, in 40 mM HEPES-NaOH buffer at pH 7.5 containing 10 mM CaCl2, at 25°C

712532

3.4.24.27

1.3

mutant enzyme N227H, 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

2.1

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

711866

3.4.24.27

49 entries

References & Links

Literature References (18)

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Show Reference (18 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

31133

The effect of inhibitors on thermolysin-catalyzed peptide bond synthesis

1986

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

Biochem. Soc. Trans.

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

651789

11726278

Effects of cobalt-substitution of the active zinc ion in thermolysin on its activity and active-site microenvironment

2001

Kuzuya, K.; Inouye, K.

J. Biochem.

130

783-788

668003

15322372

Substrate-dependent activation of thermolysin by salt

2004

Oneda, H.; Muta, Y.; Inouye, K.

Biosci. Biotechnol. Biochem.

1811-1813

668246

Control of hydrolysis and condensation activities of thermolysin by ultrasound irradiation

2005

Kawasaki, T.; Hoshino, Y.; Ishizu, Y.; Mizushiro, Y.; Okahata, Y.

Chem. Lett.

1602-1603

669153

16788052

Engineering of the pH-dependence of thermolysin activity as examined by site-directed mutagenesis of Asn112 located at the active site of thermolysin

2006

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

J. Biochem.

139

1017-1023

670784

16169746

Extracellular production of recombinant thermolysin expressed in Escherichia coli, and its purification and enzymatic characterization

2006

Inouye, K.; Minoda, M.; Takita, T.; Sakurama, H.; Hashida, Y.; Kusano, M.; Yasukawa, K.

Protein Expr. Purif.

248-255

683182

17869197

Improving the activity and stability of thermolysin by site-directed mutagenesis

2007

Yasukawa, K.; Inouye, K.

Biochim. Biophys. Acta

1774

1281-1288

683276

17875473

Engineering, expression, purification, and production of recombinant thermolysin

2007

Inouye, K.; Kusano, M.; Hashida, Y.; Minoda, M.; Yasukawa, K.

Biotechnol. Annu. Rev.

43-64

683614

17405799

Effects of site-directed mutagenesis of the surface residues Gln128 and Gln225 of thermolysin on its catalytic activity

2007

Tatsumi, C.; Hashida, Y.; Yasukawa, K.; Inouye, K.

J. Biochem.

141

835-842

683615

17405798

Kinetic analysis of the activation-and-inhibition dual effects of cobalt ion on thermolysin activity

2007

Hashida, Y.; Inouye, K.

J. Biochem.

141

843-853

684019

17616558

A new method for the extracellular production of recombinant thermolysin by co-expressing the mature sequence and pro-sequence in Escherichia coli

2007

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

Protein Eng. Des. Sel.

375-383

711393

19720529

Lanthanide-based fluorogenic peptide substrate for the highly sensitive detection of thermolysin

2009

Marguerre, A.K.; Kraemer, R.

Bioorg. Med. Chem. Lett.

5757-5759

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.

320-325

712532

20214932

Effects of the mutational combinations on the activity and stability of thermolysin

2010

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

J. Biotechnol.

147

7-16

717396

21150094

Effects of site-directed mutagenesis of the loop residue of the N-terminal domain Gly117 of thermolysin on its catalytic activity

2010

Menach, E.; Yasukawa, K.; Inouye, K.

Biosci. Biotechnol. Biochem.

2457-2462

733524

22153596

A novel and efficient method for the immobilization of thermolysin using sodium chloride salting-in and consecutive microwave irradiation

2012

Chen, F.; Zhang, F.; Du, F.; Wang, A.; Gao, W.; Wang, Q.; Yin, X.; Xie, T.

Biores. Technol.

115

158-163

734109

22648563

Effects of site-directed mutagenesis of Asn116 in the beta-hairpin of the N-terminal domain of thermolysin on its activity and stability

2012

Menach, E.; Yasukawa, K.; Inouye, K.

J. Biochem.

152

231-239

Links to other databases for N-carbobenzoxy-L-Asp-L-Phe methyl ester

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PubChem

Ligand N-carbobenzoxy-L-Asp-L-Phe methyl ester

Basic Ligand Information

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

Substrate in Enzyme-catalyzed Reactions (8 results)

Product in Enzyme-catalyzed Reactions (2 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (45 results)

KM Value (49 results)

References & Links

Literature References (18)

Links to other databases for N-carbobenzoxy-L-Asp-L-Phe methyl ester

k_cat Value (Turnover Number) (45 results)

K_M Value (49 results)