print visible entries

print all entries

Ligand 4-nitrophenylalanine

Basic Ligand Information

Molecular Structure

close all tables

open all tables

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (6 results)

top print hide

Show Substrate (6 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.1.20

4-nitro-L-phenylalanine + H2O + NAD+ = 4-nitro-phenylpyruvate + NH3 + NADH

686436

-

1.4.3.2

L-4-nitrophenylalanine + H2O + O2 = (4-nitrophenyl)pyruvate + NH3 + H2O2

651026

-

3.5.1.11

4-nitro-L-phenylalanine + phenylacetamide = N-[(4-nitrophenyl)acetyl]-L-tyrosine + NH3

721069

-

4.3.1.24

(2S)-2-amino-3-(4-nitrophenyl)propanoic acid = (2E)-3-(4-nitrophenyl)prop-2-enoic acid + NH3

729395

-

4.3.1.24

4-nitro-L-phenylalanine = 4-nitro-(E)-cinnamate + NH3

716820

-

4.3.1.24

2 entries

5.4.3.11

4-nitro-L-phenylalanine = (S)-3-amino-3-(4-nitrophenyl)propanoic acid

746575

-

Product in Enzyme-catalyzed Reactions (50 results)

top print hide

Show Product (50 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.99.67

L-4-aminophenylalanine + reduced phenazine methosulfate + 2 O2 = L-4-nitrophenylalanine + phenazine methosulfate + 2 H2O

0

-

1.4.1.20

4-nitro-phenylpyruvate + NH3 + NADH = 4-nitro-L-phenylalanine + H2O + NAD+

0

-

3.4.11.9

(4-nitro)Phe-Pro-HN-CH2-CH2-NH-o-aminobenzoyl + H2O = (4-nitro)Phe + Pro-HN-CH2-CH2-NH-o-aminobenzoyl

36052

-

3.4.11.9

(4-nitro)Phe-Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl + H2O = (4-nitro)Phe + Pro-Pro-HN-CH2-CH2-NH-o-aminobenzoyl

36052

-

3.4.18.1

2-aminobenzoyl-Ala-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Ala-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Arg-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Arg-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Asn-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Asn-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Asp-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Asp-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Cys-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Cys-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Gln-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Gln-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Glu-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Glu-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Gly-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Gly-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-His-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-His-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Ile-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Ile-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Leu-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Leu-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Lys-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Lys-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Met-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Met-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Ala-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Ala + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Asn-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Asn + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Asp-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Asp + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Cys-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Cys + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Gln-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Gln + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Glu-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Glu + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Gly-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Gly + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-His-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-His + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Ile-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Ile + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Leu-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Leu + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Lys-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Lys + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Met-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Met + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Phe-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Phe + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Ser-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Ser + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Thr-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Thr + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Trp-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Trp + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Tyr-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Tyr + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Phe-Val-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Phe-Val + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Pro-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Pro-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Ser-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Ser-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Thr-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Thr-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Trp-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Trp-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Tyr-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Tyr-Arg + 4-nitrophenylalanine

0

-

3.4.18.1

2-aminobenzoyl-Val-Arg-4-nitrophenylalanine + H2O = 2-aminobenzoyl-Val-Arg + 4-nitrophenylalanine

0

-

3.4.21.26

Abz-Ala-Ala-Pro-4-nitrophenylalanine + H2O = Abz-Ala-Ala-Pro + 4-nitrophenylalanine

0

-

3.4.21.26

Abz-Gly-Gly-Pro-4-nitrophenylalanine + H2O = Abz-Gly-Gly-Pro + 4-nitrophenylalanine

0

-

3.4.21.26

Abz-Gly-Pro-4-nitrophenylalanine + H2O = Abz-Gly-Pro + 4-nitrophenylalanine

0

-

3.4.21.26

Abz-Lys-Pro-4-nitrophenylalanine + H2O = Abz-Lys-Pro + 4-nitrophenylalanine

0

-

3.4.11.9

2 entries

3.4.18.1

38 entries

3.4.21.26

4 entries

3.4.23.20

(4-Nitro)Phe-Nle-Ala-Leu methyl ester + H2O = Nle-Ala-Leu methyl ester + (4-nitro)Phe

30603

-

4.3.1.24

(2E)-3-nitro-cinnamic acid + NH3 = 4-nitro-L-phenylalanine

0

-

4.3.1.24

(2E)-4-nitro-cinnamic acid + NH3 = 4-nitro-L-phenylalanine

0

-

4.3.1.24

4-nitro-trans-cinnamate + NH3 = 4-nitro-L-phenylalanine

0

-

4.3.1.24

3 entries

Inhibitor in Enzyme-catalyzed Reactions (1 result)

top print hide

Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.4.22.1

inactivation rate is 3.0 mM/min

753558

-

3D Structure of Enzyme-Ligand-Complex (PDB) (22 results)

top print hide

Show 3D Structure of Enzyme-Ligand-Complex (PDB) (22 entries)

EC NUMBER

ENZYME 3D STRUCTURE

2.4.99.19

5ogl, 3D-view

2.4.99.19

6gxc, 3D-view

2.4.99.19

5ogl, 3D-view

2.4.99.19

6gxc, 3D-view

2.4.99.19

5ogl, 3D-view

2.4.99.19

6gxc, 3D-view

2.4.99.19

5ogl, 3D-view

2.4.99.19

6gxc, 3D-view

2.4.99.19

5ogl, 3D-view

2.4.99.19

6gxc, 3D-view

2.4.99.19

10 entries

2.7.10.2

5bmm, 3D-view

3.2.1.8

7xna, 3D-view

3.4.23.16

1ytj, 3D-view

3.4.23.16

2whh, 3D-view

3.4.23.16

1ytj, 3D-view

3.4.23.16

2whh, 3D-view

3.4.23.16

1ytj, 3D-view

3.4.23.16

2whh, 3D-view

3.4.23.16

1ytj, 3D-view

3.4.23.16

2whh, 3D-view

3.4.23.16

1ytj, 3D-view

3.4.23.16

2whh, 3D-view

3.4.23.16

10 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (2 results)

top print hide

Show Turnover Number (2 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

4.3.1.24

1.08

-

pH 8.3, 30°C

729395

5.4.3.11

0.038

-

pH 8.0, 31°C, recombinant enzyme

746575

K_M Value (4 results)

top print hide

Show KM Value (4 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

4.3.1.24

0.23

-

pH 8.3, 30°C

729395

4.3.1.24

2

-

wild-type, pH 10, 30°C

716820

4.3.1.24

2.2

-

mutant F137V, pH 10, 30°C

716820

4.3.1.24

3 entries

5.4.3.11

0.752

-

pH 8.0, 31°C, recombinant enzyme

746575

References & Links

Literature References (9)

top print hide

Show Reference (9 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

30603

393302

Further characterization of the Penicillium roqueforti acid protease

1979

Houmard, J.; Raymond, M.N.

Biochimie

61

979-982

36052

6749499

Fluorogenic substrates for bacterial aminopeptidase P and its analogs detected in human serum and calf lung

1982

Fleminger, G.; Carmel, A.; Goldenberg, D.; Yaron, A.

Eur. J. Biochem.

125

609-615

651026

-

A new bacterial L-amino acid oxidase with a broad substrate specificity: purification and characterization

2002

Geueke, B.; Hummel, W.

Enzyme Microb. Technol.

31

77-87

686436

-

An engineered mutant, L307V of phenylalanine dehydrogenase from Bacillus sphaericus: high activity and stability in organic-aqueous solvent mixtures and utility for synthesis of non-natural L-amino acids

2007

Chen, S.; Engel, P.C.

Enzyme Microb. Technol.

40

1407-1411

716820

21036782

Mutational analysis of phenylalanine ammonia lyase to improve reactions rates for various substrates

2010

Bartsch, S.; Bornscheuer, U.

Protein Eng. Des. Sel.

23

929-933

721069

-

Alcaligenes faecalis penicillin G acylase-catalyzed enantioselective acylation of dl-phenylalanine and derivatives in aqueous medium

2011

Gong, X.; Su, E.; Wang, P.; Wei, D.

Tetrahedron Lett.

52

5398-5402

729395

25037641

Bacterial Anabaena variabilis phenylalanine ammonia lyase: A biocatalyst with broad substrate specificity

2014

Lovelock, S.; Turner, N.

Bioorg. Med. Chem.

22

5555-5557

746575

-

Ring-substituted beta-arylalanines for probing substituent effects on the isomerization reaction catalyzed by an aminomutase

2014

Ratnayake, N.; Liu, N.; Kuhn, L.; Walker, K.

ACS Catal.

4

3077-3090

753558

-

Active center differences between cathepsins L and B the S, binding region

1988

Kirschke, H.; Wikstrom, P.; Shaw, E.

FEBS Lett.

228

128-130

Links to other databases for 4-nitrophenylalanine

top print hide

Show Links (1 entry)

ChEBI

PubChem

-