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Ligand 3-phenylpropionamide

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Substrate (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.4

3-phenyl-propionamide + H2O = 3-phenyl-propionate + NH3

711039

-

3.5.1.4

3-phenylpropionamide + H2O = 3-phenylpropionate + NH3

719432, 724144

-

3.5.1.86

3-phenylpropionamide + H2O = 3-phenylpropionate + NH3

680440

-

3.5.1.86

3-phenylpropionamide + H2O = ?

650254

-

3.5.1.4

2 entries

3.5.1.86

2 entries

Product in Enzyme-catalyzed Reactions (2 results)

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Show Product (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.2.1.84

3-phenylpropanenitrile + H2O = 3-phenylpropanamide

-

-

4.2.1.84

3-phenylpropionitrile + H2O = 3-phenylpropionamide

-

-

4.2.1.84

2 entries

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.4.21.62

-

29470

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (4 results)

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Show Turnover Number (4 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.5.1.4

7.1

-

pH 7.5, 70°C

719432

3.5.1.4

12.82

-

pH 5.0, 70°C, wild-type enzyme

711039

3.5.1.4

15.3

-

pH 5.0, 70°C, wild-type enzyme

724144

3.5.1.4

18

-

pH 5.0, 70°C, mutant enzyme Y41C

724144

3.5.1.4

4 entries

K_M Value (5 results)

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Show KM Value (5 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.5.1.4

2.325

-

pH 5.0, 70°C, wild-type enzyme

711039

3.5.1.4

2.5

-

pH 5.0, 70°C, mutant enzyme Y41C

724144

3.5.1.4

3

-

pH 5.0, 70°C, wild-type enzyme

724144

3.5.1.4

4

-

pH 7.5, 70°C

719432

3.5.1.4

4 entries

3.5.1.86

0.049

-

pH 7.5, 30°C

650254

References & Links

Literature References (6)

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Show Reference (6 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

29470

4364061

Inhibition of subtilisin by boronic acids, potential analogs of tetrahedral reaction intermediates

1974

Lindquist, R.N.; Terry, C.

Arch. Biochem. Biophys.

160

135-144

650254

15196015

Mandelamide hydrolase from Pseudomonas putida: characterization of a new member of the amidase signature family

2004

Gopalakrishna, K.N.; Stewart, B.H.; Kneen, M.M.; Andricopulo, A.D.; Kenyon, G.L.; McLeish, M.J.

Biochemistry

43

7725-7735

680440

12670968

Identification and characterization of a mandelamide hydrolase and an NAD(P)+dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633

2003

McLeish, M.J.; Kneen, M.M.; Gopalakrishna, K.N.; Koo, C.W.; Babbitt, P.C.; Gerlt, J.A.; Kenyon, G.L.

J. Bacteriol.

185

2451-2456

711039

19478917

pH-, temperature- and ion-dependent oligomerization of Sulfolobus solfataricus recombinant amidase: a study with site-specific mutants

2009

Politi, L.; Chiancone, E.; Giangiacomo, L.; Cervoni, L.; Scotto dAbusco, A.; Scorsino, S.; Scandurra, R.

Archaea

2

221-231

719432

11453462

Molecular and biochemical characterization of the recombinant amidase from hyperthermophilic archaeon Sulfolobus solfataricus

2001

dAbusco, A.S.; Ammendola, S.; Scandurra, R.; Politi, L.

Extremophiles

5

183-192

724144

16243781

Oligomerization of Sulfolobus solfataricus signature amidase is promoted by acidic pH and high temperature

2005

D'Abusco, A.S.; Casadio, R.; Tasco, G.; Giangiacomo, L.; Giartosio, A.; Calamia, V.; Di Marco, S.; Chiaraluce, R.; Consalvi, V.; Scandurra, R.; Politi, L.

Archaea

1

411-423

Links to other databases for 3-phenylpropionamide

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Show Links (1 entry)

ChEBI

PubChem

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