print visible entries

print all entries

Ligand 4-hydroxyphenylacetyl-CoA

Basic Ligand Information

Molecular Structure

close all tables

open all tables

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (3 results)

top print hide

Show Substrate (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.80

(4-hydroxyphenyl)acetyl-CoA + O2 = (4-hydroxyphenyl)glyoxylate + CoA

729199

-

3.1.2.20

4-hydroxyphenylacetyl-CoA + H2O = CoA + 4-hydroxyphenylacetate

690932, 707486

-

3.1.2.B5

4-hydroxyphenylacetyl-CoA + H2O = 4-hydroxyphenylacetate + CoA

727853

-

Product in Enzyme-catalyzed Reactions (5 results)

top print hide

Show Product (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.7.11

4-hydroxyphenylpyruvate + CoA + 2 methyl viologen = (4-hydroxyphenyl)acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+

0

-

1.2.7.7

hydroxyphenylpyruvate + CoA + oxidized ferredoxin = 4-hydroxyphenylacetyl-CoA + CO2 + reduced ferredoxin

0

-

1.2.7.8

4-hydroxyphenylpyruvate + CoA + oxidized ferredoxin = 4-hydroxyphenylacetyl-CoA + CO2 + reduced ferredoxin + H+

0

-

1.2.7.8

p-hydroxyphenylpyruvate + CoA + oxidized ferredoxin = p-hydroxyphenylacetyl-CoA + CO2 + reduced ferredoxin

0

-

1.2.7.8

2 entries

6.2.1.30

ATP + 4-hydroxyphenylacetate + CoA = AMP + diphosphate + 4-hydroxyphenylacetyl-CoA

0

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (9 results)

top print hide

Show Turnover Number (9 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.1.2.20

0.14

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.20

75

-

pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay

690932

3.1.2.B5

0.17

-

pH 8.1, 25°C, mutant enzyme D16A

727853

3.1.2.B5

0.26

-

pH 8.1, 25°C, mutant enzyme H52A

727853

3.1.2.B5

0.31

-

pH 8.1, 25°C, mutant enzyme N46A

727853

3.1.2.B5

3.2

-

pH 8.1, 25°C, mutant enzyme N15A

727853

3.1.2.B5

11

-

pH 8.1, 25°C, wild-type enzyme

727853

3.1.2.B5

19

-

pH 8.1, 25°C, mutant enzyme E14A

727853

3.1.2.B5

79

-

pH 8.1, 25°C, wild-type enzyme

727853

3.1.2.20

2 entries

3.1.2.B5

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

3.1.2.20

0.0076

-

pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay

690932

3.1.2.20

0.049

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.B5

0.018

-

pH 8.1, 25°C, mutant enzyme N15A

727853

3.1.2.B5

0.028

-

pH 8.1, 25°C, mutant enzyme H52A

727853

3.1.2.B5

0.035

-

pH 8.1, 25°C, wild-type enzyme

727853

3.1.2.B5

0.055

-

pH 8.1, 25°C, wild-type enzyme

727853

3.1.2.B5

0.09

-

pH 8.1, 25°C, mutant enzyme E14A

727853

3.1.2.B5

0.25

-

pH 8.1, 25°C, mutant enzyme D16A

727853

3.1.2.B5

0.28

-

pH 8.1, 25°C, mutant enzyme N46A

727853

3.1.2.20

2 entries

3.1.2.B5

7 entries

References & Links

Literature References (4)

top print hide

Show Reference (4 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

690932

18247525

Divergence of function in the hot dog fold enzyme superfamily: the bacterial thioesterase YciA

2008

Zhuang, Z.; Song, F.; Zhao, H.; Li, L.; Cao, J.; Eisenstein, E.; Herzberg, O.; Dunaway-Mariano, D.

Biochemistry

47

2789-2796

707486

19170545

The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis

2009

Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.

Biochemistry

48

1293-1304

727853

16464851

Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI

2006

Song, F.; Zhuang, Z.; Finci, L.; Dunaway-Mariano, D.; Kniewel, R.; Buglino, J.A.; Solorzano, V.; Wu, J.; Lima, C.D.

J. Biol. Chem.

281

11028-11038

729199

18004875

Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC

2007

Fielding, E.N.; Widboom, P.F.; Bruner, S.D.

Biochemistry

46

13994-4000

Links to other databases for 4-hydroxyphenylacetyl-CoA

top print hide

Show Links (1 entry)

ChEBI

PubChem

-