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Ligand 3,5-dihydroxyphenylacetyl-CoA

Basic Ligand Information

Molecular Structure

Related pathways

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.80

(3,5-dihydroxyphenyl)acetyl-CoA + O2 = (3,5-dihydroxyphenyl)glyoxylate + CoA

730462, 729199, 729572

-

1.13.11.80

(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA

763838

-

1.13.11.80

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.246

4 malonyl-CoA = (3,5-dihydroxyphenylacetyl)-CoA + 3 CoA + 4 CO2 + H2O

-

-

2.3.1.246

4 malonyl-CoA = 3,5-dihydroxyphenylacetyl-CoA + 3 CoA + 4 CO2 + H2O

-

-

2.3.1.246

2 entries

Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Substrate (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.80

(3,5-dihydroxyphenyl)acetyl-CoA + O2 = (3,5-dihydroxyphenyl)glyoxylate + CoA

730462, 729199, 729572, 730839

-

1.13.11.80

(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA

763838

-

1.13.11.80

2 entries

3.1.2.20

3,5-dihydroxyphenylacetyl-CoA + H2O = CoA + 3,5-dihydroxyphenylacetate

707486

-

3.1.2.B5

3,5-dihydroxyphenylacetyl-CoA + H2O = 3,5-dihydroxyphenylacetate + CoA

727853

-

Product in Enzyme-catalyzed Reactions (2 results)

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Show Product (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.246

4 malonyl-CoA = (3,5-dihydroxyphenylacetyl)-CoA + 3 CoA + 4 CO2 + H2O

-

-

2.3.1.246

4 malonyl-CoA = 3,5-dihydroxyphenylacetyl-CoA + 3 CoA + 4 CO2 + H2O

-

-

2.3.1.246

2 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (14 results)

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Show Turnover Number (14 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.13.11.80

0.019

-

pH 7.4, 24°C

730462

1.13.11.80

0.037

-

pH 7.4, 24°C

730462

1.13.11.80

0.05

-

pH 7.4, 24°C

730462

1.13.11.80

0.069

-

pH 7.5, 24°C, mutant enzyme Q299N

729199

1.13.11.80

0.085

-

pH 7.5, 24°C, mutant enzyme E189Q

729199

1.13.11.80

0.086

-

pH 7.5, 24°C, mutant enzyme R254K

729199

1.13.11.80

0.095

-

mutant enzyme A319C, at pH 7.5 and 24°C

763838

1.13.11.80

0.153

-

pH 7.5, 24°C, mutant enzyme E255Q

729199

1.13.11.80

0.17

-

pH 7.5, 24°C

730839

1.13.11.80

0.172

-

pH 7.4, 24°C

730462

1.13.11.80

0.172

-

pH 7.5, 24°C, wild-type enzyme

729199

1.13.11.80

11 entries

3.1.2.20

0.19

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.B5

2.3

-

pH 8.1, 25°C, wild-type enzyme

727853

3.1.2.B5

9

-

pH 8.1, 25°C, wild-type enzyme

727853

3.1.2.B5

2 entries

K_M Value (14 results)

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Show KM Value (14 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.80

0.0025

-

pH 7.5, 24°C, mutant enzyme Q299N

729199

1.13.11.80

0.0036

-

pH 7.5, 24°C, mutant enzyme E255Q

729199

1.13.11.80

0.0039

-

pH 7.4, 24°C

730462

1.13.11.80

0.0039

-

pH 7.5, 24°C, wild-type enzyme

729199

1.13.11.80

0.006

-

pH 7.5, 24°C

730839

1.13.11.80

0.0138

-

pH 7.4, 24°C

730462

1.13.11.80

0.0147

-

pH 7.4, 24°C

730462

1.13.11.80

0.058

-

pH 7.4, 24°C

730462

1.13.11.80

0.064

-

pH 7.5, 24°C, mutant enzyme E189Q

729199

1.13.11.80

0.125

-

mutant enzyme A319C, at pH 7.5 and 24°C

763838

1.13.11.80

0.217

-

pH 7.5, 24°C, mutant enzyme R254K

729199

1.13.11.80

11 entries

3.1.2.20

0.025

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.B5

0.028

-

pH 8.1, 25°C, wild-type enzyme

727853

3.1.2.B5

0.2

-

pH 8.1, 25°C, wild-type enzyme

727853

3.1.2.B5

2 entries

References & Links

Literature References (7)

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Show Reference (7 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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

729572

15380180

DpgC is a metal- and cofactor-free 3,5-dihydroxyphenylacetyl-CoA 1,2-dioxygenase in the vancomycin biosynthetic pathway

2004

Tseng, C.C.; Vaillancourt, F.H.; Bruner, S.D.; Walsh, C.T.

Chem. Biol.

11

1195-1203

730462

17507985

Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis

2007

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

Nature

447

342-345

730839

11752437

Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine

2001

Chen, H.; Tseng, C.C.; Hubbard, B.K.; Walsh, C.T.

Proc. Natl. Acad. Sci. USA

98

14901-14906

763838

28695857

Probing the structural basis of oxygen binding in a cofactor-independent dioxygenase

2017

Li, K.; Fielding, E.N.; Condurso, H.L.; Bruner, S.D.

Acta Crystallogr. Sect. D

73

573-580

Links to other databases for 3,5-dihydroxyphenylacetyl-CoA

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Show Links (1 entry)